ArticlePediatric nephrology (Berlin, Germany)1996
Collagen distribution in human membranous glomerulonephritis.
Article in Pediatric nephrology (Berlin, Germany), 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 14 citations in OpenAlex.
- The fate of immune complexes in membranous nephropathy.Frontiers in immunology · 2024Review
- Article
- Early glomerular filtration defect and severe renal disease in podocin-deficient mice.Molecular and cellular biology · 2004Article
- Antibody response against perlecan and collagen types IV and VI in chronic renal allograft rejection in the rat.The American journal of pathology · 2002Article
- Podocin localizes in the kidney to the slit diaphragm area.The American journal of pathology · 2002Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
In membranous glomerulonephritis (MGN), thickening of the glomerular basement membrane (GBM) is partly due to the accumulation of basement membrane material between and around immune deposits located on the epithelial aspect of the GBM. We investigated the distribution of type IV collagen chains (alpha 1/alpha 2, alpha 3, alpha 4, alpha 5, alpha 6) and of types I, III, V, and VI collagen in the glomeruli from 16 patients, by indirect immunofluorescence in 13 and the high-resolution immunogold technique in 6. No changes were detected in stage I MGN. The spiky projections of the GBM in stage II MGN and the basement membrane layers encircling immune deposits in stage III contained the alpha 3, alpha 4, and alpha 5 chains of type IV collagen. In contrast, the alpha 1/alpha 2 chains of type IV, as well as type VI collagen accumulated in the subendothelial aspect of the GBM. No significant staining for types I, III, and V collagens or for the alpha 6 chain of type IV collagen was detected. The results show that, as in the normal glomeruli, the different chains of type IV collagen are not co-distributed in the glomerular extracellular matrix in MGN. They also indicate that type IV collagen chains and type IV collagen play an important role in the thickening of the GBM in human MGN.
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Registered trials
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