Mesenchymal Cell Growth Factors

Antoniades, H. and Owen, A.J., Growth factors and regulation of cell growth, Annu. Rev. Med., 33, 445, 1982.

Ross, R., Raines, E.W., and Bowen-Pope, F., The biology of platelet-derived growth factor, Cell, 46, 155, 1986.

Stiles, C.D., The molecular biology of platelet-derived growth factor, Cell. 33, 653, 1983.

Heldin, C.H., Hammacher, A., Nister, M., and Westermark, B., Structural and functional aspects of platelet-derived growth factor, Br. J. Cancer, 57, 591, 1988.

Ross, R., Glomset, J.A., Kariya, B., and Harber, L., A platelet-dependent serum factor that stimulates proliferation of arterial smooth muscle cells in vitro, Proc. Natl. Acad. Sci. U.S.A., 71, 1207, 1974.

Kohler, A. and Lipton, A., Platelets as a source of fibroblast growth-promoting activity, Exp. Cell Res., 87, 297, 1974.

Antoniades, H.N., Human platelet-derived growth factor (PDGF): purification of PDGF-I and PDGF-II and separation of their reduced subunits, Proc. Natl. Acad. Sci. U.S.A., 78, 7314, 1981.

Raines, E.W. and Ross, R., Platelet-derived growth factor. I. High yield purificaiton and evidence for multiple forms, J. Biol. Chem., 257, 5154, 1982.

Heldin, C.H., Westermark, B., and Wasterson, A., Platelet-derived growth factor: isolation by a large-scale procedure and analysis of subunit composition, Biochem. J., 193, 907, 1981.

Deuel, T.F., Huang, J.S., Proffit, R.T., Baenziger, J.U., Chang, D., and Kennedy, B.B., Human platelet-derived growth factor-purification and resolution into two active protein fractions, J. Biol. Chem., 256, 8896, 1981.

Antoniades, H.N. and Hunkapiller, M.W., Human platelet-derived growth factor (PDGF): amino terminal amino acid sequence, Science, 220, 963, 1983.

Betsholtz, C., Johnsson, A., Heldin, C.H., Westermark, B., Lind Urdea, M.S., Eddy, R., Shows, T.B., Philpott, K., Mellor, A.L., Knott, T.J., and Scott, J., cDNA sequence and chromosomal localization of human platelet-derived growth factor A-chain and its expression in tumour cell lines, Nature, 320, 695, 1986.

Waterfield, M.D., Scrace, G.T., Whittle, N., Stroobant, P., Johnsson, A., Wasterson, A., Westermark, B., Heldin, C.H., Huang, S., and Deuel, T.F., Platelet-derived growth factor is structurally related to the putative transforming protein p28sis of simian sarcoma virus, Nature, 304, 35, 1983.

Hammacher, A., Hellman, U., Johnsson, A., Ostman, A., Gunnarrsson, K., Westermark, B., Wasterson, A., and Heldin, C.H., A major part of PDGF purified from human platelets is a heterodimer of one A and one B chain, J. Biol. Chem., 263, 16493, 1988.

Stroobant, P. and Waterfield, M.D., Purification and properties of porcine platelet-derived growth factor, EMBO J., 3, 2963, 1984.

Nister, M., Hammacher, A., Mellstrom, K., Siegbahn, A., Ronnstrand, A., Westermark, B., and Heldin, C.H., A glioma-derived PDGF A chain homodimer has different functional activities than a PDGF-AB heterodimer from human platelets, Cell, 52, 791, 1988.

Kazlauskas, A., Bowen-Pope, D., Seifert, R., Hart, C.E., and Cooper, J.A., Different effects of homo- and heterodimers of platelet-derived growth factor A and B chains on human and mouse fibroblasts, EMBO J., 7, 3727, 1988.

Heldin, C.H., Backstrom, G., Ostman, A., Hammacher, A., Ronnstrand, A., Rubin, K., Nister, M., and Westermark, B., Binding of different dimeric forms of PDGF to human fibroblasts: evidence for two separate receptor types, EMBO J., 7, 1387, 1988.

Hart, C.E., Frostrom, J.W., Kelly, J.D., Seifert, R.A., Smith, R.A., Ross, R., Murray, M.J., and Bowen-Pope, D.F., Two classes of PDGF receptor recognize different isoforms of PDGF, Science, 240, 1529, 1988.

Graves, D.T., Antoniades, H.N., Williams, S.R., and Owen, A.J., Evidence for functional platelet-derived growth factor receptors on MG-63 human osteosarcoma cells, Cancer Res., 44, 2966, 1984.

Piche, J.E. and Graves, D.T., Study of the growth factor requirements of human bone-derived cells, Bone, 10, 131, 1989.

Piche, J.E., Carnes, D.L., and Graves, D.T., Initial characterization of cells derived from human periodontia, J. Dent. Res., in press.

Bowen-Pope, D. and Ross, R., Platelet-derived growth factor. II. Specific binding to cultured cells., J. Biol. Chem., 257, 5161, 1982.

Frackelton, J.A.R., Tremble, P.M., and Williams, L.T., Evidence for the platelet-derived growth factor-stimulated tyrosine phosphorylation of the platlet-derived growth factor receptor in vivo. Immunopurification using a monoclonal antibody to phosphotyrosine, J. Biol. Chem., 259, 7909, 1984.

Yarden, Y., Escobedo, J.A., Kuang, W.J. et al., Structure of the receptor for platelet-derived growth factor helps define a family of closely related growth factor receptors, Nature, 323, 226, 1986.

Gronwald, R.T., Grant, F.J., Hademan, B.A., Hart, C.E., O'Hara, A.J., Hagen, F.S., Ross, R., Bowen-Pope, D.F., and Murray, M.J., Cloning and expression of a cDNA coding for the human platelet-derived growth factor receptor: evidence for more than one receptor class, Proc. Natl. Acad. Sci. U.S.A., 85, 3435, 1988.

Claesson-Welsh, L., Eriksson, A., Moren, A., Severinsson, L., Ek, B., Ostman, A., Betsholtz, C., and Heldin, C.H., cDNA cloning and expression of a human platelet-derived growth factor (PDGF) receptor specific for B-chain-containing PDGF molecules, Mol. Cell. Biol., 8, 3476, 1988.

Matsui, T., Heidaran, M., Miki, T., Popescu, N., Rochelle, W.L., Kraus, M., Pierce, J., and Aaronson, S., Isolation of a novel receptor cDNA establishes the existence of two PDGF receptor genes, Science, 243, 800, 1989.

Hunter, T., A thousand and one protein kinases, Cell, 50, 823, 1987.

Ek, B., Westermark, B., Wasterson, A., and Heldin, C.H., Stimulation of tyrosine-specific phosphorylation by platelet-derived growth factor, Nature, 295, 419, 1982.

Pike, L.J., Bowen-Pope, D.F., Ross, R., and Krebs, E.G., Characterization of platelet derived growth factor-stimulated phosphorylation in cell membranes, J. Biol. Chem., 258, 9383, 1983.

Habenicht, A.J., Glomset, J.A., King, W.C., Nist, C., Mitchell, A.D., and Ross, R., Early changes in phosphatidylinsoitol and acrachidonic acid metabolism in quiescent Swiss 3T3 cells stimulated to divide by platelet-derived growth factor, J. Biol. Chem., 256, 12329, 1981.

Nishizuka, Y., The role of protein kinase C in cell surface signal transduction and tumor promotion, Nature, 308, 693, 1984.

Kruijer, W., Cooper, J.A., Hunter, T., and Verma, I.M., Platelet-derived growth factor induced rapid but transient expression of the c-fos gene and protein, Nature, 312, 711, 1984.

Muller, R., Bravo, R., Burskhardt, J., and Curran, T., Induction of c-fos gene and protein by growth factors precedes activation of c-myc, Nature, 312, 716, 1984.

Kelly, K., Cochran, B.H., Stiles, C.D., and Leder, P., Cell specific regulation of the c-myc gene by lymphocyte mitogens and platelet-derived growth factor, Cell, 35, 607, 1983.

Erikson, R.L., Regulation of cell proliferation by oncogene products and growth factors, Som. Cell Mol. Gen., 13, 459, 1987.

Pledger, W.J., Stiles, C.D., Antoniades, H.N., and Scher, D., Induction of DNA synthesis in Balb/c-3T3 cells by serum components: reevaluation of the commitment process, Proc. Natl. Acad. Sci. U.S.A., 74,4481, 1977.

Clemmons, D.R., Underwood, L.E., and Van Wyk, J.J., Hormonal control of immunoreactive somatomedin production by cultured human fibroblasts, J. Clin. Invest., 67, 10, 1981.

Clemmons, D.R. and Van Wyk, J.J., Evidence for a functional role of endogenously produced somatomedin-like peptides in the regulation of DNA synthesis in cultured human fibroblasts and procine smooth muscle cells, J. Clin. Invest., 75, 1914, 1985.

Theilen, G.J., Gould, D., Fowler, M., and Dung worth, D.L., C-type virus in tumor tissue of a woolly monkey (Lagothrix spp.) with fibrosarcoma, J. Natl. Cancer Inst., 47, 881, 1971.

Robbins, K.C., Devare, S.G., and Aaronson, S.A., Molecular cloning of integrated simian sarcoma virus: genome organization of infectious DNA clones, Proc. Natl. Acad. Sci. U.S.A., 78, 2918, 1981.

Owen, A.J., Pantazis, P., and Antoniades, H.N., Simian Sarcoma virus-transformed cells secrete a mitogen identical to platelet-derived growth factor, Science, 225, 54, 1984.

