Ritossa, F.M., A new puffing pattern induced by heat shock and DNP in Drosophilia, Experimentia, 18, 571, 1962.
2.
Ritossa, F.M., Experimental activation of specific loci in polytene chromosomes of Drosophilia, Exp. Cell Res., 36, 515, 1964.
3.
Tissieres, A., Mitchell, H.K., and Tracy, U.M., Protein synthesis in salivary glands of Drosophilia melanogaster: relation to chromosome puffs, J. Mol. Biol., 84, 389, 1974.
Lindquist, S. and Craig, E.A., The heat-shock proteins, Annu. Rev. Genet., 22, 631, 1989.
6.
Subjeck, J.R., Shyy, T., Shen, J., and Johnson, R.J., Association between the mammalian 110,000-dalton heat-shock protein and nucleoli, J. Cell Biol., 97, 1389, 1983.
7.
Shyy, T-T., Subjeck, J.R., Heinaman, R., and Anderson, G., Effect of growth state and heat shock on nucleolar localization of the 110,000-Da heat shock protein in mouse embryo fibroblasts, Cancer Res., 36, 4738, 1986.
8.
Welch, W.J. and Suhan, J.P., Cellular and biochemical events in mammalian cells during and after recovery from physiological stress, J. Cell Biol., 103, 2035, 1986.
9.
Nover, L., Munsche, D., Neumann, D., Ohme, K., and Schraf, K.D., Control of ribosome biosynthesis in plant cells cultures under heat-shock conditions. Ribosomal RNA, Eur. J. Biochem., 160, 297, 1986.
10.
Bar dwell, J.C.A. and Craig, E.A., Ancient heat shock gene is dispensible, J. Bacteriol., 7, 2977, 1988.
11.
Dragon, E.A., Sias, S.R., Kato, E.A., and Gabe, J.D., The genome of Trypanosoma cruzi contains a constitutively expressed, tandemly arranged multicopy gene homologous to a major heat shock protein, J. Biol. Chem., 259, 11882, 1984.
12.
Farrelly, F.W. and Finkelstein, D.B., Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae, J. Biol. Chem., 9, 5745, 1984.
13.
Marrarella, R.A. and Green, M., ERp99, an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90-kDa heat shock protein (hsp90) and the 94-kDa glucose regulated protein (grp94), J. Biol. Chem., 262, 8875, 1987.
14.
Blackman, R.K. and Meselson, M., Interspecific nucleotide sequence comparisons used to identify regulatory and structural features of the Drosophilia hsp82 gene, J. Mol. Biol., 188, 499, 1986.
15.
Kulomaa, M.S., Weigel, N.L., Kleinsek, D.A., Beattie, W.G., Conneely, O.M. et al., Amino acid sequence of a chicken heat shock protein derived from the complementary DNA nucleotide sequence, Biochemistry, 25, 6244, 1986.
16.
Moore, S.K., Kozak, C., Robinson, E.A., Ullrich, S.J., and Apella, E., Cloning and nucleotide sequence of the murine hsp84 cDNA and chromosome assignment of related sequences, Gene, 56, 29, 1987.
17.
Sorger, P.K. and Pelham, H.R.B., The glucose-regulated protein grp94 is related to heat shock protein hsp90, J. Mol. Biol., 194, 341, 1987.
18.
Carbajal, M.E., Duband, J.L., Lettre, F., Valet, J.P., and Tanguay, R.M., Cellular localization of Drosophilia 83-kilodalton heat shock protein in normal, heat shocked, and recovering cultured cells with a specific antibody, Biochem. Cell Biol., 64, 816, 1986.
19.
Collier, N.C. and Schlesinger, M.J., The dynamic state of heat shock proteins in chicken embryo fibroblasts, J. Cell Biol., 103, 1495, 1986.
20.
Lai, B.T., Chin, N.W., Stanek, A.E., Keh, W., and Lanks, K.W., Quantitation and intracellular localization of the 85 kDa heat shock protein by using monoclonal and polyclonal antibodies, Mol. Cell. Biol., 4, 2802, 1984.
21.
van Bergen en Henegouwen, P.M.P., Berbers, G., Linnemans, W.A.M., and van Wijk, R., Subcellular localization of the 84,000 dalton heat-shock protein in mouse neuroblastoma cells: evidence for a cytoplasmic and nuclear location, Eur. J. Cell Biol., 43, 469, 1987.
22.
Munro, S. and Pelham, H.R.B., A C-terminal signal prevents secretion of luminal ER proteins, Cell, 48, 899, 1987.
23.
Sciandra, J.J. and Subjeck, J.R., The effects of glucose on protein synthesis and thermosensitivity in Chinese hamster ovary cells, J. Biol. Chem., 258, 12091, 1983.
24.
Shiu, R.P.C., Pouyssegur, J., and Pastan, I., Glucose depletion accounts for the induction of two transformation sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts, Proc. Natl. Acad. Sci. U.S.A., 74, 3840, 1977.
25.
