Vacuoles of mesenchymal cells in the papillae of bovine kidneys with amyloidosis were studied by histochemical electron microscopy for acid phosphatase as a marker for lysosomes. The vacuoles contained parallel amyloid fibrils. The vacuoles of reticular interstitial cells were found to be lysosomes. Vacuoles of macrophage-like cells of the same papillae were positive, partially positive, or negative for the enzyme activity. A suspension of papillary material was injected subcutaneously in rats in a 21-day light and electron microscopy and enzyme histochemistry study. Amyloid was demonstrated in vacuoles of macrophages throughout this period and initially also in neutrophils. In most vacuoles amyloid fibrils were randomly arranged but in others parallel arrangement was demonstrated. Amyloid was only at the inoculation sites. Intralysosomal bovine amyloid may occur in parallel fibrillar arrangement without a definite indication for amyloid production.
References
1.
AndersR.F.; NatvigJ.B.; MichaelsenF.E.; HusbyG.: Isolation and preliminary characterization of the amyloid related serum protein S A A.Scand J Rheumatol Supp8: abstract 3901, 1975
2.
AzarH.A.: Amyloidosis and plasma cell disorders; in Multiple myeloma and related disorders, ed. Azar, and Potter; pp. 328–403, vol. 1, Harper and Row, Hagerstown, 1973
3.
BattagliaS.: Elektronenoptische Untersuchungen am Leberamyloid der Maus.Beitr Pathol Anat Allg Pathol126: 300–320, 1962
4.
BendittE.P.; EriksenN.: Chemical classes of amyloid substance.Am J Pathol65: 231–252, 1971
5.
BendittE.P.; EriksenN.: The chemical classes of amyloid substance in men, monkeys and ducks; in Protides of the biological fluids. Proc 20th colloquium, ed. Peeters, pp. 81–85, Pergamon Press, Oxford, 1972
6.
Ben-IshayZ.; ZlotnickA.: The cellular origin of amyloid. Electron microscopic study in a case of amyloidosis.J Med Sci4: 987–994, 1962
7.
BhathalP.S.: Presence of modified fibroblasts in cirrhotic livers in man.Pathol4: 139–144, 1972
8.
DaemsW.Th.; WisseE.; BrederooP.: Lysosomes in biology and pathology, ed. Dingle, and Fell, pp. 82–88, vol. I, North-Holland Publishing Co., Amsterdam, 1969
9.
De LellisR.A.; RamJ.S.; GlennerG.G.: Further kinetic studies on experimental murine amyloidosis.Int Arch Allergy Appl Immunol37: 175–183, 1970
10.
DreherR.; VandreF.: Amyloid unter dem Einfluss der Autolyse.Beitr Pathol145: 256–268, 1972
11.
EpsteinW.V.; TanM.; WoodJ.S.: Formation of “amyloid” fibrils in vitro by action of human kidney lysosomal enzymes on Bence Jones protein.J Lab Clin Med84: 107–110, 1974
12.
FieldsM.; PolliackA.; LauferA.: Resorption of amyloid and enzymatic studies in amyloidosis.Isr J Med Sci9: 875–880, 1973
13.
FranklinE.C.; Zucker-FranklinD.: Current concepts of amyloid.Adv Immunol15: 249–304, 1972
14.
GabbianiG.; RyanG.B.; MajnoG.: Presence of modified fibroblasts in granulation tissue and their possible role in wound contraction.Experientia27: 549–550, 1971
15.
GlennerG.G.; EinD.; EanesE.D.; BladenH.A.; TerryW.; PageD.L.: Creation of amyloid fibrils from Bence Jones proteins in vitro.Science174: 712–714, 1971
16.
GlennerG.G.: The pathogenetic and therapeutic implications of the discovery of the immunoglobulin origin of amyloid fibrils.Hum Pathol3: 157–162, 1972
17.
GlennerG.G.; TerryW.D.: The immunoglobulin origin of amyloid fibril proteins; in Protides of the biological fluids. Proc 20th colloquium, ed. Peeters, pp. 55–61, Pergamon Press, Oxford, 1972
18.
GlennerG.G.; TerryW.D.; IserskyC.: Amyloidosis: its nature and pathogenesis.Sem Hematol10: 65–86, 1973
19.
GreenC.J.: Amyloidosis as an incidental finding in rats on experiment.Lab Anim8: 99–101, 1974
20.
GruysE.: Bovine renal amyloidosis I. incidence, macroscopical and microscopical features.Tijdschr Diergeneeskd99: 715–728, 1974
GruysE.: Ultrastructural and enzyme-histochemical aspects of amyloidosis in the bovine renal medulla.Vet Pathol12: 94–110, 1975
23.
GueftB.; GhidoniJ.J.: The site of formation and ultrastructure of amyloid.Amer J Pathol43: 837–854, 1963
24.
HaudenschildC.C.; CotranR.S.; GimbroneM.A.; FolkmanJ.: Fine structure of vascular endothelium in culture.J Ultrastruct Res50: 22–32, 1975
25.
