Immunochemical Characterization and Quantitation of the Human Glomerular Basement Membrane Antigen from the Urine of Patients with Glomerular Diseases

2015 ◽  
pp. 124-135 ◽  
Author(s):  
Yoko Wakashin ◽  
Masafumi Wakashin ◽  
Mitsuharu Narita ◽  
Shizuo Tojo
1980 ◽  
Vol 3 (1-6) ◽  
pp. 395-404
Author(s):  
M.C. Gubler ◽  
M. Levy ◽  
C. Naizot ◽  
R. Habib

1980 ◽  
Vol 3 (1-6) ◽  
pp. 405-413 ◽  
Author(s):  
M.C. Gubler ◽  
M. Levy ◽  
C. Naizot ◽  
R. Habib

1992 ◽  
Vol 2 (9) ◽  
pp. 1388-1397
Author(s):  
R Johnson ◽  
H Yamabe ◽  
Y P Chen ◽  
C Campbell ◽  
K Gordon ◽  
...  

Cultured rat glomerular epithelial cells (GEC) were examined for their ability to release extracellular matrix-degrading proteinases with [3H]gelatin as substrate. GEC-conditioned media, under serum-free conditions, contained modest amounts of gelatinase activity (1 to 10 U/mg of protein); the activity was maximal at neutral pH, was inhibited by zinc chelators, was not inhibited by tissue inhibitor of metalloproteinase-2, and could not be further activated by trypsin or organomercurials. Gelatin substrate sodium dodecyl sulfate-polyacrylamide gels of GEC-conditioned medium revealed several zones of lysis, with molecular sizes of 150 kd (major band), and 220, 86 to 93, and 52 to 54 kd (minor bands). Northern blot analysis demonstrated that the GEC metalloproteinase(s) were distinct from the 68- to 72-kd type IV collagenase/gelatinase present in mesangial cells or the 92-kd type IV collagenase present in neutrophils. The GEC gelatinolytic activity also degraded insoluble type IV collagen in glomerular basement membrane in a dose-dependent manner. The major metalloproteinase activity responsible for the type IV collagen degradation has a molecular size of 150 kd with a type IV collagen substrate gel. Thus, GEC produce several neutral metalloproteinases, which, by virtue of their substrate specificity, may play an important role in glomerular basement membrane remodeling and in glomerular diseases characterized by alterations in basement membrane permeability.


2002 ◽  
Vol 109 (4) ◽  
pp. 517-524 ◽  
Author(s):  
Jean Wu ◽  
John Hicks ◽  
Jason Borillo ◽  
William F. Glass ◽  
Ya-Huan Lou

2000 ◽  
Vol 11 (12) ◽  
pp. 2243-2255
Author(s):  
TAKASHI NAITO ◽  
MOHAMMED S. RAZZAQUE ◽  
ARIFA NAZNEEN ◽  
DIANGE LIU ◽  
HIROSHI NIHEI ◽  
...  

Abstract. The ets-1 proto-oncogene is a member of the transcriptional factor family and was identified by homology to the v-ets oncogene. It was recently demonstrated that Ets-1 protein interacts with the promoter region of the genes coding for proteinases, including matrix metalloproteinase-1 (MMP-1), MMP-3, and urokinase-type plasminogen activator, suggesting that it may play an important role in the regulation of MMP expression. The role of the ets-1 proto-oncogene in advanced glomerular diseases, where extracellular matrix accumulation is observed, remains undefined. In this study, the expression of ets-1 mRNA and protein during the progression of rat crescentic glomerulonephritis was examined using immunohistochemical analysis, reverse transcription-PCR, and in situ hybridization. Passive accelerated anti-glomerular basement membrane-induced nephritis was induced in rats by intravenous injection of nephrotoxic serum. Rats were euthanized on day 7, 14, 21, 28, or 42. Immunohistochemical analysis demonstrated significant upregulation of Ets-1 protein expression in glomeruli and the interstitium in anti-glomerular basement membrane-induced nephritis. The numbers of Ets-1-positive cells were increased 8.8-fold on day 21 in glomeruli (1.2 ± 0.1 cells/glomerular cross-section, P < 0.001) and sixfold on day 28 in the interstitium (21 ± 1.3 cells/mm2, P < 0.001), compared with control samples. Ets-1 protein was predominantly localized in glomerular epithelial cells, endothelial cells, and interstitial cells. A small number of vascular endothelial cells, macrophages, and T cells also expressed Ets-1 protein. MMP-3 deposition was upregulated and positive cells in the interstitium often coexpressed Ets-1, whereas only a few glomerular cells were positive for both MMP-3 and Ets-1 protein. The expression of ets-1 mRNA was also markedly increased in diseased kidneys. The distribution of ets-1 mRNA was similar to that of the protein. These results indicate that overexpression of the ets-1 proto-oncogene by phenotypically altered renal cells might be associated with the pathogenesis of rat crescentic glomerulonephritis.


1978 ◽  
Vol 92 (6) ◽  
pp. 952-953 ◽  
Author(s):  
Sudhir K. Anand ◽  
Benjamin H. Landing ◽  
Eva T. Heuser ◽  
David L. Olson ◽  
Carl M. Grushkin ◽  
...  

2017 ◽  
Vol 32 (suppl_3) ◽  
pp. iii138-iii139 ◽  
Author(s):  
Janina Müller-Deile ◽  
Jan Dannenberg ◽  
Jeffrey H. Miner ◽  
Jan-Hinrich Bräsen Bräsen ◽  
Patricia Schroder ◽  
...  

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