Liu, A.Y.-C., Bae-Lee, M.S., Choi, H.-S., and Li, B., Heat shock of Hsp89 is regulated in cellular aging, Biochem. Biophys. Res. Commun., 162, 1302, 1989.
26.
Yufu, Y., Nishimura, J., Takahira, H., Ideguchi, H., and Nawata, H., Down-regulation of a M, 90,000 heat shock cognate protein during granulocytic differentiation in HL-60 human leukemia cells, Cancer Res., 49, 2405, 1989.
27.
Dougherty, J.J., Puri, R.K., and Toft, D.O., Polypeptide components of two 8 S forms of chicken oviduct progesterone receptor, J. Biol. Chem., 259, 8004, 1984.
28.
Joab, I., Radanyi, C., Renoir, M., Buchou, T., Catelli, M-G. et al., Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones, Nature, 308, 850, 1984.
29.
Redeuilh, G., Moncharmont, B., Secco, C., and Bautieu, E-E., Subunit composition of the molybdate-stabilized "8-9S" nontransformed estradiol receptor purified from calf uterus, J. Biol. Chem., 262, 6969, 1987.
30.
Renoir, J-M., Buchou, T., and Baulieu, E-E., Involvement of a non-hormone-binding 90-kilodalton protein in the nontransformed 8S form of the rabbit uterus progesterone receptor, Biochemistry, 25, 6405, 1986.
31.
Sanchez, E.R., Housley, P.R., and Pratt, W.B., The molybdate-stabilized glucocorticoid binding complex of L-cells contains a 98-100 kDa steroid binding phosphoprotein and a 90 kDa nonsteroid-binding phosphoprotein that is part of the murine heat-shock complex, J. Steroid Biochem., 24,9, 1986.
32.
Sanchez, E.R., Meschinchi, S., Tienrungroj, W., Schlesinger, M.J., Toft, D.O., and Pratt, W.B., Relationship of the 90-kDa murine heat shock protein to the untransformed and transformed states of the L cell glucocorticoid receptor, J. Biol. Chem., 262, 6986, 1987.
33.
Picard, D., Salser, S.J., and Yamamoto, K.R., A moveable and regulable inactivation function within the steroid-binding domain of the glucocorticoid receptor, Cell, 54, 1073, 1988.
34.
Brugge, J.S., Erikson, E., and Erikson, R.L., The specific interaction of the Rous sarcoma virus transforming protein, pp60snc,with two cellular proteins, Cell, 25, 363, 1981.
35.
Oppermann, H., Levinson, W., and Bishop, J.M., A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein, Proc. Natl. Acad. Sci. U.S.A., 78, 1067, 1981.
36.
Brugge, J.S., Yuonemoto, W., and Darrow, D., Interaction between the Rouse sarcoma virus transforming protein and two subcellular phosphoproteins: analysis of the turnover and distribution of this complex, Mol. Cell. Biol., 4, 2697, 1983.
37.
Courtneidge, S.A. and Bishop, J.M., Transit of pp60src to the plasma membrane, Proc. Natl. Acad. Sci. U.S.A., 79, 7117, 1982.
38.
Adkins, B., Hunter, T., and Sefton, B.M., The transforming proteins of PRCII virus and Rous sarcoma virus form a complex with the same two cellular phosphoproteins, J. Virol., 43, 448, 1982.
39.
Lipsich, L.A., Cutt, J.R., and Brugge, J.S., Association of the transforming proteins of Rous, Fujinami, and Y73 avian sarcoma viruses with the same two cellular proteins, Mol. Cell. Biol., 2, 875, 1982.
40.
Ziemiecki, A., Characterization of the monomeric and complex-associated forms of the gag-onc fusion proteins of three isolates of feline sarcoma virus: phosphorylation, kinase activity, acylation, and kinetics of complex formation, Virology, 151, 265, 1986.
41.
Koyasu, S., Nishida, E., Kadowaki, T., Matsuzaki, F., Iida, K. et al., Two mammalian heat shock proteins, HSP90 and HSP100, are actin binding proteins, Proc. Natl. Acad. Sci. U.S.A., 83, 8054, 1983.
42.
Nishida, E., Koyasu, S., Sakai, H., and Yahara, I., Calmodulinregulated binding of the 90-kDA heat-shock protein to actin filaments, J. Biol. Chem., 261, 16033, 1986.
43.
Minota, S., Koyasu, S., Yahara, I., and Winfield, J., Autoantibodies to the heat-shock hsp90 in systemic lupus erythematosus, J. Clin. lnvest., 81, 106, 1988.
44.
Minota, S., Cameron, B., Welch, W.J., and Winfield, J.B., Autoantibodies to the constitutive 73-kDa member of the hsp70 family of heat shock proteins in systemic lupus erythematosus, J. Exp. Med., 168, 1475, 1988.
45.
Norton, P., Isenberg, D.A., and Latchman, D.S., Elevated levels of the 90kDa heat shock protein in a proportion of SLE patients with active disease, J. Autoimmun., 2, 187, 1989.
46.
