Identification of a novel truncated alphaIIb integrin.
Integrin alphaIIb beta3 requires its cytoplasmic tails to participate in tumor cell adhesion, spreading, and migration. Using 3' rapid amplification of cDNA ends, we have amplified two alphaIIb cDNAs from human leukemia, prostate adenocarcinoma, and melanoma cells. One of these is the predicted wild-type alphaIIb cDNA, and the other is a novel truncated alphaIIb variant. This variant is unique in that it lacks the transmembrane and cytoplasmic portions of the alphaIIb light chain. The truncated alphaIIb integrin protein is expressed by human leukemia, prostate adenocarcinoma, and melanoma cells but not by platelets or normal prostate epithelial or normal breast epithelial cells. Tumor cells secrete this protein and deposit it on the extracellular matrix. To our knowledge, this is the first report of a naturally occurring variant of an alpha integrin that lacks the transmembrane and cytoplasmic tail.
Trikha
M
M
Department of Radiation Oncology, Wayne State University, and Barbara Ann Karmanos Cancer Center, Detroit, Michigan 48202, USA.
Cai
Y
Y
Grignon
D
D
Honn
K V
KV
D017398:Alternative Splicing; D000595:Amino Acid Sequence; D001483:Base Sequence; D018076:DNA, Complementary / Q000032:analysis; D006801:Humans; D007150:Immunohistochemistry; D007938:Leukemia / Q000378:metabolism; D008297:Male; D008545:Melanoma / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009369:Neoplasms / Q000737:chemistry*; D019039:Platelet Glycoprotein GPIIb-IIIa Complex / Q000032:analysis* / Q000235:genetics; D011471:Prostatic Neoplasms / Q000737:chemistry; D014176:Protein Biosynthesis; D014407:Tumor Cells, Cultured
D018076:DNA, Complementary; D019039:Platelet Glycoprotein GPIIb-IIIa Complex