Linked Life Data

10363975

Source:http://linkedlifedata.com/resource/pubmed/id/10363975

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1999-6-29
pubmed:databankReference
pubmed:abstractText
A cDNA encoding a new member of the membrane-type (MT) matrix metalloproteinase (MMP) family has been identified and cloned from a human brain cDNA library. The isolated cDNA encodes a polypeptide of 645 amino acids that displays a similar domain organization as other MMPs, including a predomain with the activation locus, a zinc-binding site, and a hemopexin domain. The deduced amino acid sequence contains a COOH-terminal extension, rich in hydrophobic residues and similar in size to the equivalent domains identified in MT-MMPs. Immunofluorescence and Western blot analysis of COS-7 cells transfected with the isolated cDNA revealed that the encoded protein is localized in the plasma membrane. On the basis of these features, this novel human MMP has been called MT5-MMP because it represents the fifth member of the MT-MMP subfamily of MMPs. Fluorescent in situ hybridization experiments showed that the human MT5-MMP gene (MMP-24) maps to 20q11.2, a region frequently amplified in tumors from diverse sources. Northern blot analysis demonstrated that MT5-MMP is predominantly expressed in brain, kidney, pancreas, and lung. In addition, MT5-MMP transcripts were detected at high levels compared to normal brain tissue in a series of brain tumors, including astrocytomas and glioblastomas. The catalytic domain of MT5-MMP, produced in Escherichia coli as a fusion protein with glutathione S-transferase, exhibits a potent proteolytic activity against progelatinase A, leading to the generation of the Mr 62,000 active form of this enzyme. These data suggest that MT5-MMP may contribute to the activation of progelatinase A in tumor tissues, in which it is overexpressed, thereby facilitating tumor progression.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0008-5472
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2570-6
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed-meshheading:10363975-Amino Acid Sequence, pubmed-meshheading:10363975-Animals, pubmed-meshheading:10363975-Base Sequence, pubmed-meshheading:10363975-Blotting, Western, pubmed-meshheading:10363975-Brain Neoplasms, pubmed-meshheading:10363975-COS Cells, pubmed-meshheading:10363975-Chromosome Mapping, pubmed-meshheading:10363975-Chromosomes, Human, Pair 20, pubmed-meshheading:10363975-DNA, Complementary, pubmed-meshheading:10363975-DNA Probes, pubmed-meshheading:10363975-Enzyme Activation, pubmed-meshheading:10363975-Enzyme Precursors, pubmed-meshheading:10363975-Gelatinases, pubmed-meshheading:10363975-Genetic Vectors, pubmed-meshheading:10363975-Humans, pubmed-meshheading:10363975-Matrix Metalloproteinases, Membrane-Associated, pubmed-meshheading:10363975-Metalloendopeptidases, pubmed-meshheading:10363975-Molecular Sequence Data, pubmed-meshheading:10363975-Neoplasm Proteins, pubmed-meshheading:10363975-Transfection
pubmed:year
1999
pubmed:articleTitle
Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors.
pubmed:affiliation
Departamento de Bioquimica y Biologia Molecular, Facultad de Medicina, Universidad de Oviedo, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't