Lathangue, N.B. and Latchman, D.S., A cellular protein related to heat-shock protein 90 accumulates during herpes simplex infection and is overexpressed in transformed cells, Exp. Cell Res., 178, 169, 1988.
47.
Young, R.A. and Elliott, T.J., Stress proteins, infection, and immune surveillance, Cell, 59, 5, 1989.
48.
Chappell, T.G., Welch, W.J., Schlossman, D.M., Palter, K.B., Schlesinger, M.J., and Rothman, J.E., Uncoating ATPase is a member of the 70 kilodalton family of stress proteins, Cell, 45, 3, 1986.
49.
Welch, W.J. and Feramisco, J.R., Rapid purification of mammalian 70,000-dalton stress proteins: affinity of the proteins of nucleotides, Mol. Cell. Biol., 5, 1229, 1985.
50.
Zylicz, M., LeBowitz, J.H., McMacken, R., and Georgopoulos, C.P., The dnaK protein of Escherichia coli processes an ATPase and autophosphorylating activity and is essential to an in vitro DNA replication system, Proc. Natl. Acad. Sci. U.S.A., 80, 6431, 1983.
51.
Mues, G.I., Munn, T.Z., and Raese, J.D., A human gene family with sequence homology to Drosophila melanogaster Hsp70 heat shock gene, J. Biol. Chem., 26, 874, 1986.
52.
Welch, W.J. and Feramisco, J.R., Nuclear and nucleolar localization of the 72,000-dalton heat shock in heat shocked mammalian cells, J. Biol. Chem., 259, 4501, 1984.
53.
Pelham, H.R.B., HSP70 accelerates the recovery of nucleolar morphology after heat shock, EMBO. J., 3, 3095, 1984.
54.
White, F. and Currie, R.W., A mammalian response to trauma: the synthesis of a 71-kDa protein, in Heat Shock: From Bacteria to Man, Schlesinger, M. J., Ashbumer, M., and Tissieres, A., Eds., Cold Spring Harbor Laboratory, New York, 1982, 379.
55.
Lowe, D.G. and Moran, L.A., Molecular-cloning and analysis of DNA complementary to three mouse M, = 68,000 heat-shock protein mRNAs, J. Biol. Chem., 261, 2102, 1986.
56.
Milarski, K.L. and Morimoto, R., Expression of human HSP70 during the synthetic phase of the cell cycle, Proc. Natl. Acad. Sci. U.S.A., 83, 9517, 1986.
57.
Munro, S. and Pelham, H., An hsp70-like protein in the ER: identity with the 78 kDa glucose-regulated protein and immunoglobulin heavy chain binding protein, Cell, 46, 291, 1986.
58.
Ungewickell, E., The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelion from coated vesicles, EMBO J., 4, 3385, 1985.
59.
Schlossman, D.M., Schmid, S.L., Braell, W.A., and Rothman, J.E., An enzyme that removes clathrin coats: purification of an uncoating ATPase, J. Cell Biol., 99, 723, 1984.
60.
Finley, D., Crechanover, A., and Varshavsky, A., Thermolability of ubiquitin-activating enzyme from the mammalian cell cycle mutant ts85, Cell, 37, 43, 1984.
61.
Pelham, H.R.B., Speculations on the functions of the major heat shock and glucose-regulated proteins, Cell, 46, 959, 1986.
62.
Chiang, H.L., Terlecky, S.R., Plant, C.P., and Dice, J.F., A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins, Science, 246, 382, 1989.
63.
Hinds, P.W., Finlay, C.A., Frey, A.B., and Levine, A.J., Immunological evidence for the association of p53 with a heat protein, hsc70, in p53-plus-ras-transformed cell lines, Mol. Cell. Biol., 7, 2863, 1987.
64.
Pinhasi-Kimhi, O., Michalovitz, D., Ben-Zeev, A., and Oren, M., Specific interaction between the p53 cellular tumour antigen and major heat shock proteins, Nature, 320, 182, 1986.
65.
Pedersen, R.C. and Brownie, A.C., Steroidogenesis-activator polypeptide isolated from a rat leydig cell tumor, Science, 236, 188, 1987.
66.
Guidon, P.T. and Hightower, L.E., Purification and initial characterization of the 71-kilodalton rat heat-shock protein and its cognate as fatty acid binding proteins, Biochemistry, 25, 3231, 1986.
67.
Dura, J.M., Stage dependent synthesis of heat shock induced protein in early embryos of Drosophila melanogaster, Mol. Gen. Genet., 184, 381, 1981.
68.
Graziosi, G., Micali, F., Marzari, R., de Christini, F., and Savoini, A., Variability of response of early Drosophila embryos to heat shock, J. Exp. Zool., 214, 141, 1980.
69.
Bienz, M., Developmental control of the heat shock response in Xenopus, Dev. Biol., 81, 3138, 1984.
70.
Bensaude, O., Babinet, C., Morange, M., and Jacob, F., Heat shock proteins, first major products of zygotic gene activity in mouse embryo, Nature (London), 305, 331, 1983.
71.
Bensaude, O. and Morange, M., Spontaneous high expression of heat-shock proteins in mouse embryonal carcinoma cells and ectoderm from day 8 mouse embryo, EMBO. J., 2, 173, 1983.
72.
Kothary, R., Perry, M.D., Moran, L.A., and Rossant, J., Cell-lineage-specific expression of the mouse hsp68 gene during embryogenesis, Dev. Biol., 121, 342, 1987.
73.
Krawczyk, Z., Wisniewski, J., and Biesiada, I., Expression of hsp70-related gene in developing and degenerating rat testis, Mol. Biol. Rep., 12, 35, 1987.
74.
Zakeri, Z.F. and Wolgemuth, D.J., Developmental-stage-specific expression of the hsp70 gene family during differentiation of the mammalian male germ line, Mol. Cell. Biol., 7, 1791, 1987.
75.
Zakeri, Z.F., Wolgemuth, D.J., and Hunt, C.R., Identification and sequence analysis of a new member of the mouse hsp70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line, Mol. Cell. Biol., 8, 2925, 1988.
76.
Zakeri, Z.F. and Wolgemuth, D.J., Developmental-stage-specific expression of the hsp70 gene family during differentiation of the mammalian male germ line, Mol. Cell. Biol., 7, 1791, 1987.
77.
Young, D.B., Lathigra, R., and Mehlert, A., Stress-Induced Proteins, Pardue, M. L., Feramisco, J. R., and Lindquist, S., Eds., Alan R. Liss, New York, 1989, 275.
78.
Lamb, J.R., Bal, V., Rothbard, J.B., Mehlert, A., Mendez-Samperio, P., and Young, D.B., The mycobacterium Gro EL stress protein - a common target of T-cell recognition in infection and immunity, Jol. Autoimmun., 2, 93, 1989.
79.
Sargent, C.A., Dunham, I., Trowsdale, J., and Campbell, R.D., Human major histocompatibility complex contains genes for the major heat shock protein hsp70, Proc. Natl. Acad. Sci. U.S.A., 86, 1968, 1989.
80.
Vokes, E.E., Golomb, H.M., Samuels, B.L., and Brownstein, B.H., Heat shock proteins in normal and leukemic blood cells, J. lnterferon Res., 9, 195, 1989.
81.
Aujame, L. and Firko, H., The major inducible heat shock protein hsp68 is not required for acquisition of thermal resistance in mouse plasmacytoma cell lines, Mol. Cell. Biol., 8, 5486, 1988.
82.
Mivechi, N.F., Heat sensitivity, thermotolerance, and profile of heat shock protein synthesis of human myelogenous leukemias, Cancer Res., 49, 1954, 1989.
83.
McMullin, T.W. and Hallberg, K.L., A normal mitochondrial protein is selectively synthesized and accumulated during heat shock in Tetrahymena thermophila, Mol. Cell. Biol., 7, 4414, 1987.
84.
McMullin, T.W. and Hallberg, R.L., A highly evolutionary conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli Gro EL gene, Mol. Cell. Biol., 8, 371, 1988.
85.
Georgopoulos, C.P., Hendrix, R.W., Casjens, S.R., and Kaiser, A.D., Host participation in bacteriophage lambda head assembly, J. Mol. Biol., 76, 45, 1973.
86.
Hendrix, R.W., Purification and properties of GroE, a host protein involved in bacteriophage assembly, J. Mol. Biol., 129, 375, 1979.
87.
Hemmingsen, S.M., Woolford, C., van der Vies, S.M., Tilly, K., Dennis, D.T., Georgopoulos, C.P., Hendrix, R.W., and Ellis, R.J., Homologous plant and bacterial proteins chaperone oligomeric protein assembly, Nature, 333, 330, 1988.
88.
Shinnick, T.M., Vodkin, M.H., and Williams, J.C., The mycobacterium tuberculosis 65-kilodalton antigen is a heat shock protein which corresponds to a common antigen and to the Escherichia coli and GroEL protein, Infect. Immun., 56, 446, 1988.
89.
Young, D., Lathigra, R., Hendrix, R., Sweetser, D., and Young, R.A., Stree protein are immune targets in leprosy and tuberculosis, Proc. Natl. Acad. Sci. U.S.A., 85, 4267, 1988.
90.
Shinnick, T.M., Plikaytis, B.B., Hyche, A.D., Van Landingham, R.M., and Walker, L.L., The mycobacterium tuberculosis BCG-A protein that has homology with Escherichia coli GroES protein, Nucl. Acids Res., 17, 1254, 1989.
91.
Van Eden, W., Thole, J.E.R., van der Zee, R. et al., Cloning of the mycobacterial epitope recognized by T lymphocytes in adjuvant arthritis, Nature, 331, 171, 1988.
92.
Liden, O., Karin, N., Shinitzky, M., and Cohen, I.R., Therapeutic vaccination against adjuvant arthritis using autoimmune T-cells treated with hydrostatic pressure, Proc. Natl. Acad. Sci. U.S.A., 84, 4577, 1987.
