Suppression of calphobindin I (CPB I) production in carcinoma of uterine cervix and endometrium.
Calphobindin I (CPB I) is a member of the family of Ca(2+)-dependent phospholipid binding proteins collectively termed as annexins. CPB I (Annexin V) has recently been shown to be an endogenous inhibitor of protein kinase C, a key enzyme in the cellular signal transduction and its inhibition by CPB I is presumed to be related ultimately to carcinogenesis. We therefore examined the level of production of CPB I in uterine cancer cells. Immunohistochemical analysis, northern blot, and in situ hybridization showed that the production of CPB I was markedly suppressed at the level of transcription in both cervical and endometrial carcinoma cells when compared to their normal counterparts. Decrease in production of CPB I may lead to dysregulated activation of protein kinase C and, accordingly, may be involved in a disorder of cell differentiation, proliferation, and carcinogenesis.
Karube
A
A
Department of Obstetrics and Gynecology, Akita University School of Medicine, Japan.
Shidara
Y
Y
Hayasaka
K
K
Maki
M
M
Tanaka
T
T
D017304:Annexin A5 / Q000037:antagonists & inhibitors* / Q000096:biosynthesis; D001483:Base Sequence; D015152:Blotting, Northern; D002277:Carcinoma / Q000378:metabolism*; D004717:Endometrium / Q000378:metabolism*; D005260:Female; D006801:Humans; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D015335:Molecular Probes / Q000235:genetics; D008969:Molecular Sequence Data; D012016:Reference Values; D002583:Uterine Cervical Neoplasms / Q000378:metabolism*
D017304:Annexin A5; D015335:Molecular Probes