Deuel, T.F., Huang, J.S., Huang, S.S., and Waterfield, A.D., Expression of a PDGF-like protein in simian sarcoma virus-transformed cells, Science, 221, 1348, 1983.

Johnsson, A., Heldin, C.-H., Wasterson, A., Westermark, B., Deuel, A.F., Huang, J.S., Seeburg, P.H., Gray, A., Ullrich, A., Scrace, G., Stroobant, P., and Waterfield, M.D., The c-sis gene encodes a precursor of the B-chain of platelet-derived growth factor, EMBO J., 3,921, 1984.

Doolittle, R.F., Hunkapiller, M.W., Hood, L.E., DeVare, S.G., Robbins, K.C., Aaronson, S.A., and Antoniades, H.N., Simian sarcoma virus onc gene, v-sis, is derived from the gene (or genes) encoding a platelet-derived growth factor, Science, 221, 275, 1983.

Leal, F., Williams, L.T., Robbins, K.C., and Aaronson, S.A., Evidence that the v-sis gene product transforms by interaction with the receptor for platelet-derived growth factor, Science, 320, 327, 1985.

Sporn, M.B. and Todaro, G.J., Autocrine secretion and malignant transformation of cells, N. Engl. J. Med., 303, 878, 1980.

Keating, M.T. and Williams, L.T., Autocrine stimulation of intracellular PDGF receptors in v-sis transformed cells, Science, 239, 914, 1988.

Huang, S.S. and Huang, J.S., Rapid turnover of the platelet-derived growth factor receptor in sis-transformed cells and reversal by suramin, J. Biol. Chem., 263, 12608, 1988.

Heldin, C.-H., Westermark, B., and Wasterson, A., Chemical and biological properties of a growth factor from human-cultured osteosarcoma cells: resemblance with platelet-derived growth factor, J. Cell. Physiol., 105, 35, 1980.

Graves, D.T., Owen, A.J., and Antoniades, H.N., Evidence that a human osteosarcoma cell line which secretes a mitogen similar to platelet-derived growth factor requires growth factors present in platelet-poor plasma, Cancer Res., 43, 83, 1983.

Graves, D.T., Owen, A.J., Varth, R.K., Tempst, P., Winoto, A., Fors, A., Hood, L.E., and Antoniades, H.N., Detection of c-sis transcripts and synthesis of PDGF-like proteins by human osteosarcoma cells, Science, 226, 972, 1984.

Nister, M., Heldin, C.H., Wasterson, A., and Westermark, B., A glioma derived analog to platelet-derived growth factor: demonstration of receptor competing activity and immunological cross reactivity, Proc. Natl. Acad. Sci. U.S.A., 81, 926, 1984.

Pantazis, P., Pelicci, P.G., Dalla-Favera, R., and Antoniades, H.N., Synthesis and secretion of proteins resembling platelet-derived growth factor by human glioblastoma and fibrosarcoma cells in culture, Proc. Natl. Acad. Sci. U.S.A., 82, 2404, 1985.

Rozengurt, E., Sinnett-Smith, J., and Tylor-Papadimitriou, J., Production of PDGF-like growth factor by breast cancer cell lines, Int. J. Cancer, 36, 247, 1985.

Richter, M.R. and Graves, D.T., DNA synthesis in U-2 OS human osteosarcoma cells is independent of PDGF binding to functional PDGF cell surface receptors, J. Cell. Physiol., 137, 263, 1988.

DiCorleto, P.E. and Bowen-Pope, D.F., Cultured endothelial cells produce a platelet-derived growth factor-like protein, Proc. Natl. Acad. Sci. U.S.A., 80, 1919, 1983.

Deuel, T.F., Senior, R.M., Huang, J.S., and Griffin, G.L., Chemotaxis of monocytes and neutrophils to platelet-derived growth factor, J. Clin. Invest., 69, 1046, 1982.

Williams, L.T., Antoniades, H.N., and Goetzl, E.J., Platelet-derived growth factor stimulates mouse 3T3 cell mitogenesis and leukocyte chemotaxis through different structural determinants, J. Clin. Invest., 72, 1759, 1983.

Graves, D.T., Grotendorst, G.R., Antoniades, H.N., Schwartz, C., and Valente, A.J., Platelet-derived growth factor is not chemotactic for human peripheral blood monocytes, Exp. Cell Res., 180, 497, 1989.

Shimokado, K., Raines, E.W., Madtes, D.K., Barrett, T.B., Benditt, A.P., and Ross, R., A significant part of macrophage-derived growth factor consists of at least two forms of PDGF, Cell, 43, 277, 1985.

Martint, Y., Bitterman, P.B., Mornex, J.-A., Grotendorst, G.R., Martin, G.R., and Crystal, R.G., Activated human monocytes express the c-sis proto-oncogene and release a mediator showing PDGF-like activity, Nature, 319, 158, 1986.

Leibovich, S.J. and Ross, R., A macrophage-dependent factor that stimulates the proliferation of fibroblasts in vitro, Am. J. Pathol., 84, 501, 1976.

Goustin, A.S., Betsholtz, C., Pfeifer-Ohlsson, S. et al. Coexpression of the sis and myc proto-oncogenes in human placenta suggest autocrine control of the trophoblast growth, Cell, 41, 301, 1985.

Seifert, R.A., Schwartz, S.M., and Bowen-Pope, D.F., Developmentally regulated production of platelet-derived growth factor-like molecules, Nature, 311, 669, 1984.

Nilsson, J., Sjolund, M., Palmberg, L., Thyberg, J., and Heldin, C.H., Arterial smooth muscle cells in primary culture produce a platelet-derived growth factor-like protein, Proc. Natl. Acad. Sci. U.S.A., 82, 4418, 1985.

Valente, A.J., Delgado, R., Metter, J.D., Cho, C., Sprague, E.A., Schwartz, C.J., and Graves, D.T., Cultured primate aortic smooth muscle cells express both the PDGF-A and PDGF-B genes but do not secrete a mitogenic platelet-derived growth factor-like protein, J. Cell. Physiol., 135, 474, 1988.

Graves, D.T., Valentin-Opran, A., Delgado, R., Valente, A.J., Mundy, G., and Piche, J.E., Platelet-derived growth factor as an autocrine and paracrine factor for bone cells, Conn. Tissue Res., in press.

Grotendorst, G.R., Grotendorst, C.A., and Gilman, T., Production of growth factors (PDGF and TGF-B) at the site of tissue repair, in Growth Factors and Other Aspects of Wound Healing, Alan R. Liss, New York, 1988.

Grotendorst, G.R., Can collagen metabolism be controlled?, Front. Understanding Burn Injury, 24, S49, 1984.

Sprugel, K.H., McPherson, J.M., Clowes, A.W., and Ross, R., The effects of different growth factors in subcutaneous wound chambers, in Growth Factors and Other Aspects of Wound Healing, Alan R. Liss, New York, 1988, 77.

Lynch, S.E., Nixon, J.C., Covlin, R.B., and Antoniades, H.N., Role of platelet-derived growth factor in wound healing: synergistic effects with other growth factors, Proc. Natl. Acad. Sci. U.S.A., 84, 7696, 1987.

Gospodarowicz, D., Localization of a fibroblast growth factor and its effect alone and with hydrocortisone on 3T3 cell growth, Nature, 249, 123, 1974.

Gospodarowicz, D. and Moran, J., Effect of a fibroblast growth factor, insulin, dexamethasone and serum on morphology of BALB/ c-3T3 cells, Proc. Natl. Acad. Sci. U.S.A., 71, 4648, 1974.

Maciag, R., Cerundolo, J., Isley, S., Kelly, P.R., and Forand, R., An endothelial cell growth factor from bovine hypothalamus: identification and partial characterization, Proc. Natl. Acad. Sci. U.S.A., 76, 5674, 1979.

Gospodarowicz, D., Bialecki, H., and Thakral, T.K., The angiogenic activity of the fibroblast and epidermal growth factor, Exp. Eye Res., 28, 501, 1979.

Gospodarowicz, D., in Methods in Molecular and Cell Biology, Vol. 1, Alan R. Liss, New York, 1984, 275.

Thomas, K.A., Rios-Candelore, M., and Fitzpatrick, S., Purification and characterization of acidic fibroblast growth factor from bovine brain, Proc. Natl. Acad. Sci. U.S.A., 81, 357, 1984.

Esch, F., Baird, A., Ling, N., Ueno, N., Hill, F., Deneroy, L., Klepper, R., Gospodarowicz, D., Bohlen, P., and Guillemin, R., Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF, Proc. Natl. Acad. Sci. U.S.A., 85, 6507, 1985.

Gospodarowicz, D., Massoglia, S., Cheng, J., Lui, G.M., and Bohlen, P., Isolation of pituitary fibroblast growth factor by fast protein liquid chromatography (FPLC): partial chemical and biological characterization, J. Cell. Physiol., 122, 323, 1985.

Esch, F., Ueno, N., Baird, A., Hill, F., Deneroy, L., Ling, N., Gospodarowicz, D., and Guillemin, R., Primary structure of bovine brain acidic fibroblast growth factor (FGF), Biochem. Biophys. Res. Commun., 133, 554, 1985.

Gimenez-Gallego, G., Rodkey, J., Bennett, C., Rios Candelore, M., Disalvo, J., and Thomas, K., Brain-derived acidic fibroblast growth factor: complete amino acid sequence and homologies, Science, 230, 1385, 1985.

Lobb, R.R. and Fett, J.W., Purification of two distinct growth factors from bovine neural tissue by heparin affinity chromatography, Biochemistry, 23, 6295, 1984.

Hauschka, P.V., Mavrakas, A.E., Iafrati, M.D., Doleman, S.E., and Klagsburn, N., Growth factors in bone matrix: isolation of multiple types by affinity chromatography on heparin-sepharose, J. Biol. Chem., 261, 12665, 1986.

Baird, A., Esch, F., Gospodarowicz, D., and Guillemin, R., Retina-and eye-derived endothelial cell growth factors: partial molecular characterization and identity with acidic and basic fibroblast growth factors, Biochemistry, 24, 7855, 1985.

Bohlen, P., Esch, F., Baird, A., and Gospodarowicz, D., Acidic fibroblast growth factor (PFGF) from bovine brain: amino-terminal sequence and comparison with basic FGF, EMBO J., 4, 1951, 1985.

Gospodarowicz, D. and Cheng, J., Heparin protects basic and acidic FGF from inactivation, J. Cell. Physiol., 128, 475, 1986.

Roberts, A.B., Anzano, M.A., Wakefield, L.M., Roche, N.S., Stern, A.F., and Sporn, M.B., Type beta transforming growth factor: a bifunctional regulator of cellular growth. Proc. Natl. Acad. Sci. U.S.A., 82, 119, 1985.

Klagsbrun, M., Sasse, J., Sullivan, R., and Smith, J.A., Human tumor cells synthesize an endothelial cell growth factor that is structurally related to basic fibroblast growth factor, Proc. Natl. Acad. Sci. U.S.A., 83, 2448, 1986.

Vlodavsky, I., Folkman, J., Sullivan, R., Friedman, R., Ishai-Michaeli, R., and Klagsburn, M., Endothelial cell derived basic fibroblast growth factor: synthesis and deposition into subendothelial extracellular matrix, Proc. Natl. Acad. Sci. U.S.A., 84. 2292. 1987.

Abraham, J.A., Whang, J.L., Tumolo, A., Mergia, A., Friedman, J., Gospodarowicz, D., and Fiddes, J.C., Human basic fibroblast growth factor: nucleotide sequence and genomic organization, EMBO J., 5, 2523, 1986.

Delli-Bovi, P., Curatola, A.M., Newman, K.M., Sato, Y., Moscatelli, D., Hewick, R.M., and Basilico, C., Processing, secretion and biological properties of a novel growth factor of the fibroblast growth factor family with oncogenic potential, Mol. Cell. Biol., 8, 2933, 1988.

Saksela, O., Moscatelli, D., Sommer, A., and Rifkin, D.B., Endothelial cell-derived heparin sulfate binds basic fibroblast growth factor and protects it from proteolytic degradation, J. Cell Biol., 107, 743, 1988.

Shreiber, A.B., Kenney, J., Kowalski, W.J., Friesel, R., Mehlaman, A., and Maciag, T., Interaction of endothelial cell growth factor with heparin: characterization by receptor and antibody recognition, Proc. Natl. Acad. Sci. U.S.A., 82, 6138, 1985.

Gospodarowicz, D., Neufeld, G., and Schweigerer, L., Fibroblast growth factor, Mol. Cell. Endocrinol., 46, 187, 1986.

Globus, R.K., Patterson-Buckendahl, P., and Gospodarowicz, D., Regulation of bovine bone cell proliferation by fibroblast growth factor and transforming growth factor B, Endocrinology, 123, 98, 1988.

Neufeld, G. and Gospodarowicz, D., Basic and acidic fibroblast growth factors interact with the same cell surface receptors, J. Biol. Chem., 261, 5631, 1986.

Tsuda, T., Kaibuchi, K., Kawahara, H., Fukuzaki, Y., and Takai, Y., Induction of protein kinase C activation and Ca2+ mobilization by fibroblast growth factor in Swiss 3T3 cells, FEBS Lett., 191, 205, 1985.

Kaibuchi, K., Tsuda, T., Kikuchi, A., Tanimoto, T., Yamashita, T., and Takai, Y., Possible involvement of protein kinase C and calcium ion in growth factor-induced expression of c-myc oncogene in Swiss 3T3 fibroblasts, J. Biol. Chem., 261, 1187, 1986.

Greenberg, M.E. and Ziff, E.B., Stimulation of 3T3 cells induces transcription of the c-fos proto-oncogene, Nature, 311, 433, 1984.

Rudland, P.S., Seifert, W., and Gospodarowicz, D., Growth control in cultured mouse fibroblasts: induction of the pleiotypic and motogenic responses by a purified growth factor, Proc. Natl. Acad. Sci. U.S.A., 71, 2600, 1974.

Nilsen-Hamilton, M., Shapiro, J.M., Massoglia, S.L., and Hamilton, R.T., Selective stimulation by mitogens of incorporation of 35S-methionine into a family of proteins released into the medium by 3T3 cells, Cell, 20, 19, 1980.

Nilsen-Hamilton, M., Hamilton, R.T., Allen, W.R., and Massoglia, S.L., Stimulation of the release of two glycoproteins from mouse 3T3 cells by growth factors and by agents that increase intralysosomal pH, Biochem. Biophys. Res. Commun., 101, 411, 1981.

Lobb, R., Sasse, J., Shing, Y., D'Amore, P., Fett, J., Sullivan, R., Jacobs, J., and Klagsbrun, M., Purification and characterization of heparin-binding endothelial cell growth factors, J. Biol. Chem., 261, 1924, 1986.

Baird, A., Mormede, P. and Bohlen, P., Immunoreactive fibroblast growth factor in cells of peritoneal exudate suggests its identity with macrophage-derived growth factor, Biochem. Biophys. Res. Commun., 126, 358, 1985.

Vlodavsky, I. and Gospodarowicz, D., Structural and functional alterations in the surface of vascular endothelial cells associated with the formation of a confluent cell monolayer and with a withdrawal of fibroblast growth factor, J. Supramol. Struct., 12, 73, 1979.

Kato, Y. and Gospodarowicz, D., Sulfated proteoglycan synthesis by confluent cultures of rabbit costal chondrocytes grown in the presence of fibroblast growth factor, J. Cell Biol., 100, 486, 1985.

Thomas, K.A., Rios-Candelore, M., Gimenez-Gallego, G., DiSalvo, J., Bennet, C., Rodkey, J., and Fitzpatrick, S., Pure brain-derived acidic fibroblast growth factor is a potent angiogenic vascular endothelial cell mitogen with sequence homology to interleukin 1, Proc. Natl. Acad. Sci. U.S.A., 82, 6409, 1985.

Folkman, J., Anti-angiogenesis: new concept for therapy of solid tumors, Ann. Surg., 175, 409, 1972.

Montensano, R., Vassali, J.D., Baird, A., Guillemin, R., and Orci, L., Basic fibroblast growth factor induces angiogenesis in vitro, Proc. Natl. Acad. Sci. U.S.A., 83, 7297, 1986.

Buntrock, P., Jentzsch, K.D., and Heder, G., Stimulation of wound healing using brain extract with fibroblast growth factor (FGF) activity, Exp. Pathol., 21, 46, 1982.

Davidson, J., Klagsbrun, K., Hill, M., Buckley, A., Sulivan, R., Brewer, P., and Woodward, S.J., Accelerated wound repair, cell proliferation, and collagen accumulation are produced by a cartilage-derived growth factor, Cell Biol., 100, 1219, 1985.

Dickson, C. and Gordon, P., Potential oncogene product related to growth factors, Nature, 326, 833, 1987.

Taira, M.Y., Miyagawa, K., Sakamoto, H., Terada, M., and Sugimura, T., cDNA sequence of human transforming gene hst and identification of the coding sequence required for transforming activity, Proc. Natl. Acad. Sci. U.S.A., 84, 2980, 1987.

Zhan, X., Bates, B., Hu, X., and Goldfarb, M., The human FGF-5 oncogene encodes a novel protein related to fibroblast growth factors, Mol. Cell. Biol., 3487, 1988.

Jaye, M., Lyall, R.M., Mudd, R., Schlessinger, J., and Sarver, N., Expression of acidic fibroblast growth factor cDNA confers growth advantage and tumorigenesis to Swiss 3T3 cells, EMBO J., 7, 963, 1988.

Rogelj, S., Weinberg, R.A., Fanning, P., and Klagsbrun, M., Basic fibroblast growth factor fused to a signal peptide transforms cells, Nature, 31, 173, 1988.

Slack, J.M., Darlington, B.G., Heath, J.K., and Godsave, S.F., Mesoderm induction in early Xenopus embryos by heparin-binding growth factors, Nature, 326, 197, 1987.

Hay, E.D., Collagen and embryonic development, in Cell Biology of Extracellular Matrix, Hay, E. D., Ed., Plenum Press, New York, 1981, 379.

Sporn, M.B., Roberts, A.B., Wakefield, L.M., and de Crombrugghe, B., Some recent advances in the chemistry and biology of transforming growth factor beta, J. Cell Biol., 105, 1039, 1987.

Keski-Oja, J., Leof, E.B., Lyons, R.M., Coffey, R.J., Jr., and Moses, H.L., Transforming growth factors and control of neoplastic cell growth, J. Cell. Biochem., 33, 95, 1987.

Massague, J., The TGF-B family of growth and differentiation factors, Cell, 49, 437, 1987.

Cate, R.L., Mattaliano, R.J., Hession, C., and Tizard, R., Isolation of the bovine and human genes for mullerian inhibiting substance and expression of the human gene in animal cells, Cell, 45, 385, 1986.