93.
Gaston, J.S.H., Life, P.F., Bailey, L., and Bacon, P.A., Synovial fluid T cells and 65 kDa heat-shock protein, Lancet, 2, 856, 1988.
94.
Tsoulfa, G., Rook, G.A.W., Van-Embden, J.D.A. et al., Raised serum IgG and IgA antibodies to mycobacterial antigens in rheumatoid arthritis, Ann. Rheum. Dis., 48, 118, 1989.
95.
Koga, T., Wand-Wurttenberger, A., DeBruyn, J., Munk, M.E., Schoel, B., and Kaufmann, S.H.E., T cell against a bacterial heat shock protein recognize stressed macrophages, Science, 245, 1112, 1989.
96.
Nagata, K., Saga, S., and Yamada, K.M., A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein, J. Cell Biol., 103, 223, 1986.
97.
Sauk, J.J., Norris, K., Moehring, J., Foster, R.A., and Somerman, M.J., Colligin/HSP47 is expressed after diverse forms of stress in fibroblasts derived from human periodontal ligaments in vitro, Arch. Oral Biol., submitted.
98.
Nagata, K. and Yamada, K.M., Phosphorylation and transformation sensitivity of a major collagen-binding protein of fibroblasts, J. Biol. Chem., 261, 7531, 1986.
99.
Kurkinen, M.A., Taylor, A., Garrels, J.I., and Hogan, B.L.M., Cell surface-associated proteins which bind native type IV collagen or gelatin, J. Biol. Chem., 259, 5915, 1984.
100.
Saga, S., Nagata, K., Chen, W.T., and Yamada, K.M., Phdependent function, purification, and intracellular location of a major collagen-binding glycoprotein, J. Cell Biol., 105, 517, 1987.
101.
Hughes, R.C., Taylor, A., Sage, H., and Hogan, B.L.M., Distinct patterns of glycosylation of colligin, a collagen-binding glycoprotein, and SPARC (osteonectin), a secreted Ca2+-binding glycoprotein: evidence for the localization of colligin in the endoplasmic reticulum, Eur. J. Biochem., 163, 57, 1987.
102.
Veis, A., Leibovich, S.J., Evans, J., and Kirk, T.Z., Supramolecular assemblies of mRNA direct the coordinate synthesis of type I procollagen chains, Proc. Natl. Acad. Sci. U.S.A., 82, 3693, 1985.
103.
Kirk, T.Z., Evans, J.S., and Veis, A., Biosynthesis of type I procollagen, J. Biol. Chem., 262, 5540, 1987.
104.
Veis, A. and Kirk, T.Z., The coordinate synthesis and cotranslational assembly of type I procollagen, J. Biol. Chem., 264, 3884, 1989.
105.
Nene, V., Dunne, D.W., Johnson, K.W., Taylor, D.W., and Cordingley, J.S., Sequence and expression of major egg antigen from Schistosoma mansoni. Homologies to heat shock proteins and alphacrystallins, Mol. Biochem. Parasitol., 21, 179, 1986.
106.
Rossi, J. and Lindquist, S., Intracellular location of hsp26 in yeast cells varies with metabolism, J. Cell Biol., 108, 425, 1989.
107.
Bloemendal, H., Berns, T., Zweers, A., Hoenders, H., and Benedetti, E.L., The state of aggregation of a-crystallin detected after large-sclae preparation by zonal centrifugation, Eur. J. Biochem., 24, 401, 1972.
108.
Ingolia, T.D. and Craig, E.A., Four small Drosophila heat shock proteins are related to each other and to mammalian a-crystallin, Proc. Natl. Acad. Sci. U.S.A., 79, 2360, 1982.
109.
Arrigo, A.-P. and Welch, W.J., Characterization and purification of the small 28000-dalton mammalian heat shock protein, J. Biol. Chem., 262, 15359, 1987.
110.
Nover, L., Scharf, K.D., and Neumann, D., Cytoplasmic heat shock granules are formed from precursor particles and contain a specific set of mRNAs, Mol. Cell. Biol., 9, 1298, 1989.
111.
Schuldt, C. and Kloetzel, B.M., Analysis of cytoplasmic 19S ring-type particles in Drosophila which contain hsp23 at normal growth temperature, Dev. Biol., 11, 65, 1985.
112.
Vierling, E., Nagao, K.I., DeRocher, A.E., and Harris, L.M., A heat shock protein localized to chloroplasts is a member of a eukaryotic superfamily of heat shock proteins, EMBO J., 7, 575, 1988.
113.
Collier, N.C., Heuser, J., Levy, M.A., and Schlesinger, M.J., Ultrastructural and biochemical analysis of the stress granule in chicken embryo fibroblasts, J. Cell Biol., 106, 1131, 1988.
114.
Neumann, D., zur Nieden, U., Mateuffel, R., Walter, G., Scharf, K.-D., and Nover, L., Intracellular localization of heat-shock proteins in tomato cell cultures, Eur. J. Cell Biol., 43, 71, 1987.
115.
