Sequence and tissue distribution of the integrin alpha 9 subunit, a novel partner of beta 1 that is widely distributed in epithelia and muscle

Détails

ID Serval
serval:BIB_00A7AB538416
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Sequence and tissue distribution of the integrin alpha 9 subunit, a novel partner of beta 1 that is widely distributed in epithelia and muscle
Périodique
Journal of Cell Biology
Auteur(s)
Palmer  E. L., Ruegg  C., Ferrando  R., Pytela  R., Sheppard  D.
ISSN
0021-9525 (Print)
Statut éditorial
Publié
Date de publication
12/1993
Volume
123
Numéro
5
Pages
1289-97
Notes
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S. --- Old month value: Dec
Résumé
The integrin family of adhesion receptors consists of several heterodimeric glycoproteins, each composed of one alpha and one beta subunit. A novel integrin alpha subunit partial cDNA isolated from TGF-beta stimulated guinea pig airway epithelial cells has previously been reported (Erle, D.J., D. Sheppard, J. Bruess, C. Ruegg, and R. Pytela. 1991. Am. J. Respir. Cell Mol. Biol. 5:170-177). We have now determined cDNA and amino acid sequence for the human homolog of this subunit, named alpha 9, from a human lung cDNA library, a human small intestine cDNA library, and cDNA from the cell lines U937, HL-60 and Tera-2. This sequence is predicted to encode a 1006-amino acid mature protein that shares 39% identity with the previously identified integrin subunit alpha 4. By Northern blot analysis, alpha 9 mRNA was detected in the human carcinoma cell lines Tera-2 and Caco-2. Anti-peptide antibodies against the predicted COOH-terminal sequence of alpha 9 immunoprecipitated a heterodimer (140 kD/115 kD nonreduced; 150 kD/130 kD reduced) from Tera-2 lysates. Immunodepletion of beta 1-containing integrins with Tera-2 lysates removed alpha 9 immunoreactivity, suggesting that beta 1 is the principal beta subunit partner for alpha 9 in these cells. alpha 9 was detected by immunohistochemistry in airway epithelium, in the basal layer of squamous epithelium, and in smooth muscle, skeletal muscle, and hepatocytes.
Mots-clé
Amino Acid Sequence Animals Base Sequence Cloning, Molecular Dna Epithelium/metabolism Humans *Integrin alpha Chains Integrins/*genetics/metabolism Liver/cytology/metabolism Mice Molecular Sequence Data Muscles/*metabolism Sequence Analysis Sequence Homology, Amino Acid Tumor Cells, Cultured
Pubmed
Web of science
Open Access
Oui
Création de la notice
28/01/2008 9:36
Dernière modification de la notice
08/05/2019 13:39
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