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Purification and characterization of integrin alpha 9 beta 1.

Authors: Forsberg, E  Ek, B  Engstrom, A  Johansson, S 
Citation: Forsberg E, etal., Exp Cell Res. 1994 Jul;213(1):183-90.
Pubmed: (View Article at PubMed) PMID:8020590
DOI: Full-text: DOI:10.1006/excr.1994.1189

A new beta 1-containing integrin was isolated from rat liver by affinity chromatography on Sepharose conjugated with the peptide GRGDSPC. The interaction was weakened but not abolished when the arginine and/or aspartic acid in the peptide were replaced with lysine and glutamic acid, respectively. In contrast, the cysteine was necessary for binding of the integrin. The beta 1-associated protein, referred to as alpha 9, had an N-terminal amino acid sequence related to but distinct from previously described integrin alpha-subunits. In addition, an internal peptide sequence was obtained which confirmed that the protein is a new member of the family of integrin alpha-subunits. An antiserum raised against a synthetic peptide corresponding to amino acids 1-16 of alpha 9 reacted specifically with this protein and was used to identify alpha 9 in several tissues. The integrin alpha 9 beta 1 was not retained on Sepharose conjugated with Englebreth-Holm-Swarm tumor (EHS)-laminin, collagen type I, or a 105-kDa cell-binding fragment of fibronectin. However, it did bind specifically to EHS-laminin and collagen type I adsorbed to plastic microtiter wells. The sites of the interactions were localized to fragment E8 of EHS-laminin and to cyanogen bromide fragment 8 of collagen alpha 1(I) and were not inhibited by soluble RGD-containing peptides. The results indicate that alpha 9 beta 1 is a widely distributed laminin/collagen receptor which may have additional, yet unidentified ligands.

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RGD Object Information
RGD ID: 2317878
Created: 2010-04-29
Species: All species
Last Modified: 2010-04-29
Status: ACTIVE



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