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.
McLean
J W
JW
Department of Cardiovascular Research, Genentech Inc., South San Francisco, California 94080.
Vestal
D J
DJ
Cheresh
D A
DA
Bodary
S C
SC
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