Mason, A.J., Hayflick, J.S., and Ling, N., Complementary DNA sequences of ovarian follicular fluid inhibin show precursor structure and homology with transforming growth factor-B, Nature, 318, 659, 1985.

Vale, W., Rivier, J., Vaughan, J. et al., Purification and characterization of an FSH releasing protein from porcine ovarian follicular fluid, Nature, 321, 776, 1986.

Padgett, R.W., St. Johnston, D., and Gelbart, W.M., A transcript from Drosophila pattern gene predicts a protein homologous to the transforming growth factor beta family, Nature, 325, 81, 1987.

DeLarco, J.E. and Todaro, G.J., Growth factors from murine sarcoma virus-transformed cells, Proc. Natl. Acad. Sci. U.S.A., 75, 4001, 1978.

Moses, H.L., Branum, E.B., Proper, J.A., and Robinson, R.A., Transforming growth factor production by chemically transformed cells, Cancer Res., 41, 2842, 1981.

Shin, S.I., Freedman, V.H., and Pollack, R., Tumorigenicity of virus-transformed cells in nude mice is correlated specifically with anchorage independent growth in vitro, Proc. Natl. Acad. Sci. U.S.A., 72, 4435, 1975.

Holley, R., Bohlen, W.P., Fava, R., Baldwin, J.H., Kleeman, G., and Armour, R., Purification of kidney epithelial cell growth inhibitors, Proc. Natl. Acad. Sci. U.S.A., 77, 5989, 1980.

Tucker, R.F., Shiley, G.D., Moses, H.L., and Holley, R.W., Growth inhibitor from BSC-1 cells closely related to platelet type beta transforming growth factor, Science, 226, 705, 1984.

Assoian, R.K., Komoriya, A., Meyers, C.A., Miller, D.M., and Sporn, M.B., Transforming growth factor beta in human platelets, J. Biol. Chem., 258, 7155, 1983.

Frolick, C.A., Dart, L.L., Meyers, C.A., Smith, D.M., and Sporn, M.B., Purification and initial characterization of type beta transforming growth factor from human placenta, Proc. Natl. Acad. Sci. U.S.A., 80, 3676, 1983.

Roberts, A.B., Anzano, M.A., Meyers, C.A., Wideman, J., Blacher, R., Pan, Y.C., Stein, S., Lehrman, R., Smith, J.M., Lamb, L.C., and Sporn, M.B., Purification and properties of a type beta transforming growth factor from bovine kidney, Biochemistry, 22, 5692, 1983.

Derynck, R., Jarrett, J.A., Chen, E.Y., and Goeddel, D.V., The murine transforming growth factor-beta precursor, J. Biol. Chem., 261, 4377, 1986.

Derynck, R., Jarrett, J.A., Chen, E.Y., Eaton, D.H., Bell, J.R., Assoian, R.K., Roberts, A.B., Sporn, M.B., and Goeddel, D.V., Human transforming growth factor-beta cDNA sequence and expression in tumor cell lines, Nature, 316, 701, 1985.

Derynck, R., Lindquist, B., Lee, A., Wen, D., Tamm, J., Graycar, J.L., Rhee, L., Mason, A., Miller, D.A., Coffey, R.L., Moses, H.L., and Chen, E.Y., A new type of transforming growth factor-B, TGF-B3, EMBO J., 7, 3737, 1988.

Marquardt, H., Lioubin, M.N., and Ikeda, Y., Complete amino acid sequence of human transforming growth factor type B2, J. Biol. Chem., 262, 12127, 1987.

ten Dijke, P., Hansen, P., Iwata, K.K., Pieler, C., and Foulkes, J.G., Identification of another member of the transforming growth factor type B gene family, Proc. Natl. Acad. Sci. U.S.A., 85, 4715, 1988.

Cheifetz, S., Weatherbee, J.A., Tsang, M.L., Anderson, J.K., Mole, A.E., Lucas, R., and Massague, J., The transforming growth factor-beta system: a complex pattern of cross-reactive ligands and receptors, Cell, 48, 409, 1987.

Roberts, A.B., Anzano, M.A., Lamb, L.C., Smith, J.M., and Sporn, M.B., New class of transforming growth factors potentiated by epidermal growth factor: isolation from non-neoplastic tissues, Proc. Natl. Acad. Sci. U.S.A., 78, 5339, 1981.

Seyedin, S.M., Thompson, A.Y., Bentz, H., Rosen, D.M., McPherson, A.M., Conti, A., Siegel, N.R., Galluppi, G.R., and Piez, K.A., Cartilage inducing factor A, J. Biol. Chem., 261, 5693, 1986.

Wakefield, L.M., Smith, D.M., Flanders, K.C., and Sporn, M.B., Latent transforming growth factor-B from human platelets, J. Biol. Chem., 263, 16, 7646, 1988.

Wakefield, L.M., Smith, D.M., Masui, T., Harris, C.C., and Sporn, M.B., Distribution and modulation of the cellular receptor for transforming growth factor beta, J. Cell Biol., 105, 965, 1987.

Lawrence, D.A. and Jullien, P., Conversion of a high molecular weight latent beta TGF from chicken embryo fibroblasts into a low molecular weight active beta TGF under acidic conditions, Biochem. Biophys. Res. Commun., 133, 1026, 1985.

O'Connor-McCourt, M.D. and Wakefield, L.M., Latent transforming growth factor-B in serum, J. Biol. Chem., 262, 14090, 1987.

Massague, J. and Like, B., Cellular receptors for type B transforming growth factor: ligand binding and affinity labelling in human and rodent cell lines, J. Biol. Chem., 260, 2636, 1985.

Ohata, M., Greenberger, J.S., Anklesaria, P., Bassols, A., and Massague, J., Two forms of transforming growth factor-B distinguished by multipotential hematopoietic progenitor cells, Nature, 329, 539, 1987.

Rosa, F., Roberts, A.B., Danielpour, D., Dart, L.L., Sporn, M.B., and Dawid, I., Mesoderm induction in amphibians: the role of TGF-B2-like factors, Science, 239, 783, 1988.

Anzano, M.A., Roberts, A.B., and Sporn, M.B., Anchorage independent growth of primary rat embryo cells is induced by platelet-derived growth factor and inhibited by type-beta transforming growth factor, J. Cell. Physiol., 126, 312, 1986.

Takehara, K., LeRoy, E.C., and Grotendorst, G.R., TGF-B inhibition of endothelial cell proliferation: alteration of EGF binding and EGF-induced growth-regulatory (competence) gene expression, Cell, 49, 415, 1987.

Leoff, E.B., Proper, J.A., Gousin, A.S., Shipley, G.D., DiCorleto, A.E., and Moses, H.L., Induction of c-sis mRNA and activity similar to platelet-derived growth factor B: a proposed model for indirect mitogenesis involving autocrine activity, Proc. Natl. Acad. Sci. U.S.A., 83, 2453, 1986.

Van Obberghen-SchiLting, E., Roche, N.S., Flanders, K.C., Sporn, M.B., and Roberts, A.B., Transforming growth factor-B 1 positively regulates its own expression in normal and transformed cells, J. Biol. Chem., 263, 16, 7741, 1988.

Seyedin, P.R., Segarinin, P.R., Rosen, D.M., Thompson, A.Y., Bentz, A., and Graycar, J., Cartilage inducing factor B is a unique protein structurally and functionally related to transforming growth factor-beta, J. Biol. Chem., 262, 1946, 1987.

Seyedin, S.M., Thomas, T.C., Thompson, A.Y., Rosen, D.M., and Piez, K.A., Purification and characterization of two cartilage-inducing factors from bovine demineralized bone, Proc. Natl. Acad. Sci. U.S.A., 82, 2267, 1985.

Rosen, D.M., Stempiens, S.A., Thompson, A.Y., and Seyedin, S.M., Transforming growth factor-beta modulates the expression of osteoblast and chondroblast phenotypes in vitro, J. Cell. Physiol., 134, 337, 1988.

Sandberg, M., Vuorio, T., Hirvonen, H., Alitalo, K., and Vuorio, E., Enhanced expression of TGF-B and c-fos mRNAs in the growth plates of developing human long bones, Development, 102, 461, 1988.

Hiraki, Y., Inoue, H., Hirai, R., Kato, Y., and Suzuki, F., Effect of transforming growth factor B on cell proliferation and glycosaminoglycan synthesis by rabbit growth-plate chondrocytes in culture, Biochim. Biophys. Acta, 167, 91, 1988.

Robey, P.G., Young, M.F., Flanders, K.C., Roche, N.S., Kondaiah, A., Reddi, A.H., Termine, J.D., Sporn, M.B., and Roberts, A.B., Osteoblasts synthesize and respond to transforming growth factor-type B (TGF-B) in vitro, J. Cell Biol., 105, 457, 1987.

Centrella, M., McCarthy, T.L., and Canalis, E., Transformin growth factor beta is a bifunctional regulator of replication and collagen synthesis in osteoblast-enriched cell cultures from fetal rat bone, J. Biol. Chem., 262, 2869, 1987.

Pfeilschifter, J. and Mundy, G.R., Modulation of type beta transforming growth factor activity in bone cultures by osteotropic hormones, Proc. Natl. Acad. Sci. U.S.A., 84, 2024, 1987.

Sporn, M.B., Roberts, A.B., Shull, J.H., Smith, J.M., Ward, J.M., and Sodek, J., Polypeptide transforming growth factors isolated from bovine sources and used for wound healing in vivo, Science, 219, 1329, 1983.

