A Study of the Fine Structure of the Kidney in Casein-Induced Amyloidosis in Rabbits

Cohen, Alan S.; Calkins, Evan

doi:10.1084/jem.112.3.479

Cited by 45 publications

(11 citation statements)

References 17 publications

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“…A common feature of all the known amyloid proteins is that their precursors in polypeptide chains condense to form amyloid fibrils. All deposits have a fibrillar ultrastructure 18 forming extensive antiparallel ␤ pleated sheets. 19 The amyloid P component is a consistent feature of all types of amyloid, irrespective of the nature of the protein.…”

Section: Discussionmentioning

confidence: 99%

Localised deposition of amyloid in tears of the rotator cuff

Cole

Cordiner-Lawrie

Carr

et al. 2001

The Journal of Bone and Joint Surgery. British volume

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A ge-related localised deposition of amyloid in connective tissue has been found in degenerative articular and periarticular tissue. Biopsies of the supraspinatus tendon of 28 patients undergoing repair of the rotator cuff were analysed histologically for the presence of localised deposition of amyloid. There was a long history of impingement in 20 patients, and eight patients had suffered an acute traumatic tear with no preceding symptoms. Localised deposition of amyloid identified by Congo Red staining was detected in 16 samples (57%). Amyloid was present in 14 (70%) of the degenerative tears, but in only two (25%) of the acute tears. Immunohistochemical staining showed that the amyloid deposits were positive for P component, but negative for and light chains, prealbumin, and ␤2 microglobulin. Critical electrolyte staining revealed highly-sulphated glycosaminoglycans at sites of deposition of amyloid. The presence of localised deposition of amyloid in tears of the rotator cuff is likely to represent irreversible structural changes. These findings support the theory that impingement and tears are due to intrinsic degenerative changes within the tendons of the rotator cuff.

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Section: Discussionmentioning

confidence: 99%

Localised deposition of amyloid in tears of the rotator cuff

Cole

Cordiner-Lawrie

Carr

et al. 2001

The Journal of Bone and Joint Surgery. British volume

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“…In our four autopsy cases no such antecedents were noted. ad B) Five rabbits were given 5 ml of a 10 per cent solution of casein twice a week subcutaneously by the method of Cohen and Calkins [5] and were killed by air embolism at the end of six months. Three animals had demonstrable proteinuria from the month onwards.…”

Section: Methodsmentioning

confidence: 99%

Immunofluorescence in the study of amyloid nephrosis

Beregi

Hatala

1969

Urology and Nephrology

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The kidneys were studied by the fluorescent antibody technique in four autopsy cases of human amyloidosis and casein-induced amyloidosis in rabbits. In the cases of human amyloid nephrosis massive deposits of human gamma-globulin were identified in the glomerules, in the vascular walls, in the tubular basement membrane and in the interstitial tissue, and lipoprotein was demonstrable in the cytoplasms of the tubular epithelial cells. In experimental amyloidosis the studies revealed the presence of rabbit gamma-globulin in the glomerules and in the vascular walls.More than a century after Virchow's original description of amyloidosis [17], the pathogenesis of this process is still obscure. Certain authors connect it with an abnormal protein metabolism, ascribing significance to hyperglobulinaemia [6J. Others incriminate a disordered function of the RES for this condition:

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“…A burst in amyloid research developed after the electron-microscopical discovery of amyloid fibrils in 1958 by Cohen (Cohen et al, 1958;Cohen and Calkins, 1959) and subsequent description by others (Spiro, 1959). It offered new possibilities for isolation (Pras et al, 1968), peptide separation and analysis of a large series of different chemical amyloid types corresponding to the known variations in clinicopathological patterns, and offered a rational base for nomenclature (WHO-IUIS, 1993;INC, 1998a;1998b): the first letter, A, for amyloid and one or more others for the chemical type.…”

Section: Amyloid and Virchowmentioning

confidence: 99%

Protein folding pathology in domestic animals

Gruys

2004

J. Zheijang Univ.-Sci.

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Fibrillar proteins form structural elements of cells and the extracellular matrix. Pathological lesions of fibrillar microanatomical structures, or secondary fibrillar changes in globular proteins are well known. A special group concerns histologically amorphous deposits, amyloid. The major characteristics of amyloid are: apple green birefringence after Congo red staining of histological sections, and non-branching 7−10 nm thick fibrils on electron microscopy revealing a high content of cross beta pleated sheets. About 25 different types of amyloid have been characterised. In animals, AA-amyloid is the most frequent type. Other types of amyloid in animals represent: AIAPP (in cats), AApoAI, AApoAII, localised AL-amyloid, amyloid in odontogenic or mammary tumors and amyloid in the brain. In old dogs Aβ and in sheep APrP sc -amyloid can be encountered. AA-amyloidosis is a systemic disorder with a precursor in blood, acute phase serum amyloid A (SAA). In chronic inflammatory processes AA-amyloid can be deposited. A rapid crystallization of SAA to amyloid fibrils on small beta-sheeted fragments, the 'amyloid enhancing factor' (AEF), is known and the AEF has been shown to penetrate the enteric barrier. Amyloid fibrils can aggregate from various precursor proteins in vitro in particular at acidic pH and when proteolytic fragments are formed. Molecular chaperones influence this process. Tissue data point to amyloid fibrillogenesis in lysosomes and near cell surfaces. A comparison can be made of the fibrillogenesis in prion diseases and in enhanced AA-amyloidosis. In the reactive form, acute phase SAA is the supply of the precursor protein, whereas in the prion diseases, cell membrane proteins form a structural source. Aβ-amyloid in brain tissue of aged dogs showing signs of dementia forms a canine counterpart of senile dementia of the Alzheimer type (ccSDAT) in man. Misfolded proteins remain potential food hazards. Developments concerning prevention of amyloidogenesis and therapy of amyloid deposits are shortly commented.

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A Study of the Fine Structure of the Kidney in Casein-Induced Amyloidosis in Rabbits

Abstract: PLATES 40 TO 46

Cited by 45 publications

References 17 publications

Localised deposition of amyloid in tears of the rotator cuff

Localised deposition of amyloid in tears of the rotator cuff

Immunofluorescence in the study of amyloid nephrosis

Protein folding pathology in domestic animals

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