Linked Life Data

7540230

Source:http://linkedlifedata.com/resource/pubmed/id/7540230

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1995-7-17
pubmed:abstractText
We examined the role of the plasminogen activator/plasmin system in extracellular matrix (ECM) degradation by human mesangial cells cultured on thin films of 125I-labeled ECM (Matrigel). ECM degradation (release of 125I into the medium) was dependent on exogenous plasminogen, proportional to the number of mesangial cells and amount of plasminogen added, and coincident with the appearance of plasmin in the medium. ECM degradation was completely blocked (P < 0.001) by two plasmin inhibitors, alpha-2-antiplasmin (40 micrograms/ml) and aprotinin (216 KIU/ml), and partially reduced (-33 +/- 1.8%, P < 0.01) by TIMP-1 (40 micrograms/ml), a specific inhibitor of matrix metalloproteinases. Zymography of medium obtained from cells cultured in the absence of plasminogen revealed the presence of latent matrix metalloproteinase-2 (MMP-2) which was converted to a lower molecular weight, active form in the presence of mesangial cells and plasminogen. Northern analysis of poly A+RNA prepared from cultured human mesangial cells revealed mRNA for tissue-type plasminogen activator (tPA), urokinase-type plasminogen activator (uPA), plasminogen activator inhibitor-1 (PAI-1), and uPA receptor (uPAR). The presence of uPA protein in medium obtained from cultured human mesangial cells was demonstrated by Western blotting and ELISA which revealed a large molar excess of PAI-1 (1.2 +/- 0.1 x 10(-9) M) over uPA (1.2 +/- 0.1 x 10(-12) M) and tPA (0.19 +/- 0.04 x 10(-9) M). ECM degradation was reduced by a monoclonal antibody (MAb) against human tPA (-54 +/- 8.6%) or human uPA (-39 +/- 5.2%) compared to cells treated with identical amounts of non-specific monoclonal IgG (P < 0.01).(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0085-2538
pubmed:author
pubmed:issnType
Print
pubmed:volume
47
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1039-47
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:7540230-Aprotinin, pubmed-meshheading:7540230-Blotting, Northern, pubmed-meshheading:7540230-Blotting, Western, pubmed-meshheading:7540230-Cells, Cultured, pubmed-meshheading:7540230-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:7540230-Extracellular Matrix, pubmed-meshheading:7540230-Extracellular Space, pubmed-meshheading:7540230-Fibrinolysin, pubmed-meshheading:7540230-Gelatinases, pubmed-meshheading:7540230-Glomerular Mesangium, pubmed-meshheading:7540230-Glycoproteins, pubmed-meshheading:7540230-Humans, pubmed-meshheading:7540230-Matrix Metalloproteinase 2, pubmed-meshheading:7540230-Metalloendopeptidases, pubmed-meshheading:7540230-Plasminogen, pubmed-meshheading:7540230-Plasminogen Activators, pubmed-meshheading:7540230-Tissue Inhibitor of Metalloproteinases, pubmed-meshheading:7540230-alpha-2-Antiplasmin
pubmed:year
1995
pubmed:articleTitle
ECM degradation by cultured human mesangial cells is mediated by a PA/plasmin/MMP-2 cascade.
pubmed:affiliation
Department of Biochemistry, Tulane Medical School, New Orleans, Louisiana, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't