IshiharaT.: Experimental amyloidosis using silver nitrate. Electronmicroscopic study on the relationship between silver granules, amyloid fibrils and reticuloendothelial system.Acta Pathol Jpn23: 439–464, 1973
26.
LendrumA.C.; SliddersW.; FraserD.S.: Renal hyalin, a study of amyloidosis and diabetic fibrinous vasculosis with new staining methods.J Clin Pathol25: 373–396, 1972
27.
LinkeR.P.; SipeJ.D.; Scott-PollockP.; IgnaczakT.F.; GlennerG.G.: Isolation of a low-molecular-weight serum component antigenetically related to an amyloid fibril protein of unknown origin.Proc Nat Acad Sci USA72: 1473–1476, 1975
28.
MohrW.; PauliniK; BenekeG.; ScomazzoniG.: Resorption of amyloid. Studies of implanted amyloid.Pathol Microbiol41: 240–252, 1974
29.
ParakkalP.F.: Involvement of macrophages in collagen resorption.J Cell Biol41: 345–354, 1969
30.
PolliackA.; LauferA.; TalC.: Studies on the resorption of experimental amyloidosis.Br J Exp Pathol51: 236–241, 1970
31.
PolliackA.; LauferA.; GeorgeR.; FieldsM.: The effect of cortisone on the formation and resorption of experimental amyloid.Br J Exp Pathol54: 6–12, 1973
32.
PruzanskiW.; KatzA.; NyburgS.C.; FreedmanM.H.: In vitro production of an amyloid-like substance from gamma 3 heavy chain disease protein.Immunol Commun3: 469–476, 1974
33.
RomhányiG.: Selective differentiation between amyloid and connective tissue structures based on the collagen specific topo-optical staining reaction with Congo red.Virchows Arch354: 209–222, 1971
34.
RosenthalC.J.; FranklinE.C.: Variation with age and disease of an amyloid “A” related serum component.J Clin Invest55: 746–753, 1975
35.
RuinenL.; van BruggenE.F.J.; ScholtenJ.H.; GruberM.; MandemaE.: Isolation of amyloid according to Bestetti; in Amyloidosis (addendum), ed. Mandema; Ruinen; Scholten, and Cohen, p. 202, Excerpta Medica Foundation, Amsterdam, 1968
36.
RyanG.B.; CliffA.J.; PhilD.; GabbianiG.; IrleC.: Myofibroblasts in an avascular fibrous tissue.Lab Invest29: 197–206, 1973
37.
ShirahamaT.; CohenA.S.: Lysosomal breakdown of amyloid fibrils by macrophages.Am J Pathol63: 463–485, 1971
38.
ShirahamaT.; CohenA.S.: An analysis of the close relationship of lysosomes to early deposits of amyloid. Ultrastructural evidence in experimental mouse amyloidosis.Am J Pathol73: 97–115, 1973
SkinnerM.; BensonM.D.; CohenA.S.: Amyloid fibril protein related to immunoglobulin λ-chains.J Immunol114: 1433–1435, 1975
42.
SlettenK; HusbyG.; NatvigJ.B.: N-terminal amino acid sequence of amyloid fibril protein A R. Prototype of a new λ-variable subgroup VλV.Scand J Immunol3: 833–836, 1974
43.
SorensonG.D.; HufnerW.A.; KirkpatrickJ.B.: Experimental amyloidosis. II. Light and electron microscopic observations of liver.Am J Pathol44: 629–644, 1964
44.
SorensonG.D.; BariW.A.: Murine amyloid deposits and cellular relationship; in Amyloidosis, ed. Mandema; Ruinen; Scholten, and Cohen, pp. 58–73, Excerpta Medica Foundation, Amsterdam, 1968
45.
SteinsiepeK.F.; WeibelE.R.: Elektronenmikroskopische Untersuchungen an spezifischen Organellen von Endothelzellen des Froshes (Rana temporaria).Z Zellforsch108: 105–126, 1970
46.
TotovicV.; WucherpfennigH.: Methoden für den Enzymnachweis; in Methodensammlung der Elektronenmikroskopie Band 2, ed. Schimmel, and Vogell, pp. 18–19, Wissenschaftliche Verlagsgesellschaft MBH, Stuttgart, 1970
47.
TorhorstJ.: Studies on the pathogenesis and morphogenesis of glomerulonephrosis (application of a newly developed morphometric method).Curr Top Pathol59: 1–68, 1974
48.
WeibelE.R.; PaladeG.E.: New cytoplasmic components in arterial endothelia.J Cell Biol23: 101–112, 1964
49.
WeissS.W.; PageD.L.: Amyloid nephropathy of Ostertag with special reference to renal glomerular giant cells.Am J Pathol72: 447–460, 1973
50.
WrightJ.R.; OzdemirA.I.; MatsuzakiM.; BinetteP.; CalkinsE.: Amyloid resorption. Possible role of multinucleated giant cells. The apparent failure of penicillamine treatment.Johns Hopkins Med J130: 278–288, 1972
51.
Zucker-FranklinD.: Immunophagocytosis of human amyloid fibrils by leukocytes.J Ultrastruct Res32: 247–257, 1970