Glaser, R.L., Wolfner, M.F., and Lis, J.T., Spatial and temporal pattern of HSP26 expression during normal development, EMBO J., 5, 747, 1986.
116.
Berger, E.M. and Woodward, M.P., Small heat shock proteins in Drosophila may confer thermal tolerance, Exp. Cell Res., 147, 437, 1983.
117.
Thomas, S.R. and Lengyel, J.A., Ecdysteroid-regulated heat-shock gene expression during Drosophila melanogaster development, J. Cell. Physiol., 127,451, 1986.
118.
Zimmerman, J.L., Petri, W.L., and Meselson, M., Accumulation of specific subsets of D. melanogaster heat shock mRNAs in normal development without heat shock, Cell, 32, 1161, 1983.
119.
Ayme, A. and Tissieres, A., Locus 67B of Drosophila melanogaster contains seven, not four, closely related heat shock genes, EMBO J., 4, 2949, 1985.
120.
Cheney, C.M. and Shearn, A., Developmental regulation of Drosophila disc proteins: synthesis of a heat shock protein under non-heat shock conditions, Dev. Biol., 95, 325, 1983.
121.
Joab, I., Kadanyl, C., Renoir, M., Buchou, T., Catelli, M.-G. et al., Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones, Nature, 308, 850, 1984.
122.
Landry, J., Chretien, P., Lambert, H., Hickey, E., and Weber, L.A., Heat shock resistance conferred by expression of the human hsp27 gene in rodent cells, J. Cell Biol., 109, 7, 1989.
123.
Eissenberg, J.C. and Elgin, S.C.R., Hsp28: a P-element insertion mutation that alters the expression of a heat shock gene in Drosophila melanogaster, Genetics, 115, 333, 1987.
124.
McGarry, T.J. and Lindquist, S., Inhibition of heat-shock protein-synthesis by heat-inducible antisense RNA, Proc. Natl. Acad. Sci. U.S.A., 83, 399, 1986.
125.
Sirotkin, K., Bartley, N., Perry, W.L., Briggs, D., Grell, E.H. et al., Deletion polymorphism in a Drosophila melanogaster heat shock gene, Mol. Gen. Genet., 204, 266, 1986.
126.
Termine, J.D., Kleinman, H.K., Whitson, S.W., Conn, K.M., McGarvey, M.L., and Martin, G.R., Osteonectin, a bone-specific protein linking mineral to collagen, Cell, 26, 99, 1981.
127.
Fisher, L.W., Hawkin, G.R., Tuross, N., and Termine, J.D., Purification and partial characterization of small proteoglycans I and II, bone sialoproteins I and II, and osteonectin from the mineral compartment of developing human bone, J. Biol. Chem., 262, 9702, 1987.
128.
Bianco, P., Hayashi, Y., Silvestrini, G., Termine, J.D., and Bonucci, E., Osteonectin and GLA-protein in calf bone: ultrastructural immunohistochemical localization using the protein A-gold method, Calcif. Tissue Int., 37, 684, 1985.
129.
Otsuka, K., Yao, K.-L., Wasi, S., Tung, P.S., Aubin, J.E., Sodek, J., and Termine, J.D., Biosynthesis of osteonectin by fetal porcine calvarial cells, in vitro, J. Biol. Chem., 259, 9805, 1984.
130.
Wasi, S., Otsuka, K., Yao, K.-L., Tung, P.S., Aubin, J.E., Sodek, J., and Termine, J.D., An osteonectin-like protein in porcine periodontal ligament and its synthesis by periodontal ligament fibroblasts, Biochem. Cell Biol., 62, 470, 1984.
131.
Mason, I.J., Taylor, A., Williams, J.G., Sage, H., and Hogan, B., Evidence from molecular cloning that SPARC a major product of mouse embryo parietal endoderm, is related to an endothelial cell "culture shock" glycoprotein, EMBO J., 5, 1465, 1986.
132.
Stenner, D.D., Tracy, R.P., Riggs, B.L., and Mann, K.G., Human platelets contain and secrete osteonectin, a major protein of mineralized bone, Proc. Natl. Acad. Sci. U.S.A., 83, 6892, 1986.
133.
Young, M.F., Bolander, M.E., Day, A.A., Ramis, C.I., Robey, P.G., Yamada, Y., and Termine, J.D., Osteonectin mRNA: Distribution in normal and transformed cells, Nucleic Acids Res., 14, 4483, 1986.
134.
Zung, P., Domenicucci, C., Wasi, S., Kuwata, F., and Sodek, J., Osteonectin is a minor component of mineralized connective tissues in rat, Biochem. Cell Biol., 64, 356, 1986.
135.
Bolander, M.E., Young, M.F., Fisher, L.W., Yamada, Y., and Termine, J.D., Osteonectin cDNA sequence reveals potential binding regions for calcium and hydroxyapatite and shows homologies with both a basement membrane protein (SPARC) and a serine proteinase inhibitor (ovomucoid), Proc. Natl. Acad. Sci. U.S.A., 85, 2919, 1988.
