Pathology of Experimental Amyloidosis

Amyloidosis ◽  
1986 ◽  
pp. 295-300
Author(s):  
Tsuranobu Shirahama ◽  
Alan S. Cohen
Author(s):  
A. Kawaoi

Numbers of immunological approach have been made to the amyloidosis through the variety of predisposing human diseases and the experimentally induced animals by the greater number of agents. The results suggest an important role of impaired immunity involving both humoral and cell-mediated aspects.Recently the author has succeeded in producing amyloidosis in the rabbits and mice by the injections of immune complex of heat denatured DNA.The aim of this report is to demonstrate the details of the ultrastructure of the amyloidosis induced by heterologous insoluble immune complex. Eleven of twelve mice, dd strain, subcutaneously injected twice a week with Freund's complete adjuvant and four of seven animals intraperitonially injected developed systemic amyloidosis two months later from the initial injections. The spleens were electron microscopically observed.


1991 ◽  
Vol 39 (10) ◽  
pp. 1321-1330 ◽  
Author(s):  
A D Snow ◽  
R Bramson ◽  
H Mar ◽  
T N Wight ◽  
R Kisilevsky

Previous histochemical studies have suggested a close temporal relationship between the deposition of highly sulfated glycosaminoglycans (GAGs) and amyloid during experimental AA amyloidosis. In the present investigation, we extended these initial observations by using specific immunocytochemical probes to analyze the temporal and ultrastructural relationship between heparan sulfate proteoglycan (HSPG) accumulation and amyloid deposition in a mouse model of AA amyloidosis. Antibodies against the basement membrane-derived HSPG (either protein core or GAG chains) demonstrated a virtually concurrent deposition of HSPGs and amyloid in specific tissue sites regardless of the organ involved (spleen or liver) or the induction protocol used (amyloid enhancing factor + silver nitrate, or daily azocasein injections). Polyclonal antibodies to AA amyloid protein and amyloid P component also demonstrated co-localization to sites of HSPG deposition in amyloid sites, whereas no positive immunostaining was observed in these locales with a polyclonal antibody to the protein core of a dermatan sulfate proteoglycan (known as "decorin"). Immunogold labeling of HSPGs (either protein core or GAG chains) in amyloidotic mouse spleen or liver revealed specific localization of HSPGs to amyloid fibrils. In the liver, heparan sulfate GAGs were also immunolocalized to the lysosomal compartment of hepatocytes and/or Kupffer cells adjacent to sites of amyloid deposition, suggesting that these cells are involved in HSPG production and/or degradation. The close temporal and ultrastructural relationship between HSPGs and AA amyloid further implies an important role for HSPGs during the initial stages of AA amyloidosis.


2004 ◽  
pp. 231-234
Author(s):  
R. Bradunaite ◽  
D. Povilenaite ◽  
L. Leonaviciene ◽  
D. Vaitkiene ◽  
A. Venalis

1968 ◽  
Vol 127 (3) ◽  
pp. 925-929 ◽  
Author(s):  
E. R. Dalferes ◽  
B. Radhakrishnamurthy ◽  
G. S. Berenson

1977 ◽  
Vol 12 (2) ◽  
pp. 129-133
Author(s):  
Antti Ahonen ◽  
Olli Penttilä ◽  
Erik Klinge

2020 ◽  
pp. 30-36
Author(s):  
Liliya Yu. Ilyina ◽  
Vadim A. Kozlov ◽  
Sergey P. Sapozhnikov ◽  
Ruslan A. Geraev

The reaction of lymphoid splenic tissue of mice on albumin model of systemic amyloidosis (case group, N = 5) was studied and compared to a similar indicator of intact mice (N = 5). Paraffin sections of the spleen, stained with hematoxylin and eosin and Congo red, were microscoped in a regredient LED white light on "Lumam-4" microscope. The absolute area of lymphatic follicles (LFs), their diameters and the area of amyloid lesion were measured on microphotos obtained with the help of video-eyepiece Levenhuk C800 NG 8M in LevenhukLite program. The obtained data were used for calculating the indicators: the relative areas of amyloid lesion (SrelA)), the red (SrelKB) and the white (SrelBP) pulp, the red/white pulp index, LFs' ovalityindex. The number of LFs was counted in the field of vision at magnification of 100. The obtained data were processed using the methods of descriptive and variative statistics and presented in the form of M±m, where M is the mean, m is the standard deviation. Differences of the means were determined using z test. The morphological pattern of the spleen in intact mice corresponded to the histological norm. The wet mass of the spleen in intact animals was 0.75±0.01 g, no signs of amyloidosis were found. In the case group, the wet mass of the spleen increased to 2.2±0.06 g (p=0.000), SrelA was 33.85± 3.39%. The average number of LFs in the field of vision did not change. The diameters by the large and small axes differed by 18% in intact animals and by 6.6% in experimental ones (p=0.000). Respectively, the area of LFs decreased by 11.2% and the ovality index increased by 10.3% (p = 0.0066) in experimental mice. SrelKB and SrelBPdid not change during the formation of amyloidosis. But the Red/White Pulp Index increased by 59.2% (p=0.008). Simulation of amyloidosis in experimental animals was accompanied by a significant increase in the area of the red pulp and by a reduction in the area of white pulp. Thus, the calculated relative morphometric indicators are more informative than the directly measured initial data; the wet mass of the spleen during experimental amyloidosis formation significantly increases; the lymphoid tissue of the spleen readily responds to amyloidogenesis by the change in the ratio of the red and white pulp, as well as by the change in the shape and the area of the lymph follicles.


1968 ◽  
Vol 127 (3) ◽  
pp. 854-856 ◽  
Author(s):  
J. Sri Ram ◽  
G. G. Glenner ◽  
R. A. Delellis

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