Linked Life Data

11511522

Source:http://linkedlifedata.com/resource/pubmed/id/11511522

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2001-9-4
pubmed:abstractText
Membrane-type matrix metalloproteinases-1 and -3 (MT1- and MT3-MMPs) are expressed by activated smooth muscle cells (SMCs) both in vitro and in vivo (19). To define their functions in SMCs, we transduced MT1- and MT3-MMP cDNAs into baboon SMCs by using adenoviral vectors. Overexpression of MT1-MMP increased the conversion of proMMP-2 to the intermediate and active forms. In contrast, in MT3-MMP-overexpressing cells, MMP-2 was activated partially. Immunoblot analyses revealed that MT1-MMP protein was present in the SMCs and accumulated in the presence of the synthetic MMP inhibitor, BB94, or tissue inhibitor of metalloproteinase-2 (TIMP-2). However, MT3-MMP protein was detectable only when BB94, but not TIMP-2, was present. Zymographic analyses showed that MT3-MMP had much stronger casein- and gelatin-degrading activities than did MT1-MMP. Furthermore, when MT3-MMP and MT1-MMP were coexpressed, MT1-MMP degradation was enhanced; this result supports the possibility that MT3-MMP can degrade MT1-MMP. SMCs overexpressing either MT1- or MT3-MMP exhibited altered morphology, without changing their proliferation. This alteration was prevented by BB94 addition. The cells, which underwent this change, showed reduced adhesion to both collagen and fibronectin and increased migration in a Boyden chamber. The present study demonstrates that MT1- and MT3-MMPs have different enzymatic activities but may nevertheless affect SMC function in the same way.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
15
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2010-2
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11511522-Animals, pubmed-meshheading:11511522-Cell Adhesion, pubmed-meshheading:11511522-Cell Movement, pubmed-meshheading:11511522-Cells, Cultured, pubmed-meshheading:11511522-Gene Expression, pubmed-meshheading:11511522-Humans, pubmed-meshheading:11511522-Matrix Metalloproteinase 16, pubmed-meshheading:11511522-Matrix Metalloproteinase 2, pubmed-meshheading:11511522-Matrix Metalloproteinases, Membrane-Associated, pubmed-meshheading:11511522-Metalloendopeptidases, pubmed-meshheading:11511522-Muscle, Smooth, Vascular, pubmed-meshheading:11511522-Papio, pubmed-meshheading:11511522-Phenylalanine, pubmed-meshheading:11511522-Rats, pubmed-meshheading:11511522-Thiophenes, pubmed-meshheading:11511522-Tissue Inhibitor of Metalloproteinase-2, pubmed-meshheading:11511522-Transduction, Genetic
pubmed:year
2001
pubmed:articleTitle
Membrane-type matrix metalloproteinase-1 and -3 activity in primate smooth muscle cells.
pubmed:affiliation
Division of Vascular Surgery, Department of Surgery, University of Washington School of Medicine, 1959 NE Pacific St., Seattle, WA 98195-6410, USA.
pubmed:publicationType
Journal Article