Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
41
pubmed:dateCreated
1996-11-19
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
271
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25548-54
pubmed:dateRevised
2007-11-14
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
pubmed:year
1996
pubmed:articleTitle
Cloning and developmental expression of a membrane-type matrix metalloproteinase from chicken.
pubmed:affiliation
Center for Molecular Medicine and Genetics, Wayne State University School of Medicine, Detroit, Michigan 48202, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.