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Enhanced phosphoinositide metabolism in colorectal carcinoma cells derived from familial adenomatous polyposis patients
Author(s) -
Homma Miwako K.,
Homma Yoshimi,
Namba Masayoshi,
Yuasa Yasuhito
Publication year - 1994
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240550407
Subject(s) - inositol , phosphatidylinositol , familial adenomatous polyposis , second messenger system , cancer research , diacylglycerol kinase , inositol trisphosphate , tyrosine phosphorylation , medicine , biology , carcinogenesis , endocrinology , phosphorylation , signal transduction , colorectal cancer , protein kinase c , receptor , microbiology and biotechnology , cancer
The production of the second messenger molecules diacylglycerol and inositol 1,4,5‐trisphosphate is mediated by activated phosphatidylinositol‐specific phospholipase C (PLC) enzymes. We report the enhancement of the phosphoinositide metabolism pathway in KMS‐4 and KMS‐8 cells, both of which are human colorectal carcinoma cell lines derived from familial adenomatous polyposis patients. In these cells, the cellular contents of diacylglycerol and inositol 1,4,5‐trisphosphate were constitutively increased and the PLC activity in vitro was significantly high, as compared with those in normal colon cells or in other sporadic colorectal carcinoma cells. Northern and Western analyses showed the high expression levels of both PLC‐γ1 and PLC‐δ1 in KMS‐4 and KMS‐8 cells. Moreover, we detected the enhancement of protein–tyrosine kinase activity and tyrosine phosphorylation of PLC‐γ1 in these KMS cells. These results suggest the involvement of activated phosphoinositide signaling pathways in the colorectal tumorigenesis of familial adenomatous polyposis. © 1994 Wiley‐Liss, Inc.