Localized Amyloid Deposits Research Articles

Abnormalities of the musculoskeletal system in hemodialysis patients

Osteoarticular disorders significantly limit the quality of long-term survival with chronic renal failure. β2M amyloidosis is a complication of chronic renal failure that has been recognized mostly in patients receiving long-term haemodialysis. Patients with β2M amyloidosis typically present with the triad of shoulder periarthritis, carpal tunnel syndrome, and flexor tenosynovitis of the hands. Other musculoskeletal manifestations of β2M amyloidosis include destructive spondyloarthropathy, cervico-occipital pseudotumours, bone cysts, and pathological fractures. At present, only renal transplantation may slow or halt the progession of β2M amyloidosis. Crystal-induced arthropathy, most commonly caused by basic calcium phosphate crystals, is an important cause of acute joint inflammation in the patient with renal failure. The incidence of bone and joint infection is increased in patients undergoing dialysis. Haemodialysis and peritoneal dialysis are also associated with an erosive or destructive arthropathy of finger joints, which is not explained by local amyloid deposition.

Differences in ultrastructural organization of amyloid as revealed by sensitivity or resistance to induced proteolysis.

Amyloid substance is known to be resistant to proteolytic enzymes. In the present investigations it was found that after mild preoxidation with potassium permanganate of tissue sections, the deposits of amyloid in 11 cases of secondary generalized amyloidosis were dissolved by trypsin. The amyloid deposits in three cases of primary generalized amyloidosis however, proved resistant to induced proteolysis. Furthermore, myeloma amyloid in a case of anuric nephrosis, local massive amyloid deposits in a case of medullary thyroid carcinoma, amyloid of an amyloid tumour of the skin, as well as all senile amyloid deposits investigated (in heart, aorta, meningocerebral vessels, senile plaques of cerebral cortex and in the pancreatic islets) were resistant to induced proteolysis. These findings indicate essential differences in ultrastructural organization between the various amyloids; such differences are not detectable by any morphological method. Resistant and sensitive types of amyloid thus seem to be bound to clinical forms of amyloidosis and seem to correspond to types A and B amyloid as recently distinguished on a physico-chemical basis by Benditt and Eriksen. The usefulness of testing sensitivity or resistance of amyloids to induced proteolysis in differentiating them according to their ultrastructural organization in pathohistology and the significance of this test as a new approach in amyloid research are discussed.

Local Amyloid Deposits of the Larynx: Electron Microscopic Studies of Three Cases

Three additional cases of localized laryngeal amyloidosis are presented. Electron microscopy is added for the first time as a diagnostic laboratory examination. The amyloid fibrils found in local laryngeal deposits prove to be identical with those found elsewhere in the body.

Diffuse pulmonary amyloidosis

A sixty-nine year old woman with primary diffuse alveoloseptal pulmonary amyloidosis is described. Moderate localized deposition of amyloid in the heart was also observed. Pulmonary symptoms were masked by cardiac failure; the diagnosis was made at autopsy.

Localized amyloid deposition in the lower respiratory tract

Localized amyloid deposition in the lower respiratory tract

Amyloid Disease of the Heart

A sixty-nine year old woman with primary diffuse alveoloseptal pulmonary amyloidosis is described. Moderate localized deposition of amyloid in the heart was also observed. Pulmonary symptoms were masked by cardiac failure; the diagnosis was made at autopsy.

PRIMARY AMYLOID DEPOSITS IN THE LARYNX

PRIMARY nodular amyloid deposits in the laryngeal mucosa is an infrequently reported lesion. A perusal of theQuarterly Cumulative Index Medicusof the past twenty-five years reveals only 15 reports of this lesion, and, of these, only 4 cases are in the English literature. Beavis1in 1934 reported on 5 cases, the largest series in the English language. This author stated the opinion that local amyloid deposits in the upper respiratory passages are rare, since there were no more than 50 cases in the entire literature. It was considered that the disease would be more readily recognized in the future; however, the number of recorded cases since that time has remained small. In a review of fundamental disorders of the larynx, Kernan2did not mention amyloid deposits. Standard textbooks of pathology give scant, if any, mention of this condition. Because of this paucity of reports, we wish to

LOCAL TUMOR-LIKE DEPOSITS OF AMYLOID IN THE LARYNX: REPORT OF A CASE WITH A REVIEW OF THE LITERATURE

The occurrence of isolated tumor-like deposits of amyloid in such areas as the upper air passages may have a variable significance depending on associated pathologic conditions in the body as well as on the presence or absence of a basic etiologic factor. The following classification into four groups is based on an analysis of published reports of cases in the literature: 1. Local amyloid deposits occurring secondarily within neoplasms or areas of chronic inflammation. This type should be distinguished from primary local amyloid tumors which have no obvious basis in preexisting changes of the tissue. Secondary amyloid tumors are well known and have been reported frequently, especially in fibromas and sarcomas (Martuscelli). Peroni described amyloid infiltration also in inflammatory polypi of the larynx and the ear. 2. Local tumor-like amyloid deposits which are part of a generalized amyloidosis of the usual type involving liver, spleen, kidneys and suprarenal