Open AccessFibronectin and basement membrane components in renal amyloid deposits in patients with primary and secondary amyloidosis
Author(s) -
WESTERMARK G. T.,
NORLING B.,
WESTERMARK P.
Publication year - 1991
Publication title -
clinical & experimental immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.329
H-Index - 135
eISSN - 1365-2249
pISSN - 0009-9104
DOI - 10.1111/j.1365-2249.1991.tb05788.x
Subject(s) - fibronectin , amyloidosis , basement membrane , amyloid (mycology) , pathology , glomerular basement membrane , immunology , medicine , kidney , chemistry , glomerulonephritis , extracellular matrix , biochemistry
SUMMARY Kidney biopsies from one patieni with primary (AL) and three with secondary (AA) amyloidosis were used for an ultrastructural study of the collocalization of basement membrane proteins and the extracellular matrix protein fibronectin within amyloid deposits. Antibodies against amyloid P component, laminin. and heparan sulphate proteoglycan core protein all reacted with the basement membranes and the amyloid depositions in AA and AL amyloidosis. Monoclonal and polyclonal antibodies against collagen type IV reacted only with the basement membranes. Anti‐fibronectin reaction was found in association with the basement membranes in all four cases, while labelling of amyloid depositions was found only in one of the AA amyloid cases and in the AL amyloid depositions. It is concluded that basement membrane components may be of importance for the formation of amyloid fibrils.