Linked Life Data

7559440

Source:http://linkedlifedata.com/resource/pubmed/id/7559440

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
39
pubmed:dateCreated
1995-11-6
pubmed:databankReference
pubmed:abstractText
Membrane-type matrix metalloproteinase (MT-MMP), which we have identified recently, is unique in its transmembrane (TM) domain at the C terminus and mediates activation of pro-gelatinase A on the cell surface (Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E., and Seiki, M. (1994) Nature 370, 61-65; Takino, T., Sato, H., Yamamoto, E., and Seiki, M. (1995) Gene (Amst.) 115, 293-298). In addition to MT-MMP, a novel MMP-related cDNA of 2.1 kilobases was isolated from a human placenta cDNA library. The cDNA contains an open reading frame for a new MMP. The deduced protein composed of 604 amino acids was closely related to MT-MMP in the amino acid sequence (66% homology at the catalytic domains) and has a potential TM domain at the C terminus. Monoclonal antibodies raised against the synthetic peptide recognized a 64-kDa protein as the major product in the transfected cells. TIMP-1 fused with the potential TM domain was localized on the cell surface while native TIMP-1 is in the culture medium. Thus, we called the second membrane-type MMP, MT-MMP-2 and renamed MT-MMP, MT-MMP-1. MT-MMP-1 and -2 are thought to form a distinct membrane-type subclass in the MMP family since all the others are secreted as soluble forms. Like MT-MMP-1, expression of MT-MMP-2 induced processing of pro-gelatinase A (68-kDa in gelatin zymography) into the activated form of 62-kDa fragments through a 64-kDa intermediate form. Expression of MT-MMP-2 mRNA was at the highest levels in the brain where MT-MMP-1 was at the lowest level compared to other tissues. MT-MMP-1 and -2 are thought to be utilized for extracellular matrix turnover on the surface of cells under different genetic controls.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
29
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
23013-20
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7559440-Amino Acid Sequence, pubmed-meshheading:7559440-Animals, pubmed-meshheading:7559440-Antibodies, Monoclonal, pubmed-meshheading:7559440-Base Sequence, pubmed-meshheading:7559440-Cell Line, pubmed-meshheading:7559440-Cell Membrane, pubmed-meshheading:7559440-Cercopithecus aethiops, pubmed-meshheading:7559440-DNA, Complementary, pubmed-meshheading:7559440-Epitopes, pubmed-meshheading:7559440-Female, pubmed-meshheading:7559440-Fluorescent Antibody Technique, Indirect, pubmed-meshheading:7559440-Gelatinases, pubmed-meshheading:7559440-Gene Library, pubmed-meshheading:7559440-Humans, pubmed-meshheading:7559440-Matrix Metalloproteinase 2, pubmed-meshheading:7559440-Metalloendopeptidases, pubmed-meshheading:7559440-Mice, pubmed-meshheading:7559440-Molecular Sequence Data, pubmed-meshheading:7559440-Multigene Family, pubmed-meshheading:7559440-Mutagenesis, Insertional, pubmed-meshheading:7559440-Placenta, pubmed-meshheading:7559440-Pregnancy, pubmed-meshheading:7559440-Recombinant Proteins, pubmed-meshheading:7559440-Sequence Homology, Amino Acid
pubmed:year
1995
pubmed:articleTitle
Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family.
pubmed:affiliation
Department of Molecular Virology and Oncology, Kanazawa University, Ishikawa, Japan.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't