Adhesiveness of beta5 integrin variant lacking FNK767-769 is similar to that of the prototype containing FNKFNK764-769

Little is known about the functions of two different beta5 integrins: repeated-FNK (FNKFNK764-769) and single-FNK (FNK764-766) amino acid sequences in the cytoplasmic domain. We examined whether they occurred as germ line mutations or somatic mutations associated with neoplastic transformation, and...

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Bibliographic Details
Published in:Cell biology international 2005-07, Vol.29 (7), p.521-528
Main Authors: Kawahara, Ei, Saito, Ayumi, Kobayashi, Jun, Maenaka, Shiori, Minamoto, Toshinari, Imai, Miwa Akasofu, Oda, Yoshio
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Cell Adhesion - genetics
Cell Line, Tumor
Cell Proliferation
CHO Cells
Colonic Neoplasms
Cricetinae
Cricetulus
Genetic Variation
Germ-Line Mutation
Humans
Integrin beta Chains - chemistry
Integrin beta Chains - genetics
Integrin beta Chains - metabolism
Membrane Proteins - genetics
Molecular Sequence Data
Polymorphism, Genetic
Protein Structure, Tertiary
RNA, Messenger - analysis
Transfection
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Summary:Little is known about the functions of two different beta5 integrins: repeated-FNK (FNKFNK764-769) and single-FNK (FNK764-766) amino acid sequences in the cytoplasmic domain. We examined whether they occurred as germ line mutations or somatic mutations associated with neoplastic transformation, and whether there were functional alterations. Out of six cultured cell lines, only KATO-III cells had the single-FNK beta5 sequence. The single-FNK beta5 was found in 9 out of 79 patients with colon carcinoma, but no somatic mutations were detected in cancerous tissues. CHO cells were transformed with expression vectors containing single-FNK or repeated-FNK beta5 cDNA, which were derived from KATO-III cells. CHO cells transfected with single-FNK and repeated-FNK showed similar adhesiveness to, and proliferative activity on, vitronectin substrates.
ISSN:1065-6995