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Localization of basement membrane glycoproteins in rat kidney during foetal development
Author(s) -
Cheig M.,
Bakala H.,
Cornet S.,
Djaziri R.,
Schaeverbeke J.
Publication year - 1987
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1111/j.1768-322x.1987.tb00545.x
Subject(s) - laminin , glycoprotein , fibronectin , basement membrane , biology , type iv collagen , membrane glycoproteins , glomerular basement membrane , nephron , polyclonal antibodies , extracellular matrix , immunoperoxidase , microbiology and biotechnology , renal glomerulus , kidney , antibody , immunology , monoclonal antibody , endocrinology , glomerulonephritis
The distribution of basement membrane glycoproteins (type IV collagen, laminin, fibronectin, and proteoglycans) was studied in foetal rat kidney by immunohistochemical techniques using polyclonal antibodies. From the first stages of nephron differentiation, all these glycoproteins were detectable by immunofluorescence in the tubular and glomerular basement membranes and in the mesangial matrix. As differentiation proceeded, labelling of glycoproteins progressively intensified, except for that of fibronectin, which gradually decreased in the glomerular basement membrane (GBM) and was barely observable at full differentiation. With immunoperoxidase staining in electron microscopy, all glycoproteins were seen to be widely dispersed in the spaces between the epithelial and endothelial glomerular cells so long as the GBM remained a loose structure. However, after it became a compact, 3‐layered formation, type IV collagen and laminin were distributed throughout the GBM, whereas proteoglycans and anionic sites appeared as 2 rows of granules confined to the laminae rarae.