136.
Sage, H., Pritzl, P., and Bornstein, P., Secretory phenotypes of endothelial cells in culture: a comparison of aortic, venous, capillary, and corneal endothelium, Arteriosclerosis, 1, 427, 1981.
137.
Dziadek, M., Paulsson, M., Aumailley, M., and Timpl, R., Purification and tissue distribution of a small protein (BM-40) extracted from a basement membrane tumor, Eur. J. Biochem., 161, 455, 1986.
138.
Mann, K., Deutzmann, R., Paulsson, M., and Timpl, R., Solubilization of protein BM-40 from a basement membrane tumor with chelating agents evidence for its identity with osteonectin and SPARC, FEBS Lett., 218, 167, 1987.
139.
Sage, H., Johnson, C., and Bornstein, P., Characterization of a novel albumin-binding glycoprotein secreted by endothelial cells in culture, J. Biol. Chem., 259, 3993, 1984.
140.
Sage, H., Vernon, R.B., Funk, S.E., Everitt, E.A., and Angello, J., SPARC, a secreted protein associated with cellular proliferation, inhibits cell spreading in vitro and exhibits Ca+2-dependent binding to the extracellular matrix, J. Cell Biol., 109, 341, 1989.
141.
Mason, I.J., Murphy, D., Munke, M., Francke, U., Elliott, R., and Hogan, B.L.M., Developmental and transformation-sensitive expression of the SPARC gene on mouse chromosome 11, EMBO J., 5, 1831, 1986.
142.
Sage, H., Tupper, J., and Bramson, R., Endothelial injury in vitro is associated with increase secretion of an M, 43,000 glycoprotein ligand, J. Cell Physiol., 127, 373, 1986.
143.
Holland, P., Harper, S., McVey, J., and Hogan, B.L.M., In vivo expression of mRNA for the Ca+2 binding protein SPARC (osteonectin) revealed by in situ hybridization, J. Cell Biol., 105, 473, 1987.
144.
Metsaranta, M., Young, M.F., Sandberg, M., Termine, J., and Vuorio, E., Localization of osteonectin expression in human fetal skeletal tissues by in situ hybridization, Calcif. Tissue Int., 45, 146, 1989.
145.
Fujisawa, R. and Kuboki, Y., Changes in levels of osteonectin in bovine dentine during tooth development, Arch. Oral Biol., 34, 89, 1989.
146.
Jundt, G., Schulz, A., Berghauser, K.H., Fisher, L.W., Gehron-Robey, P., and Termine, J.D., Immunocytochemical identification of osteogenic bone tumors by osteonectin antibodies, Virchows Arch. Pathol. Anat. Histopathol., 414, 345, 1989.
147.
McVey, J.H., Nomura, S., Kelly, P., Mason, I.J., and Hogan, B.L.M., Characterization of the mouse SPARC/osteonectin gene. Intron/exon organization and an unusual promoter region, J. Biol. Chem., 263, 11111, 1988.
148.
Findlay, D.M., Fisher, L.W., McQuillan, C.L., Termine, J.D., and Young, M., Isolation of the osteonectin gene: evidence that a variable region of the osteonectin molecule is encoded within one exon, Biochemistry, 27, 1483, 1988.
149.
Young, M., Findlay, D.M., Dominguez, P., Burbelo, P.D., McQuillan, C., Kopp, J., Gehron-Robey, P., and Termine, J.D., Osteonectin promoter: DNA sequence analysis and S1 endonuclease site potentially associated with transcriptional control in bone cells, J. Biol. Chem., 264, 450, 1989.
150.
Noda, M. and Rodan, G.A., Type B transforming factor (TGF beta) regulation of alkaline phosphatase expression and other phenotype-related mRNAs in osteoblastic rat osteosarcoma cells, J. Cell. Physiol., 133, 426, 1987.
151.
Kaesberg, P.R., Ershler, W.B., Esko, J.D., and Mosher, D.F., Chinese hamster ovary cell adhesion to human platelet thrombospondin is dependent on cell surface heparan sulfate proteoglycan, J. Clin. Invest., 83, 994, 1989.
152.
Murphy-Ullrich, J.E. and Mosher, D.F., Interactions of thrombospondin with endothelial cells: receptor-mediated binding and degradation, J. Cell Biol., 105, 1603, 1987.
153.
Murphy-Ullrich, J.E., Westrick, L.G., Esko, J.D., and Mosher, D.F., Altered metabolism of thrombospondin by Chinese hamster ovary cells defective in glycosaminoglycan synthesis, J. Biol. Chem., 263, 6400, 1988.
154.
Roberts, D.D., Interactions of thrombospondin with sulfated glycolipids and proteoglycans of human melanoma cells, Cancer Res., 48, 6785, 1988.
155.
Sun, X., Mosher, D.F., and Rapraeger, A., Heparan sulfate-mediated binding of epithelial cell surface proteoglycan to thrombospondin, J. Biol. Chem., 264, 2885, 1989.
156.