Roberts, A.B., Sporn, M.B., Assoian, R.K., Smith, J.M., Wakefield, L.M., Heine, U.I., Liotta, L.A., Falanga, V., Kehrl, J.H., and Fauci, A.S., Transforming growth factor type-beta: rapid induction of fibrosis and angiogenesis in vivo and stimulation of collagen formation in vitro, Proc. Natl. Acad. Sci. U.S.A., 83, 4167, 1986.

Mustoe, T.A., Pierce, G.F., Thomason, A., Gramates, P., Sporn, M.B., and Deuel, T.F., Accelerated healing of incisional wounds in rats induced by transforming growth factor beta, Science, 237, 1333, 1987.

Assoian, R.K., Fleurdelys, B.E., Stevenson, H.C., Miller, P.J., Madtes, D.K., Raines, E.W., Ross, R., and Sporn, M.B., Expression and secretion of type beta transforming growth factor by activated human macrophages, Proc. Natl. Acad. Sci. U.S.A., 84, 6020, 1987.

Kehrl, J.H., Roberts, A.B., Sporn, M.B., and Fauci, A.S., Transforming growth factor beta is an important immunomodulatory protein for human B-lymphocytes, J. Immunol., 137, 3855, 1986.

Kehrl, J.H., Wakefield, L.M., Roberts, A.B., Jakowlew, S.B., Alvarez-Mon, M., Derynck, R., Sporn, M.B., and Fauci, A.S., Production of transforming growth factor beta by human T lymphocytes and its potential role in the regulation of T cell growth factor, J. Exp. Med., 163, 1037, 1986.

Rook, A.H., Kehrl, J.H., and Wakefield, L.M., Effects of transformed growth factor-B on the functions of natural killer cells: depressed cytolytic activity and blunting of interferon responsiveness, J. Immunol., 136, 3916, 1986.

Postlethwaite, A.E., Keski-Oja, J., Moses, H.L., and Kang, A.H., Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta, J. Exp. Med., 165, 251, 1987.

Ignorz, R. and Massague, J., Transforming growth factor-beta stimulates the expression of fibronectin and collagen and their incorporation into the extracellular matrix, J. Biol. Chem., 261, 4337, 1986.

Wrana, J.L., Sodek, J., Ber, R.L., and Bellows, C.G., The effects of platelet-derived transforming growth factor B on normal human diploid gingival fibroblasts, Eur. J. Biochem., 159, 69, 1986.

Penittinen, R.P., Kobayashi, S., and Bornstein, P., Transforming growth factor B increases mRNA for matrix protein both in the presence and in the absence of changes in mRNA stability, Proc. Natl. Acad. Sci. U.S.A., 85, 1105, 1988.

Laiho, M., Sakesela, O., Andresean, P.A., and Keski-Oja, J., Enhanced production and extracellular deposition of the endothelial-type plasminogen activator inhibitor in cultured human lung fibroblasts by transforming growth factor-beta, J. Cell Biol., 103, 2403, 1986.

Chiang, C.P. and Nilsen-Hamilton, M., Opposite and selective effects of epidermal growth factor and human platelet transforming growth factor-beta on the production of secreted proteins by murine 3T3 cells and human fibroblasts, J. Biol. Chem., 261, 10478, 1986.

Heine, U.I., Flanders, K., Roberts, A.B., Munoz, E.F., and Sporn, M.B., Immunocytochemical localization of TGF-beta during embryonal development in mice, Proc. Am. Assoc. Cancer. Res., 28, 53, 1987.

Humbel, R.E., Insulin-like growth factors, somatomedins, and multiplication stimulating activity: chemistry, in Hormonal Proteins and Peptides, Li, C. H., Ed., Academic Press, New York, 1984, 12.

Dalmon, W.D., Jr. and Daughaday, W.H., A hormonally controlled serum incorporation by cartilage in vitro, J. Lab. Clin. Med., 49, 825, 1957.

Froesch, E.R., Burghi, H., Ramseir, E.B., Bally, P., and Lab-hart, A., Antibody-suppressible and nonsuppressible insulin-like activities in human serum and their physiological significance. An insulin assay with adipose tissue of increased precision and specificity, J. Clin. Invest., 42, 1816, 1963.

Pierson, R.W. and Temin, H.M., The partial purification from calf serum of a fraction with multiplication-stimulating activity for chicken fibroblasts in cell culture and with nonsuppressible insulin-like activity, J. Cell. Physiol., 79, 319, 1972.

Hall, K. and Uthne, K., Some biological properties of purified sulfation factor (SF) from human plasma, Acta Med. Scand., 190, 137, 1971.

Morell, B. and Froesch, E.R., Fibroblasts as an experimental tool in metabolic and hormone studies. II. Effects of insulin and nonsuppresible insulin-like activity (NSILA) on fibroblasts in culture, Eur. J. Clin. Endocrinol. Metab., 55, 1081, 1973.

Zingg, A.E. and Froesch, E.R., Effects of partially purified preparations with nonsuppressible insulin-like activity (NSILA) on sulfate incorporation into rat and chicken cartilage, Diabetologia, 9, 472, 1973.

Rinderknecht, E. and Humbel, R.E., Amino-terminal sequences of two polypeptides from human serum with nonsuppresible insulin-like and cell-growth-promoting activities: evidence for structural homology with insulin B chain, Proc. Natl. Acad. Sci. U.S.A., 73, 4379, 1976.

Rinderknecht, E. and Humbel, R.E., Polypeptides with nonsuppressible-like and cell growth promoting activities in human serum: isolation, chemical characterization, and some biological properties of forms I and II, Proc. Natl. Acad. Sci. U.S.A., 73, 2365, 1976.

Klapper, D.G., Svoboda, M.E., and Van Wyk, J.J., Sequence analysis of somatomedin-C: confirmation of identity with insulin-like growth factor I, Endocrinology, 112, 2215, 1983.

Rinderknecht, E. and Humbel, R.E., The amino acid sequence of human insulin-like growth factor I and its structural homology with proinsulin, J. Biol. Chem., 253, 2769, 1978.

Marquardt, H., Todaro, G.J., Henderson, L.E., and Oroszian, S., Purification and primary structure of a polypeptide with multiplication-stimulating activity from rat liver cell cultures, J. Biol. Chem., 256, 6859, 1981.

Rinderknecht, E. and Humbel, R.E., Primary structure of human insulin-like growth factor II, FEBS Lett., 89, 283, 1978.

Svobodo, M.E. and Van Schaik, J.J., Purification of somatomedin-C/insulin-like growth factor I, Methods Enzymol., 109, 798, 1985.

Jansen, M., Van Schaik, F.M.A., Ricker, A.T., Bullock, B., Woods, D.E., Gabbay, K.H., Nussbaum, A.L., Sussenbach, J.S., and Van der Brande, J.L., Sequence of cDNA encoding human insulin-like growth factor I precursor, Nature, 306, 609, 1983.

Bell, G.I., Merryweather, J.P., Sanchez-Prescador, R., Stempien, M.M., Priestly, L., Scott, J., and Ball, L.B., Sequence of a cDNA clone encoding human preproinsulin-like growth factor II, Nature, 310, 775, 1984.

Jansen, M., Van Schaik, F.M.A., Van Tul, H., Van der Brande, J.L., and Sussenbach, J.S., Nucleotide sequences of cDNA's encoding precursors of human insulin-like growth factor II (IGF-II) and an IGF-II variant, FEBS Lett., 179, 243, 1985.

Rall, L.B., Scott, J., and Bell, G.I., Human insulin-like growth factor I and II messenger RNA: isolation of complimentary DNA and analysis of expression, Methods Enzymol., 146, 239, 1987.

Blundell, T.L., Cutfield, J.F., Cutfield, S.M., Dodson, E.J., Dodson, G.G., Hodgkin, D.C., Mercola, D.A., and Vijayan, M., Atomic positions in chombohedral 2-Zinc insulin crystals, Nature, 231, 506, 1971.

Woods, D.E., Markham, A.F., Ricker, A.T., Goldberger, G., and Colton, H.R., Isolation of cDNA clones for the human complement protein factor B, a class III major histocompatibility gene product, Proc. Natl. Acad. Sci. U.S.A., 77, 5201, 1980.

Bell, G.I., Gerhard, D.S., Fong, N.M., Sanchez-Pescador, R., and Rail, L.B., Isolation of the human insulin-like growth factor gene: insulin-like growth factor II and insulin genes are contiguous, Proc. Natl. Acad. Sci. U.S.A., 82, 6450, 1985.

Brissenden, J.E., Ulrich, A., and Franke, U., Human chromosomal mapping of genes for insulin-like growth factor I and II and epidermal growth factor, Nature, 310, 781, 1984.

Tricoli, J.V., Rail, L.B., Scott, J., Bell, G.I., and Shows, T.B., Localization of insulin-like growth factor genes to human chromosomes 11 and 12, Nature, 310, 784, 1984.

Chernausek, S.D., Jacobs, S., and Van Wyk, J.J., Structural similarities between human receptors for somatomedin C and insulin: analysis by affinity labeling, Biochemistry, 20, 7345, 1981.

Massague, J. and Czech, M.P., The subunit structures of two distinct receptors for insulin-like growth factors I and II and their relationship to the insulin receptor, J. Biol. Chem., 257, 5038, 1982.

Morgan, D.O., Edman, J.C., Standring, D.N., Fried, V.A., Smith, M.C., Roth, R.A., and Rutter, W.J., Insulin like growth factor II reception as a multifunctional binding protein, Nature, 329, 301, 1987.

