cDNA sequence of the human integrin beta 5 subunit.
A novel integrin receptor involved in cell adhesion to the matrix protein vitronectin has recently been described from a human lung epithelial-derived cell line (Cheresh, D. A., Smith, J. W., Cooper, H. M., and Quaranta, V. (1989) Cell 57, 59-69). This receptor has an alpha subunit that appears identical to the alpha v of the vitronectin receptor alpha v beta 3 expressed in melanoma and endothelial cells, but is complexed with a distinct beta subunit, beta 5. cDNA clones coding for beta 5 have been isolated and used to determine the mRNA and amino acid sequence of this new subunit. A 3.3-kilobase mRNA was found to code for a mature protein of 775 amino acid residues with a hydrophobic leader sequence of 24 amino acids. A 56% identity was found between the beta 5 and beta 3 protein sequences, making them the most closely related of the integrin beta subunits. Polymerase chain reaction abundance analysis revealed that alpha v and beta 5 mRNAs were found in seven very different cell lines, compared with beta 3 mRNA which was found in only three of the them, indicating that this new integrin receptor may be widely distributed.
Department of Cardiovascular Research, Genentech Inc., South San Francisco, California 94080.
J W
JW
McLean
D J
DJ
Vestal
D A
DA
Cheresh
S C
SC
Bodary
D000595:Amino Acid Sequence; D001483:Base Sequence; D015152:Blotting, Northern; D002460:Cell Line; D003001:Cloning, Molecular; D004273:DNA, Neoplasm / Q000235:genetics* / Q000302:isolation & purification; D006801:Humans; D016023:Integrins / Q000235:genetics* / Q000302:isolation & purification; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009369:Neoplasms; D015345:Oligonucleotide Probes; D012333:RNA, Messenger / Q000235:genetics / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid
D004273:DNA, Neoplasm; D016023:Integrins; D046911:Macromolecular Substances; D015345:Oligonucleotide Probes; D012333:RNA, Messenger