Abstract
Background. In Alport syndrome (AS) impaired production and/or assembly of col IV α-chain isoforms results in abnormal structure of glomerular basement membrane (GBM), haematuria and, frequently, progressive renal disease. We investigated the relationship between col IV α-chains expression and morphology of GBM, as a possible key to the better understanding of the pathogenesis of renal disease in AS. Methods. GBM distribution of col IV αl-, α3-, and α5-chain was investigated by immunohistochemistry in 32 patients (21 males and 11 females, mean age at biopsy of 11.5 years) with ultrastructural findings suggestive of AS. Ten patients had a proven COL4A5 mutation. Based on the severity of ultrastructural findings, the biopsies were grouped in three (I-III) electron microscopy (EM) classes. Significant EM changes of GBM (thinning, thickening, splitting, basket weaving of the lamina densa) were singularly evaluated using a semiquantitative scale (0-3). Results. Col IV α1-chain was demonstrated in GBM of all patients. Three patterns of staining for col IVα3-and α5-chains were observed: positive, negative, and α3(IV)-positive/α5(IV)-negative. By Χ2-test, EM class III lesions and complete loss of α3(IV)- and α5(IV)-antigen were significantly more frequent (P
| Original language | English |
|---|---|
| Pages (from-to) | 945-952 |
| Number of pages | 8 |
| Journal | Nephrology Dialysis Transplantation |
| Volume | 16 |
| Issue number | 5 |
| Publication status | Published - 2001 |
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Keywords
- Alport syndrome
- COL4A5 gene mutations
- Electron microscopy
- Glomerular basement membrane
- Immunohistochemistry
- Type IV collagen
ASJC Scopus subject areas
- Nephrology
- Transplantation
Cite this
Distribution of α-chains of type IV collagen in glomerular basement membranes with ultrastructural alterations suggestive of Alport syndrome. / Barsotti, Paola; Muda, Andrea Onetti; Mazzucco, Gianna; Massella, Laura; Basolo, Bruno; De Marchi, Mario; Rizzoni, Gianfranco; Monga, Guido; Faraggiana, Tullio.
In: Nephrology Dialysis Transplantation, Vol. 16, No. 5, 2001, p. 945-952.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Distribution of α-chains of type IV collagen in glomerular basement membranes with ultrastructural alterations suggestive of Alport syndrome
AU - Barsotti, Paola
AU - Muda, Andrea Onetti
AU - Mazzucco, Gianna
AU - Massella, Laura
AU - Basolo, Bruno
AU - De Marchi, Mario
AU - Rizzoni, Gianfranco
AU - Monga, Guido
AU - Faraggiana, Tullio
PY - 2001
Y1 - 2001
N2 - Background. In Alport syndrome (AS) impaired production and/or assembly of col IV α-chain isoforms results in abnormal structure of glomerular basement membrane (GBM), haematuria and, frequently, progressive renal disease. We investigated the relationship between col IV α-chains expression and morphology of GBM, as a possible key to the better understanding of the pathogenesis of renal disease in AS. Methods. GBM distribution of col IV αl-, α3-, and α5-chain was investigated by immunohistochemistry in 32 patients (21 males and 11 females, mean age at biopsy of 11.5 years) with ultrastructural findings suggestive of AS. Ten patients had a proven COL4A5 mutation. Based on the severity of ultrastructural findings, the biopsies were grouped in three (I-III) electron microscopy (EM) classes. Significant EM changes of GBM (thinning, thickening, splitting, basket weaving of the lamina densa) were singularly evaluated using a semiquantitative scale (0-3). Results. Col IV α1-chain was demonstrated in GBM of all patients. Three patterns of staining for col IVα3-and α5-chains were observed: positive, negative, and α3(IV)-positive/α5(IV)-negative. By Χ2-test, EM class III lesions and complete loss of α3(IV)- and α5(IV)-antigen were significantly more frequent (P
AB - Background. In Alport syndrome (AS) impaired production and/or assembly of col IV α-chain isoforms results in abnormal structure of glomerular basement membrane (GBM), haematuria and, frequently, progressive renal disease. We investigated the relationship between col IV α-chains expression and morphology of GBM, as a possible key to the better understanding of the pathogenesis of renal disease in AS. Methods. GBM distribution of col IV αl-, α3-, and α5-chain was investigated by immunohistochemistry in 32 patients (21 males and 11 females, mean age at biopsy of 11.5 years) with ultrastructural findings suggestive of AS. Ten patients had a proven COL4A5 mutation. Based on the severity of ultrastructural findings, the biopsies were grouped in three (I-III) electron microscopy (EM) classes. Significant EM changes of GBM (thinning, thickening, splitting, basket weaving of the lamina densa) were singularly evaluated using a semiquantitative scale (0-3). Results. Col IV α1-chain was demonstrated in GBM of all patients. Three patterns of staining for col IVα3-and α5-chains were observed: positive, negative, and α3(IV)-positive/α5(IV)-negative. By Χ2-test, EM class III lesions and complete loss of α3(IV)- and α5(IV)-antigen were significantly more frequent (P
KW - Alport syndrome
KW - COL4A5 gene mutations
KW - Electron microscopy
KW - Glomerular basement membrane
KW - Immunohistochemistry
KW - Type IV collagen
UR - http://www.scopus.com/inward/record.url?scp=0035021748&partnerID=8YFLogxK
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M3 - Article
C2 - 11328899
AN - SCOPUS:0035021748
VL - 16
SP - 945
EP - 952
JO - Nephrology Dialysis Transplantation
JF - Nephrology Dialysis Transplantation
SN - 0931-0509
IS - 5
ER -