Berelowitz, M., Szabo, M., Frohman, L.A., Firestone, S., Chu, L., and Hintz, R.L., Somatomedin-C mediates growth hormone negative feedback by effects on both the hypothalamus and the pituitary, Science, 212, 1279, 1981.

Brazeau, P., Guillemin, R., Ling, N., Van Wyk, J.J., and Humbel, R.E., Somatomedin inhibition of the growth hormone secretion stimulated by the hypothalamic factor somatocrinin or the synthetic peptide, hpGRF, C.R. Seances Acad. Sci., 295, 651, 1982.

Abe, H., Molitch, M., Van Wyk, J.J., and Underwood, L.E., Human growth hormone and somatomedin C suppress the spontaneous release of growth hormone in anesthetized rats, Endocrinology, 113, 1319, 1983.

Moses, A.C., Nissley, S.P., Short, P.A., Rechler, M.M., White, R.M., Knight, A.B., and Higa, O.Z., Increased levels of multiplication-stimulating activity, an insulin-like growth factor in fetal rat serum, Proc. Natl. Acad. Sci. U.S.A., 77, 3649, 1980.

Bennet, A., Wilson, D.M., Liu, F., Nagashima, R., Rosenfeld, R.G., and Hintz, R.L., Levels of insulin-like growth factors I and II in human cord blood, J. Clin. Endocrinol. Metab., 57, 609, 1983.

Ashton, I.K., Zapf, J., Einschenk, I., and MacKenzie, I.Z., Insulin-like growth factors (GF) I and 2 in human foetal plasma and relationship to gestational age and foetal size during midpregnancy, Acta Endocrinol., 110, 558, 1985.

Adams, S. 0., Nissley, S.P., Handwerger, S., and Rechler, M.M., Developmental patterns of insulin-like growth factor-I and- II synthesis and regulation in rat fibroblasts, Nature, 302, 150, 1983.

Conover, C.A., Rosenfeld, R.G., and Hintz, R.L., Insulin-like growth factor II binding and action in human fetal fibroblasts, J. Cell. Physiol., 133, 560, 1987.

Strain, A.J., Hill, D.J., Swenne, I., and Milner, R.D.G., Regulation of DNA synthesis in human fetal hepatocytes by placental lactogen, growth hormone, and insulin-like growth factor I/somatomedin C, J. Cell. Physiol., 132, 33, 1987.

Zapf, J., Waldvogel, M., and Froesch, E.R., Binding of nonsuppressible insulin-like activity to human serum, Arch. Biochem. Biophys., 168, 638, 1975.

Engfeldt, P., Arner, P., Bolinder, J., and Ostman, J., Phosphodiesterase activity in human subcutaneous adipose tissue in insulin-and noninsulin-dependent diabetes mellitus, J. Clin. Endocrinol. Metab., 55, 983, 1982.

Hintz, R.L. and Liu, F., Demonstration of specific plasma protein binding sites for somatomedin, J. Clin. Endocrinol. Metab., 45, 988, 1977.

Smith, G.L., Lyons, R.M., Harkins, R.N., and Knaver, D.J., Purification of multiplication-stimulating activity carrier protein, Methods Enzymol., 146, 270, 1987.

Furianetto, R.W., The somatomedin C binding protein: evidence for a heterologous subunit structure, J. Clin. Endocrinol. Metab., 51, 12, 1980.

Copeland, K.C., Underwood, L.E., and Van Wyk, J.J., Induction of immunoreactive somatomedin C in human serum by growth hormone: dose response relationships and effect on chromatographic profiles, J. Clin. Endocrinol. Metab., 50, 690, 1980.

Isaksson, O.G.P., Lindahl, A., Nilsson, A., and Isgaard, J., Mechanism of the stimulatory effect of growth hormone on longitudinal bone growth, Endocrine Rev., 8, 426, 1987.

Clemmons, D.R., Underwood, L.E., and Van Wyk, J.J., Hormonal control of immunoreactive somatomedin production by cultured human fibroblasts, J. Clin. Invest.. 67, 10, 1981.

Stracke, H., Schultz, A., Moeller, D., Rossol, S., and Schatz, H., Effect of growth hormone on osteoblasts and demonstration of somatomedin-C/IGF-I in bone organ culture, Acta Endocrinol. (Copenhagen), 107, 16, 1984.

Roberts, C.T., Jr., Laky, S.R., Lowe, W.L., Seaman, W.T., and LeRoith, D., Molecular cloning of rat IGF-I cDNA: differential mRNA processing and regulation by growth hormone in extrahepatic tissues, Mol. Cell. Endocrinol., 1, 243, 1987.

Rappolee, D.A., Mark, D., Banda, M.J., and Werb, Z., Wound macrophages express TGF-alpha and other growth factors in vivo: analysis by mRNA phenotyping, Science, 241, 708, 1988.

Hock, J.M., Centrella, M., and Canalis, E., Insulin-like growth factor I has independent effects on bone matrix formation and cell replication, Endocrinology, 122, 254, 1988.

Makower, A.M., Wroblewski, J., and Pawlowski, A., Effects of IGF-I, EGF, and FGF on proteoglycans synthesized by fractionated chondrocytes of rat rib growth plate, Exp. Cell Res., 179, 498, 1988.

Taylor, A.M., Dandona, P., Morrell, D.J., and Preece, M.A., Insulin like growth factor-I, protein kinase-C, calcium and cyclic AMP: partners in the regulation of chondrocyte mitogenesis and metabolism, FEBS Lett., 236,33, 1988.

Schmid, C., Steiner, T., and Froesch, E.R., Insulin-like growth factor I supports differentiation of cultured osteoblast-like cells, FEBS Lett., 173, 48, 1984.

Canalis, E., Effect of hormones and growth factors on alkaline phosphatase activity and collagen synthesis in cultured rat calvariae, Metabolism, 32, 14, 1983.

Schoenle, E., Zapf, J., Humbel, R.E., and Froesch, E.R., Insulin-like growth factor I stimulates growth in hypophysectomized rats. Nature, 296, 252, 1982.

Oelz, O., Jakob, A., and Froesch, E.R., Nonsuppressible insulin-like activity (NSILA) of human serum. V. Hypoglycemia and preferential metabolic stimulation of muscle by NSILA, Eur. J. Clin. Invest., 1, 48, 1982.

Holly, J.M.P., Amiel, S.A., Sandhu, R.R., Rees, L.E., and Wass, J.A.H., The role of growth hormone in diabetes mellitus, J. Endocrinol., 118, 353, 1988.

Shea, B.T. and Gomez, A.M., Tooth scaling and evolutionary dwarfism: an investigation of allometry in human pygmies, Am. J. Phys. Anthropol., 77, 117, 1988.

Sporn, M.B. and Roberts, A.B., Peptide growth factors and inflammation, tissue repair and cancer, J. Clin. Invest.. 78, 329, 1986.

Cohen, S., Epidermal growth factor (EGF): historical perspectives, in Hormonal Proteins and Peptides, Vol. 12, Li, C. H., Ed., Academic Press, New York, 1984, 299.

Cohen, S. and Elliott, G.A., The stimulation of epidermal keratinization by a protein isolation from the submaxillary gland of the mouse, J. Invest. Dermatol., 40, 1, 1963.

Cohen, S., The stimulation of epidermal proliferation by a specific protein (EGF), Dev. Biol., 12, 394, 1965.

Armelin, H., Pituitary extracts and steroid hormones in the control of 3T3 cell growth, Proc. Natl. Acad. Sci. U.S.A., 70, 2702, 1973.

Hollenberg, M.D. and Cuatreecases, P., Epidermal growth factor: receptors in human fibroblasts and modulation of action by cholera toxin, Proc. Natl. Acad. Sci. U.S.A., 70, 2964, 1973.

Scott, J., Urdea, M., Quiroga, M., Sanchez-Pescador, R., Fong, N., Selby, M., Rutter, W.J., and Bell, G.I., Structure of a mouse submaxillary messenger RNA encoding epidermal growth factor and seven related proteins, Science, 221, 236, 1983.

Harper, R.A., Pierce, J., and Savage, C.R., Jr., Purification of human epidermal growth factor by monoclonal antibody affinity chromatography, Methods Enzymol., 146, 3, 1987.

Cohen, S., Carpenter, G., and Lembach, K.J., Interaction of epidermal growth factor (EGF) with cultured fibroblasts, Adv. Metab. Disorders, 8, 265, 1975.

Gregory, H., Isolation and structure of urogastrone and its relationship to epidermal growth factor, Nature, 257, 325, 1975.

Turkington, R.W., Males, J.L., and Cohen, S., Synthesis and storage of epithelial-epidermal growth factor in submaxillary gland, Cancer Res., 31, 252, 1971.

Marti, U., Burwen, S.J., and Jones, A.L., Biological effects of epidermal growth factor, with emphasis on the gastrointestinal tract and liver: an update, Hepatology, 9, 126, 1989.

Cohen, S., Epidermal growth factor, In Vitro Cell. Dev. Biol., 23, 239, 1987.

Taylor, J.M., Mitchell, W.M., and Cohen, S., Epidermal growth factor, J. Biol. Chem., 247, 5928, 1972.

Carpenter, G. and Zenegui, J.G., Epidermal growth factor, its receptor, and related proteins, Exp. Cell. Res., 164, 1, 1986.

