|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
13
|
|
pubmed:dateCreated |
2004-3-22
|
|
pubmed:databankReference |
|
|
pubmed:abstractText |
Membrane-type 1 matrix metalloproteinase (MT1-MMP/MMP-14) is an enzyme that promotes tumor cell invasion in tissues. Although the proteolytic activity of MT1-MMP is indispensable for invasion, it is also regulated by functions of the cytoplasmic tail. In this study we obtained a new human gene whose product binds to the tail sequence in yeast. The product, MTCBP-1, is a 19-kDa protein that belongs to the newly proposed Cupin superfamily composed of proteins with diverse functions. MTCBP-1 expressed in cells formed a complex with MT1-MMP and co-localized at the membrane. It was also detected in both the cytoplasm and nucleus, where MT1-MMP does not exist. In human tumor cell lines MTCBP-1 expression was significantly low compared with non-transformed fibroblasts, and enforced expression of MTCBP-1 inhibited the activity of MT1-MMP in promoting cell migration and invasion. MTCBP-1 showed significant homology to the bacterial aci-reductone dioxygenase, which is an enzyme in methionine metabolism. The C-terminal part of MTCBP-1 is identical to Sip-L, which is reported to be important for human hepatitis C virus replication. Thus, MTCBP-1 may have multiple functions other than the regulation of MT1-MMP, which presumably depends on the subcellular compartment.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Dioxygenases,
http://linkedlifedata.com/resource/pubmed/chemical/Drug Combinations,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases...,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/matrigel
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Mar
|
|
pubmed:issn |
0021-9258
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
26
|
|
pubmed:volume |
279
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
12734-43
|
|
pubmed:dateRevised |
2010-5-21
|
|
pubmed:meshHeading |
pubmed-meshheading:14718544-Amino Acid Sequence,
pubmed-meshheading:14718544-Animals,
pubmed-meshheading:14718544-Base Sequence,
pubmed-meshheading:14718544-Blotting, Northern,
pubmed-meshheading:14718544-Blotting, Western,
pubmed-meshheading:14718544-COS Cells,
pubmed-meshheading:14718544-Carrier Proteins,
pubmed-meshheading:14718544-Cell Line,
pubmed-meshheading:14718544-Cell Line, Tumor,
pubmed-meshheading:14718544-Cell Membrane,
pubmed-meshheading:14718544-Cell Movement,
pubmed-meshheading:14718544-Cell Nucleus,
pubmed-meshheading:14718544-Collagen,
pubmed-meshheading:14718544-Cytoplasm,
pubmed-meshheading:14718544-DNA, Complementary,
pubmed-meshheading:14718544-Dioxygenases,
pubmed-meshheading:14718544-Down-Regulation,
pubmed-meshheading:14718544-Drug Combinations,
pubmed-meshheading:14718544-Fibroblasts,
pubmed-meshheading:14718544-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:14718544-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:14718544-Humans,
pubmed-meshheading:14718544-Laminin,
pubmed-meshheading:14718544-Matrix Metalloproteinases, Membrane-Associated,
pubmed-meshheading:14718544-Metalloendopeptidases,
pubmed-meshheading:14718544-Microscopy, Fluorescence,
pubmed-meshheading:14718544-Molecular Sequence Data,
pubmed-meshheading:14718544-Multigene Family,
pubmed-meshheading:14718544-Neoplasm Invasiveness,
pubmed-meshheading:14718544-Open Reading Frames,
pubmed-meshheading:14718544-Peptides,
pubmed-meshheading:14718544-Plasmids,
pubmed-meshheading:14718544-Precipitin Tests,
pubmed-meshheading:14718544-Protein Structure, Tertiary,
pubmed-meshheading:14718544-Proteoglycans,
pubmed-meshheading:14718544-RNA, Messenger,
pubmed-meshheading:14718544-Recombinant Proteins,
pubmed-meshheading:14718544-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:14718544-Sequence Homology, Amino Acid,
pubmed-meshheading:14718544-Subcellular Fractions,
pubmed-meshheading:14718544-Transfection,
pubmed-meshheading:14718544-Tumor Suppressor Proteins,
pubmed-meshheading:14718544-Two-Hybrid System Techniques
|
|
pubmed:year |
2004
|
|
pubmed:articleTitle |
Membrane-type 1 matrix metalloproteinase cytoplasmic tail-binding protein-1 is a new member of the Cupin superfamily. A possible multifunctional protein acting as an invasion suppressor down-regulated in tumors.
|
|
pubmed:affiliation |
Division of Cancer Cell Research, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokane-dai, Minato-ku, Tokyo 108-8639, Japan.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
