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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
1995-7-28
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pubmed:databankReference | |
pubmed:abstractText |
Laminins are a family of heterotrimeric glycoproteins specific to basement membranes. Laminin-2, consisting of alpha 2, beta 1 and gamma 1 chains, was originally identified in the basement membranes of skeletal muscle and peripheral nerve. We have isolated and sequenced the full-length cDNA for the mouse laminin alpha 2 chain. Four overlapping clones spanning 9,330 bp encode a predicted polypeptide of 3,106 amino acids having a calculated molecular mass of 390 kDa including a 23-amino-acid signal peptide. The amino acid sequence of the alpha 2 chain shares a 45.9% identify with that of the alpha 1 chain. Similar to the structure of the alpha 1 chain, the alpha 2 chain consists of several domains beginning at the N-terminus with three globular domains alternating with three epidermal growth factor-like domains followed by two alpha-helical domains and a C-terminal globular domain. The most N-terminal globular domain is highly conserved (77.3% identity) between the alpha 2 and alpha 1 chains, whereas the alpha-helical domains have low homology (30.3% identity). Northern blot and ribonuclease protection analysis revealed expression of mRNA for the alpha 2 chain in heart, kidney, liver, skin, lung and skeletal muscle of newborn mice. such a tissue distribution suggests a role for the alpha 2 chain and, consequently, laminin-2 or -4 not only in the organization and the function of nerve and muscle tissue but possibly also in the mesenchymal components of certain tissues.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0945-053X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
447-55
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7795883-Amino Acid Sequence,
pubmed-meshheading:7795883-Animals,
pubmed-meshheading:7795883-Base Sequence,
pubmed-meshheading:7795883-Cloning, Molecular,
pubmed-meshheading:7795883-DNA, Complementary,
pubmed-meshheading:7795883-Gene Expression,
pubmed-meshheading:7795883-Laminin,
pubmed-meshheading:7795883-Mice,
pubmed-meshheading:7795883-Molecular Sequence Data,
pubmed-meshheading:7795883-Organ Specificity,
pubmed-meshheading:7795883-RNA, Messenger,
pubmed-meshheading:7795883-Sequence Alignment,
pubmed-meshheading:7795883-Sequence Homology, Amino Acid
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pubmed:year |
1995
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pubmed:articleTitle |
Cloning and expression of laminin alpha 2 chain (M-chain) in the mouse.
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pubmed:affiliation |
Laboratory of Development of Biology, National Institute of Dental Research, Bethesda, Maryland, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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