TY - JOUR
T1 - Degradation of glomerular basement membrane by a neutral metalloproteinase(s) present in glomeruli isolated from normal rat kidney
AU - Nguyen, Hung H.
AU - Baricos, William H.
AU - Shah, Sudhir V.
N1 - Funding Information:
Portions of this work have appeared in abstract form. This work was supported by grants from: the American Heart Association (81-1179); NIH (2 ROI-AM28452-04); the Medical Research Service, Veterans Administration Hopsital, New Orleans, LA.; and a Graduate Student Summer Research Grant to HHN from the American Heart Association of Louisiana, Inc. WHB and SVS are Established Investigators of the American Heart Association with funds
PY - 1986/12/30
Y1 - 1986/12/30
N2 - Incubation of glomerular homogenates (200ug protein) with glomerular basement membrane (GBM, 30-35ug hydroxyproline) at pH 7.5 for 36h at 37°C resulted in significant GBM degradation as measured by hydroxyproline release (40±6%, n=17). GBM degradation increased with increasing incubation time (12-48h) and glomerular protein concentration (50-250ug). GBM degradation was not significantly decreased by inhibitors of serine or cysteine proteinases or the inhibitor of bacterial metalloproteinases, phosphoramidon. In contrast GBM degradation by glomerular homogenates was markedly inhibited by the metal chelators 10mM EDTA (-95±3%, n=7) and 2mM 1,10-phenanthroline (-96±2%, n=4). Preincubation of glomerular homogenates with trypsin (followed by soya bean trypsin inhibitor) markedly stimulated GBM degradation (+103±20%, n=11). These results document the presence of a GBM-degrading, neutral metalloproteinase(s) in glomeruli suggesting an important role for this enzyme in glomerular pathophysiology.
AB - Incubation of glomerular homogenates (200ug protein) with glomerular basement membrane (GBM, 30-35ug hydroxyproline) at pH 7.5 for 36h at 37°C resulted in significant GBM degradation as measured by hydroxyproline release (40±6%, n=17). GBM degradation increased with increasing incubation time (12-48h) and glomerular protein concentration (50-250ug). GBM degradation was not significantly decreased by inhibitors of serine or cysteine proteinases or the inhibitor of bacterial metalloproteinases, phosphoramidon. In contrast GBM degradation by glomerular homogenates was markedly inhibited by the metal chelators 10mM EDTA (-95±3%, n=7) and 2mM 1,10-phenanthroline (-96±2%, n=4). Preincubation of glomerular homogenates with trypsin (followed by soya bean trypsin inhibitor) markedly stimulated GBM degradation (+103±20%, n=11). These results document the presence of a GBM-degrading, neutral metalloproteinase(s) in glomeruli suggesting an important role for this enzyme in glomerular pathophysiology.
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U2 - 10.1016/S0006-291X(86)80127-9
DO - 10.1016/S0006-291X(86)80127-9
M3 - Article
C2 - 3101682
AN - SCOPUS:0022870539
SN - 0006-291X
VL - 141
SP - 898
EP - 903
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -