Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
37
pubmed:dateCreated
1995-10-12
pubmed:databankReference
pubmed:abstractText
We have isolated and characterized overlapping cDNA clones encoding the alpha 3A and alpha 3B chains of mouse laminin 5. Sequence analysis of the cDNA for the alpha 3B predicts a polypeptide of 2541 amino acids (279,510 Da) comprising a truncated short arm and a carboxyl-terminal long arm common to the laminin alpha chains identified thus far. The short arm of the alpha 3B chain harbors two alternating epidermal growth factor-like domains and two globular domains. The amino-terminal globular domain, thought to mediate interactions with molecules of the extracellular matrix, shows no significant homology to any globular domain at the tips of the known laminin isoforms. The alpha 3A cDNA predicts a polypeptide of 1711 amino acids (186,230 Da) that substitutes a short sequence of 43 amino acids for the short arm seen in the alpha 3B isoform and displays 77% conservative homology to the alpha 3Ep chains of the adhesion ligand epiligrin. Northern and Western blot analyses of skin and lung epithelial cells demonstrated the tissue-specific expression of the laminin alpha 3A and alpha 3B isoforms, and in situ hybridization on mouse embryos revealed a focal localization of alpha 3B in areas of the central nervous system.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21820-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7665604-Amino Acid Sequence, pubmed-meshheading:7665604-Animals, pubmed-meshheading:7665604-Base Sequence, pubmed-meshheading:7665604-Cloning, Molecular, pubmed-meshheading:7665604-DNA, Complementary, pubmed-meshheading:7665604-DNA Primers, pubmed-meshheading:7665604-DNA Probes, pubmed-meshheading:7665604-Drosophila, pubmed-meshheading:7665604-Gene Expression, pubmed-meshheading:7665604-Gene Library, pubmed-meshheading:7665604-Humans, pubmed-meshheading:7665604-In Situ Hybridization, pubmed-meshheading:7665604-Laminin, pubmed-meshheading:7665604-Lung, pubmed-meshheading:7665604-Macromolecular Substances, pubmed-meshheading:7665604-Mice, pubmed-meshheading:7665604-Molecular Sequence Data, pubmed-meshheading:7665604-Organ Specificity, pubmed-meshheading:7665604-Polymerase Chain Reaction, pubmed-meshheading:7665604-Recombinant Proteins, pubmed-meshheading:7665604-Restriction Mapping, pubmed-meshheading:7665604-Sequence Homology, Amino Acid, pubmed-meshheading:7665604-Sequence Homology, Nucleic Acid
pubmed:year
1995
pubmed:articleTitle
Cloning and complete primary structure of the mouse laminin alpha 3 chain. Distinct expression pattern of the laminin alpha 3A and alpha 3B chain isoforms.
pubmed:affiliation
U385 INSERM, Faculté de Médecine, Nice, France.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't