Lawler, J. and Hynes, R. 0., The structure of human thrombospondin, an adhesive glycoprotein with multiple calcum-binding sites and homologies with several different proteins, J. Cell Biol., 103, 1635, 1986.
157.
Lawler, J., Weinstein, R., and Hynes, R. 0., Cell attachment to thrombospondin: the role of arg-gly-asp, calcium, and integrin receptors, J. Cell Biol., 107, 2351, 1988.
158.
Riser, B.L., Varani, J., O'Rourke, K., and Dixit, V.M., Thrombospondin binding by human squamous carcinoma and melanoma cells: relationship to biological activity, Exp. Cell Res., 174, 319, 1988.
159.
Roberts, D.D., Sherwood, J.A., and Ginsburg, V., Platelet thrombospondin mediates attachment and spreading of human melanoma cells, J. Cell Biol., 104, 131, 1987.
160.
Varani, J., Dixit, V.M., Fliegel, S.E.G., McKeever, P.E., and Carey, T.E., Thrombospondin-induced attachment and spreading of human squamous carcinoma cells, Exp. Cell Res., 167, 376, 1986.
161.
Varani, J., Nickoloff, B.J., Riser, B.L., Mitra, R.S., O'Rourke, K., and Dixit, V.M., Thrombospondin-induced adhesion of keratinocytes, J. Clin. Invest., 81, 1537, 1988.
162.
Ullrich, J.E.M. and Hook, M., Thrombospondin modulates focal adhesions in endothelial cells, J. Cell Biol., 109, 1309, 1989.
163.
Ketis, N.V., Lawler, J., Hoover, R.L., and Karnovsky, M.J., Effects of heat shock on the expression of thrombospondin by endothelial cells, J. Cell Biol., 106, 893, 1988.
164.
Phan, S.H., Dillon, R.G., McGarry, B.M., and Dixit, V.M., Stimulation of fibroblast proliferation by thrombospondin, Biochem. Biophys. Res. Commun., 163, 56, 1989.
165.
Sage, H., Vernon, R.B., Decker, J., Funk, S., and Iruelaarispe, M.L., Distribution of the calcium-binding protein SPARC in tissues of embryonic and adult mice, J. Histochem. Cytochem., 37, 819, 1989.
166.
Oshea, K.S. and Dixit, V.M., Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo, J. Cell Biol., 107, 2737, 1988.
167.
Kieffer, N., Bettaieb, A., Legrand, C., Coulombel, L., Vainchenker, W., Edelman, L., and Bretongorius, J., Developmentally regulated expression of a 78 kDa erythroblast membrane glycoprotein immunologically related to the platelet thrombospondin receptor, Biochem. J., 262, 835, 1989.
168.
Varani, J., Nickoloff, B.J., Dixit, V.M., Mitra, R.S., and Voorhees, J.J., All-trans retinoic acid stimulates growth of adult human keratinocytes cultured in growth factor-deficient medium, inhibits production of thrombospondin and fibronectin, and reduces adhesion, J. Invest. Dermatol, 93, 449, 1989.
169.
Clezardin, P., Jouishomme, H., Chavassieux, P., and Marie, P.J., Thrombospondin is synthesized and secreted by human osteoblasts and osteosarcoma cells - a model to study the different effects of thrombospondin in cell adhesion, Eur. J. Biochem., 181, 721, 1989.
170.
Robey, P.G., Young, M.F., Fisher, L.W., and McClain, T.D., Thrombospondin is an osteoblast-derived component of mineralized extracellular matrix, J. Cell Biol., 108, 719, 1989.
171.
Kreis, C., Lafleur, M., Menard, C., Paquin, R., and Beaulieu, A.D., Thrombospondin and fibronectin are synthesized by neutrophils in human inflammatory joint disease and in a rabbit model of in vivo neutrophil activation, J. Immunol., 143, 1961, 1989.
172.
Apelgren, L.D. and Bumol, T.F., Biosynthesis and secretion of thrombospondin in human melanoma cells, Cell Biol. Int. Rep., 13, 189, 1989.
173.
Varani, J., Riser, B.L., Hughes, L.A., Carey, T.E., Fligiel, S.E.G., and Dixit, V.M., Characterization of thrombospondin synthesis, secretion and cell surface expression by human tumor cells, Clin. Exp. Met., 7, 265, 1989.
174.
Imamura, N., Inada, T., Mtasiwa, D.M., and Kuramoto, A., Demonstration of thrombospondin (TSP) receptor on the cell surface of acute megakaryoblastic leukemia, Am. J. Hematol., 31, 142, 1989.
175.
Tuszynski, G.P., Karczewski, J., Smith, L., Murphy, A., Rothman, V.L., and Knudsen, K.A., The GPIIB-IIIA-like complex may function as a human melanoma cell adhesion receptor for thrombospondin, Exp. Cell Res., 182, 473, 1989.
176.
Pratt, D.A., Miller, W.R., and Dawes, J., Thrombospondin in malignant and non-malignant breast tissue, Eur. J. Cancer Clin. Oncol., 25, 343, 1989.