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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1997-4-7
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pubmed:databankReference | |
pubmed:abstractText |
Embryonic development involves a series of cell adhesive interactions that provide mechanical and instructive information required for morphogenesis. The ADAMs family of membrane-anchored proteins, containing a disintegrin and metalloprotease domain, is well suited for participating in such developmental events. They encode not only a potential adhesive function, through an integrin-binding disintegrin domain, but also a potential antiadhesive function, through a zinc-dependent metalloprotease domain. In order to investigate the role of ADAMs in early development we cloned a cDNA encoding a novel member of the ADAM family from a Xenopus laevis neurula stage library. We call this cDNA, and the 915-amino-acid protein it encodes, ADAM 13, X-ADAM 13 RNA is expressed during embryogenesis from the midblastula stage through tadpole stage 45. X-ADAM 13 is localized to somitic mesoderm and cranial neural crest cells during gastrulation, neurulation, and in tail bud stages. Sequence analyses of the X-ADAM 13 metalloprotease and disintegrin domains indicate that the protein is likely to be involved in both proteolytic and cell-adhesive functions. The X-ADAM 13 sequence is most closely related to that of mouse meltrin alpha, which is implicated in myoblast fusion. Our data suggest that X-ADAM 13 may be involved in neural crest cell adhesion and migration as well as myoblast differentiation.
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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/ADAM Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Disintegrins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Metalloendopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0012-1606
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
182
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
314-30
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pubmed:dateRevised |
2009-9-2
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pubmed:meshHeading |
pubmed-meshheading:9070330-3T3 Cells,
pubmed-meshheading:9070330-ADAM Proteins,
pubmed-meshheading:9070330-Amino Acid Sequence,
pubmed-meshheading:9070330-Animals,
pubmed-meshheading:9070330-Cloning, Molecular,
pubmed-meshheading:9070330-DNA, Complementary,
pubmed-meshheading:9070330-Disintegrins,
pubmed-meshheading:9070330-Embryo, Nonmammalian,
pubmed-meshheading:9070330-Humans,
pubmed-meshheading:9070330-Mammals,
pubmed-meshheading:9070330-Membrane Proteins,
pubmed-meshheading:9070330-Metalloendopeptidases,
pubmed-meshheading:9070330-Mice,
pubmed-meshheading:9070330-Molecular Sequence Data,
pubmed-meshheading:9070330-Neural Crest,
pubmed-meshheading:9070330-RNA, Messenger,
pubmed-meshheading:9070330-Sequence Homology, Amino Acid,
pubmed-meshheading:9070330-Somites,
pubmed-meshheading:9070330-Xenopus Proteins,
pubmed-meshheading:9070330-Xenopus laevis
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pubmed:year |
1997
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pubmed:articleTitle |
ADAM 13: a novel ADAM expressed in somitic mesoderm and neural crest cells during Xenopus laevis development.
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pubmed:affiliation |
Department of Cell Biology, Health Sciences Center, University of Virginia, Charlottesville 22908, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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