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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2002.1
- 수록면
- 444 - 450 (7page)
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Phospholipase Cγ1 (PLCγ1) plays an important role in controlling cellular proliferation and differ-entiation. PLCγ1 is overexpressed in some tu-mors, and its overexpresion induces solid tumors nisms underlying PLCγ1-induced cell proliferation are not fuly understood. Here we show that over-expression of PLCγ1 highly phosphorylated glyco-gen synthase kinase-3β (GSK-3β) at serine-9 in 3Y1 fibroblasts. Inhibition of protein kinase C (PKC)s with GF109203X abrogated GSK-3β phosphoryla-tion by PLCγ1. We also found that steady-state level of cyclin D1 protein, but not cyclin D1 mRNA, was highly elevated in response to serum stimu-lation in PLCγvector-transfected cels. Since GSK-3β is involved in cyclin D1 proteolysis in response to mitogenic stimulation, PLCγ1-mediated GSK-3β phosphoryla-tion may function as a regulation of cyclin D1 accumulation in PLCγ1-overexpressing cels.
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