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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
41
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pubmed:dateCreated |
1996-11-19
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pubmed:abstractText |
We have cloned a novel matrix metalloproteinase (MMP) from cultured chicken embryo fibroblasts. The cDNA-derived protein sequence contains 608 amino acids including a C-terminal hydrophobic transmembrane domain of 24 amino acids and a cytoplasmic domain of 20 amino acids. This chicken MMP is 72% similar to a recently described membrane-type MMP (MT-MMP) from human placenta (Sato, H., Takino, T., Okada, Y., Cao, J., Shinagawa, A., Yamamoto, E., and Seiki, M. (1994) Nature 370, 61-65). Accordingly, we name this novel MMP chicken MT-MMP. As shown by Northern blotting, two MT-MMP mRNAs of 6 and 10 kilobases are constitutively expressed but only modestly regulated by growth factors and cytokines in cultured chicken embryo fibroblasts. Both mRNAs are abundant in the head and body of 8- and 9-day-old chicken embryos. As shown by in situ mRNA hybridization, MT-MMP is expressed in embryonic neural tube, spinal ganglia, and respiratory epithelium, as well as in developing cartilage and muscle. Using reverse transcription-polymerase chain reaction, we have found MT-MMP mRNA in 2-day-old chicken embryos and extraembryonic membranes. In addition, a strong correlation was observed between the mRNA expression of MT-MMP and 72-kDa type IV collagenase. Collectively, the early MT-MMP mRNA expression and its co-localization in several tissues with 72-kDa type IV collagenase mRNA suggest that the MT-MMP plays an important role in early development.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases...,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
271
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
25548-54
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8810327-Amino Acid Sequence,
pubmed-meshheading:8810327-Animals,
pubmed-meshheading:8810327-Base Sequence,
pubmed-meshheading:8810327-Chick Embryo,
pubmed-meshheading:8810327-Chickens,
pubmed-meshheading:8810327-Cloning, Molecular,
pubmed-meshheading:8810327-Consensus Sequence,
pubmed-meshheading:8810327-DNA Primers,
pubmed-meshheading:8810327-Female,
pubmed-meshheading:8810327-Fibroblasts,
pubmed-meshheading:8810327-Ganglia, Spinal,
pubmed-meshheading:8810327-Gene Expression Regulation, Developmental,
pubmed-meshheading:8810327-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:8810327-Humans,
pubmed-meshheading:8810327-Matrix Metalloproteinases, Membrane-Associated,
pubmed-meshheading:8810327-Metalloendopeptidases,
pubmed-meshheading:8810327-Molecular Sequence Data,
pubmed-meshheading:8810327-Nervous System,
pubmed-meshheading:8810327-Placenta,
pubmed-meshheading:8810327-Polymerase Chain Reaction,
pubmed-meshheading:8810327-Pregnancy,
pubmed-meshheading:8810327-Protein Sorting Signals,
pubmed-meshheading:8810327-RNA, Messenger,
pubmed-meshheading:8810327-Recombinant Proteins,
pubmed-meshheading:8810327-Sequence Homology, Amino Acid
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pubmed:year |
1996
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pubmed:articleTitle |
Cloning and developmental expression of a membrane-type matrix metalloproteinase from chicken.
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pubmed:affiliation |
Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48202, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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