Linked Life Data

8663054

Source:http://linkedlifedata.com/resource/pubmed/id/8663054

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1996-8-13
pubmed:abstractText
A biologic role for the 72-kDa gelatinase A (matrix metalloproteinase 2; MMP-2), beyond simple extracellular matrix turnover, was evaluated in glomerular mesangial cells. To determine the significance of MMP-2 secretion for the acquisition of the inflammatory phenotype, we reduced the constitutive secretion of MMP-2 by cultured mesangial cells with antisense RNA expressed by an episomally replicating vector or with specific anti-MMP-2 ribozymes expressed by a retroviral transducing vector. The phenotype of the transfected, or retrovirally infected, cells was profoundly altered from the activated state and closely approximated that of quiescent cells in vivo. The prominent differences included a change in the synthesis and organization of the extracellular matrix, loss of activation markers, and a virtually total exit from the cell cycle. Reconstitution with exogenous active, but not latent MMP-2, induced a rapid return to the inflammatory phenotype in vitro. This effect was specific to MMP-2, because the closely related MMP-9 did not reproduce these changes. Furthermore, this pro-inflammatory effect of MMP-2 is dependent upon the active form of the enzyme, which can be produced by an autocatalytic activation process on the mesangial cell plasma membrane. It is concluded that MMP-2 acts directly upon mesangial cells to permit the development of an inflammatory phenotype. Specific inhibition of MMP-2 activity in vivo may represent an alternate means of ameliorating complex inflammatory processes by affecting the phenotype of the synthesizing cells, per se.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15074-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8663054-Animals, pubmed-meshheading:8663054-Base Sequence, pubmed-meshheading:8663054-Cell Differentiation, pubmed-meshheading:8663054-Cell Division, pubmed-meshheading:8663054-Cells, Cultured, pubmed-meshheading:8663054-Collagen, pubmed-meshheading:8663054-DNA Primers, pubmed-meshheading:8663054-Gelatinases, pubmed-meshheading:8663054-Genetic Vectors, pubmed-meshheading:8663054-Glomerular Mesangium, pubmed-meshheading:8663054-Matrix Metalloproteinase 2, pubmed-meshheading:8663054-Metalloendopeptidases, pubmed-meshheading:8663054-Microscopy, Immunoelectron, pubmed-meshheading:8663054-Molecular Sequence Data, pubmed-meshheading:8663054-Oligodeoxyribonucleotides, pubmed-meshheading:8663054-Open Reading Frames, pubmed-meshheading:8663054-RNA, Antisense, pubmed-meshheading:8663054-RNA, Catalytic, pubmed-meshheading:8663054-Rats, pubmed-meshheading:8663054-Restriction Mapping, pubmed-meshheading:8663054-Retroviridae, pubmed-meshheading:8663054-Transcription, Genetic, pubmed-meshheading:8663054-Transfection
pubmed:year
1996
pubmed:articleTitle
Matrix metalloproteinase 2 (gelatinase A) regulates glomerular mesangial cell proliferation and differentiation.
pubmed:affiliation
Department of Medicine, San Francisco Veterans Affairs Medical Center and University of California, San Francisco, California 94121, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't