Taylor, J.M., Mitchell, W.M., and Cohen, S., Epidermal growth factor: high and low molecular weight forms, Proc. Natl. Acad. Sci. U.S.A., 67, 164, 1970.

Scott, J., Urdea, M., Quiroga, M., Sanchez-Pescador, R., Fong, N., Selby, M., Rutter, W.J., and Bell, G.I., Structure of a mouse submaxillary messenger RNA encoding epidermal growth factor and seven related proteins, Science, 221, 236, 1983.

Rail, L.B., Scott, L., and Bell, G.I., Mouse preproepidermal growth factor synthesis by the kidney and other tissues, Nature, 313, 228, 1985.

Gill, G.N., Bertics, P.J., and Santon, J.B., Epidermal growth factor and its receptor, Mol. Cell. Endocrinol., 51, 169, 1987.

Tashjian, A.J., Jr. and Levine, L., Epidermal growth factor stimulates prostaglandin production and bone resorption in cultured mouse calvaria, Biochem. Biophys. Res. Commun., 85, 966, 1978.

Tashjian, A.J., Voekel, E.F., Lazzaro, M., Singer, F.R., Roberts, A.B., Derynck, R., Winkler, M.E., and Levine, L., Alpha and beta human transforming growth factors stimulate prostaglandin production and bone resorption in cultured mouse calvaria, Proc. Natl. Acad. Sci. U.S.A., 82, 4535, 1985.

Raisz, L.G. and Martin, T.J., Prostaglandins in bone and mineral metabolism, in Bone and Mineral Research, Vol. 2, Peck, W. A., Ed., Excerpta Medica, Amsterdam, 1980, 286.

Ibbotson, K.J., Twardzik, D.R., D'Souza, S.M., Hargreaves, W.R., Todaro, G.J., and Mundy, G.R., Stimulation of bone resorption by synthetic transforming growth factor alpha, Science, 228, 1007, 1985.

Canalis, E. and Raisz, L.G., Effect of epidermal growth factor on bone formation in vitro, Endocrinology, 104, 862, 1979.

Canalis, E., Effects of hormones and growth factors on alkaline phosphatase activity and collagen synthesis in cultured rat calvariae, Metabolism, 32, 14, 1983.

Hiramatsu, M., Kumegawa, M., Katakeyama, K., Yajima, T., Minami, N., and Kodama, H., Effect of epidermal growth factor on collagen synthesis in osteoblast cells derived from newborn mouse calvaria, Endocrinology, 111, 1810, 1982.

Kumegawa, M., Kiramatsu, M., Hatakeyama, K., Yajima, T., Kodama, H., Osaki, T., and Kurisu, K., Effects of epidermal growth factor on osteoblastic cells in vitro, Calcif Tissue Int., 35, 542, 1983.

Osaki, Y., Tsunoi, M., Hakeda, Y., Kurisu, K., and Kumegawa, M., Immunocytochemical study of collagen in epidermal growth factor (EGF)-treated osteoblastic cells, J. Histochem. Cytochem., 32, 1231, 1984.

Hata, R.I., Hori, H., Nagai, Y., Tanaka, S., Kondo, M., Kiramatsu, M., Utsumi, N., and Kumegawa, M., Selective inhibition of type I collagen synthesis in osteoblastic cells by epidermal growth factor, Endocrinology, 115, 867, 1984.

Ng, K.W., Partridge, N.C., Niall, N., and Martin, T.J., Stimulation of DNA synthesis by EGF in osteoblast-like cells, Calcif. Tissue Int., 35, 624, 1983.

Turkington, R.W., The role of epithelial growth factor in mammary gland development in vitro, Exp. Cell. Res., 57, 79, 1969.

Heimberg, M., Weinstein, I., LeQuire, V.S., and Cohen, S., The induction of fatty liver in neonatal animals by a purified protein (EGF) from mouse submaxillary gland, Life Sci., 4, 1625, 1965.

Hoober, J.K. and Cohen, S., Epidermal growth factor. I. The stimulation of protein and ribonucleic acid synthesis in chick embryo epidermis, Biochim. Biophys. Acta, 138, 347, 1967.

Hoober, J.K. and Cohen, S., Epidermal growth factor. II. Increased activity of ribosomes from chick embryo epidermis for cell-free protein synthesis, Biochim. Biophys. Acta, 138, 357, 1967.

Cohen, S. and Stastny, M., Epidermal growth factor. III. The stimulation of polysome formation in chick embryo epidermis, Biochim. Biophys. Acta, 166, 427, 1968.

Stastny, M. and Cohen, S., Epidermal growth factor. IV. The induction of ornithine decarboxylase, Biochim. Biophys. Acta, 204, 578, 1970.

Stastny, M. and Cohen, S., The stimulation of omithine decarboxylase activity in testes of the neonatal mouse, Biochim. Biophys. Acta, 261, 177, 1972.

Haigler, H., Ash, J.F., Singer, S.J., and Cohen, S., Visualization by fluorescence of the binding and internalization of epidermal growth factor in human carcinoma cells A-431, Proc. Natl. Acad. Sci. U.S.A., 75, 3317, 1978.

Fabricant, R.N., DeLarco, J.E., and Todaro, G.J., Nerve growth factor receptors on human melanoma cells in culture, Proc. Natl. Acad. Sci. U.S.A., 74, 565, 1977.

Carpenter, G., Lembach, K.J., Morrison, N.M., and Cohen, S., Characterization of the binding of 125I-labeled epidermal growth factor to human fibroblasts, J. Biol. Chem., 250, 4297, 1975.

Soderquist, A.M. and Carpenter, G., Biosynthesis of the epidermal growth factor receptor in cultured cells, Methods Enzymol., 146, 49, 1987.

Yarden, Y. and Schlessinger, J., The EGF receptor kinase: evidence for allosteric activation and intramolecular selfphosphorylation, in Growth Factors in Biology and Medicine, Ciba Foundation Symp., 116, Pitman, London, 1985, 23.

Ullrich, A., Coussens, L., Hayflick, J.S., Dull, T.J., Gray, A., Tam, A.W., Lee, J., Yarden, Y., Libermann, T.A., Schlessinger, J., Downward, J., Mayes, E.L.V., Whittle, N., Waterfield, M.D., and Seeburg, P.H., Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells, Nature, 309, 418, 1984.

Downward, J., Yarden, Y., Mayes, E., Scrace, G., Totty, N., Stockwell, P., Ullrich, A., Schlessinger, J., and Waterfield, M.D., Close similarity of epidermal growth factor receptor and Verb-B oncogene protein sequences, Nature, 307, 521, 1984.

Bishop, J.M., Cellular oncogenes and retroviruses - a review, Annu. Rev. Biochem., 52, 301, 1983.

Zidovetzki, R., Yarden, Y., Schlessinger, J., and Tovin, T.M., Rotational diffusion of epidermal growth factor complexed to cell surface receptors reflects rapid microaggregation and endocytosis of occupied receptors, Proc. Natl. Acad. Sci. U.S.A., 78, 6981, 1981.

Stoscheck, C.M. and Carpenter, G., Down regulation of epidermal growth factor receptors: direct demonstration of receptor degradation in human fibroblasts, J. Cell Biol., 98, 1048, 1984.

Hunter, T. and Cooper, J.A., Epidermal growth factor induced rapid tyrosine phosphorylation of proteins in A431 human tumor cells, Cell, 24, 741, 1981.

Cochet, C., Gill, G.N., Meisenhelder, J., Cooper, J.A., and Hunter, T., C-kinase phosphorylates the epidermal growth factor receptor and reduced its epidermal growth factor stimulated tyrosine protein kinase activity, J. Biol. Chem., 259, 2553, 1984.

Iwashita, S. and Fox, C.F., Epidermal growth factor and potent phorbol tumor promotes induced epidermal growth factor receptor phosphorylation in a similar but distinctively different manner in human epidermoid carcinoma A431 cells, J. Biol. Chem., 259, 2559, 1984.

Carpenter, G. and Cohen, S., Human epidermal growth factor and the proliferation of human fibroblasts, J. Cell. Physiol., 88, 227, 1976.

Haigler, H.T. and Carpenter, G., Production and characterization of antibody blocking epidermal growth factor: receptor interactions, Biochim. Biophys. Acta, 598, 314, 1980.

Shechter, Y., Hernaez, L., and Cuatrecasas, P., Epidermal growth factor: biological activity requires persistent occupation of high-affinity cell surface receptors, Proc. Natl. Acad. Sci. U.S.A., 75, 5788, 1978.

DeLarco, J.E. and Todaro, G.J., Growth factors from murine sarcoma virus-transformed cells, Proc. Natl. Acad. Sci. U.S.A., 75, 4001, 1978.

Massaque', J., Epidermal growth factor-like transforming growth factor. II. Interaction with epidermal growth factor receptors in human placenta membranes and A431 cells, J. Biol. Chem., 258, 13614, 1983.

Derynck, R., Transforming growth factor-alpha: structure and biological activities, J. Cell Biochem., 32, 293, 1986.

Schreiber, A.B., Winkler, M.E., and Derynch, R., Transforming growth factor-alpha: a more potent angiogenic mediator than epidermal growth factor, Science, 232, 1250, 1986.

Todaro, G.J., Fryling, C., and Delarco, J.E., Transforming growth factors produced by certain human tumor cells: polypeptides that interact with epidermal growth factor receptors, Proc. Natl. Acad. Sci. U.S.A., 77, 5258, 1980.

Madtes, D.K., Raines, E.W., Sakariassen, K.S., Assoian, R.K., Sporn, M.B., Bell, G.I., and Ross, R., Induction of transforming growth factor-alpha in activated human alveolar macrophages, Cell, 53, 285, 1988.

Smith, T.J. and Wagner, R.R., Rabbit macrophage interferons. I. Conditions for biosynthesis by virus-infected and uninfected cells, J. Exp. Med., 125, 559, 1967.

Fleit, H.B. and Rabinovitch, M., Production of interferon by in vitro derived bone marrow macrophages, Cell. Immunol., 57, 495, 1981.

Assoian, R.K., Fleurdelys, B.E., Stevenson, H.C., Miller, P.J., Madtes, D.K., Raines, E.W., Ross, R., and Sporn, M.B., Expression and secretion of type beta transforming growth factor by activated human macrophages, Proc. Natl. Acad. Sci. U.S.A., 84, 6020, 1987.

Shimokado, K., Raines, E.W., Madtes, D.K., Barrett, T.B., Benditt, E.P., and Ross, R., A significant part of macrophage-derived growth factor consists of at least two forms of PDGF, Cell, 43, 277. 1985.

Martinet, Y., Bitterman, P.B., Mornex, J.F., Grotendorst, G.R., Martin, G.R., and Crystal, R.G., Activated human monocytes express the c-sis proto-oncogene and release a mediator showing PDGF-like activity, Nature, 319, 158, 1986.

Mornex, J.F., Martinet, Y., Yamauchi, K., Bitterman, P.B., Grotendorst, G.R., Chytil-Weir, A., Martin, G.R., and Crystal, R.G., Spontaneous expression of the c-cis gene and release of a platelet-derived growth factor like molecule by human alveolar macrophages, J. Clin. Invest., 78, 61, 1986.

Baird, A., Mormede, P., and Bohlen, P., Immunoreactive fibroblast growth factor in cells of peritoneal exudate suggests its identity with macrophage-derived growth factor, Biochem. Biophys. Res. Commun., 126, 358, 1985.

Dinarello, C.A., Interleukin-1, Rev. Infect. Dis., 6, 51, 1984.

Wewers, M.D., Rennard, S.I., Hance, A.J., Bitterman, P.B., and Crystal, R.G., Normal human alveolar macrophages obtained by bronchoalveolar lavage have a limited capacity to release interleukin-1, J. Clin. Invest., 74, 2208, 1984.

Buckley, A., Davidson, J.M., Kamerath, D.C., Wolt, T.B., and Woodward, S.C., Sustained release of epidermal growth factor accelerates wound repair, Proc. Natl. Acad. Sci. U.S.A., 82, 7340, 1985.

Laato, M., Kahari, V., Niinikoski, J., and Buorio, E., Epidermal growth factor increases collagen production in granulation tissue by stimulation of fibroblast proliferation and not by activation of procollagen genes, Biochem. J., 247, 385, 1987.

Burstein, N.L., Review: growth factor effects on corneal wound healing, J. Occular Pharmacol., 82, 7340, 1985.

Culbertson, W.W., Schantzlin, D., West, C., Dawson, C., Gospodarowicz, D., and Kramer, S.G., The effect of epithelial growth factor on comeal epithelial defects, Invest. Ophthalmol. Vis. Sci. (Suppl.), 19, 74, 1980.

Olsen, P.S., Role of epidermal growth factor in gastroduodenal mucosal protection, J. Clin. Gastroenterol., 10 (Suppl. 1), 5146, 1988.

Itoh, M., Joh, T., Imai, S., Miyamoto, T., Matsusako, K., Iwai, A., Katsumi, K., Endo, K., Goto, K., and Takeuchi, T., Experimental and clinical studies on epidermal growth factor for gastric mucosal protection and healing of gastric ulcers, J. Clin. Gastroenterol., 10 (Suppl. 1), 57, 1988.

Dinarello, C.A. and Mier, J.W., Interleukins, Annu. Rev. Med., 37, 173, 1986.

Dinarello, C.A., An update on human interleukin-1: from molecular biology to clinical relevance, J. Clin. Immunol., 5, 287, 1985.

Krane, S.M., Goldring, S.R., and Dayer, J.M., Interactions among lymphocytes, monocytes and other synovial cells in the rheumatoid synovium, in Lymphokines, Pick, E. and Landy, M., Eds., Academic Press, New York, 1982, 75.

Wood, D.D., Bayne, E.K., Goldring, M.B., Gowen, M., Ham-merman, D., Humes, J.L., Ihrie, E.J., Lipsky, P.E., and Staruch, M., The four biochemically distinct species of human interleukin I all exhibit similar biological activities, J. Immunol., 134, 895, 1985.

Krakauer, T., Structural analysis of the charge heterogeneity of human interleukin 1, Arch. Biochem. Biophys., 234, 371, 1984.

Lachman, L.B., Hacker, M.P. and Handschumacher, R.E., Partial purification of human lymphocyte-activating factor (LAF) by ultrafiltration and electrophoretic techniques, J. Immunol., 119, 2019, 1977.

March, C.J., Mosley, B., Larsen, A., Cerretti, D.P., Braedt, G., Price, V., Gillis, S., Henney, C.S., Kronheim, S.R., Grabstein, K., Conlon, P.J., Hopp, T.P., and Cosman, D., Cloning, sequence and expression of two distinct human interleukin-1 complementary DNA's, Nature, 315, 641, 1985.

Cameron, P., Limjuco, G., Rodkey, J., Bennet, C., and Schmidt, J.A., Amino acid sequence analysis of human interleukin I (IL-1), J. Exp. Med., 162, 790, 1985.

Dinarello, C.A., Biology of interleukin 1, FASEB J., 2, 108, 1988.

Kurt-Jones, E.A., Kiely, J.M., and Unanue, E.R., Conditions required for expression of membrane IL-1 on B cells, J. Immunol., 135, 1548, 1985.

Oppenheim, J.J., Kovacs, E.J., Matsushima, K., and Durum, S.K., There is more than one interleukin 1, Immunol. Today, 7, 45, 1986.

Lowenthal, J.W. and MacDonald, H.R., Binding and intemalization of interleukin-1 by T cells, J. Exp. Med., 164, 1060, 1987.

Matsushima, K., Yodoi, J., Tagaya, Y., and Oppenheim, J.J., Down regulation of interleukin-1 receptor expression by IL-1 and fate of internalized 125-1 labelled IL-1 beta in a human large granular lymphocyte cell line, J. Immunol., 137, 3183, 1986.

Mizel, S.B., Kilian, P.L., Lewis, J.C., Paganelli, K.A., and Chizzonite, R.A., The interleukin 1 receptor. Dynamics of interleukin I binding and internalization in T cells and fibroblasts, J. Immunol., 138, 2906, 1987.

Dewhirst, F.E., Stashenko, P.P., Mole, J.E., and Tsuromachi, T., Purification and partial sequence of human osteoclast-activating factor: identity with interleukin 1B, J. Immunol., 135, 2562, 1985.

Saklatvala, J., Pilsworth, L.M.C., Sarsfield, S.J., Gavrilovic, J., and Heath, J.K., Pig catabolin is a form of interleukin 1, Biochem. J., 224, 461, 1984.

Matsushima, K., Bano, M., Kidwell, W.R., and Oppenheim, J.J., Interleukin 1 increases collagen type IV production by murine mammary epithelial cells, J. Immunol., 134, 904, 1985.

Byars, N., Schreiber, A.A., Allison, A.B., and Modabber, F., Interleukin-1-containing conditioned media stimulate the proliferation of capillary endothelial cells, Fed. Proc. (Abstr.), 43, 462, 1984.

Berilacqua, M.P., Pober, J.S., Majeau, G.R., Cotran, R.S., and Gimbrone, M.A., Interleukin 1 (IL-1) induces biosynthesis and cell surface expression of procoagulant activity in human vascular endothelial cells, J. Exp. Med., 160, 618, 1984.

Dunn, C.J. and Fleming, W.E., The role of interleukin-1 in the inflammatory response with particular reference to endothelial cellleukocyte adhesion, in The Physiologic, Metabolic, and Immunologic Actions of Interleukin-1, Kluger, M. J., Oppenheim, J. J., and Powanda, M. C., Eds., Alan R. Liss, New York, 1985, 45.

Granstein, R.D., Margolis, R., Mizel, S.B., and Sauder, D.N., Chemotactic activity of epidermal cell derived thymocyte-activating factor (ETAF) and interleukin-1 in a murine model, in The Physiologic, Metabolic, and Immunologic Actions of Interleukin-1, Kluger, M. J., Oppenheim, J. J., and Powanda, M. C., Eds., Alan R. Liss, New York, 1985, 25.

Habicht, G.S. and Beck, G., IL-1 is an endogenous mediator of acute inflammation and of the local Shwartzman reaction, in The Physiologic, Metabolic, and Immunologic Actions of Interleukin-1, Kluger, M. J., Oppenheim, J. J., and Powanda, M. C., Eds., Alan R. Liss, New York, 1985, 13.

Mackiewicz, A., Ganapathi, K., Schultz, D., Samols, D., Reese, J., and Kushner, I., Regulation of rabbit acute phase protein biosynthesis by monokines, Biochem. J., 253, 851, 1981.

Pierce, G.F., Mustoe, T.A., Lingelbach, J., Masakowski, V.R., Gramates, P., and Deuel, T.F., Transforming growth factor B reverses the glucocorticoid-induced wound-healing deficit in rats: possible regulation in macrophages by platelet-derived growth factor, Proc. Natl. Acad. Sci. U.S.A., 86, 2229, 1989.