Nishioka N, Hirai S, Mizuno K, Osada S, Suzuki A, Kosaka K, Ohno S
Department of Molecular Biology, School of Medicine, Yokohama City University, Japan.
FEBS Lett. 1995 Dec 27;377(3):393-8. doi: 10.1016/0014-5793(95)01382-2.
Treatment of rat 3Y1 fibroblasts with vasopressin (AVP) results in a transient activation of MAP kinase as potent as with EGF and serum. An antagonist of vasopressin receptor V1, but not an antagonist of V2, inhibited the AVP-induced activation of MAP kinases, indicating that AVP activates MAP kinases through V1 receptor. Prolonged TPA treatment of cells resulted in partial MAP kinase activation, indicating the presence of PKC-independent pathway. The pathway was inhibited by wortmannin, an inhibitor of PI3-kinase. The results suggest that wortmannin-sensitive molecules such as PI3-kinase, are involved in the V1 receptor-mediated activation of the MAP kinase pathway independent of TPA-sensitive PKC.
用加压素（AVP）处理大鼠3Y1成纤维细胞会导致丝裂原活化蛋白激酶（MAP激酶）短暂激活，其效力与表皮生长因子（EGF）和血清相当。血管加压素受体V1的拮抗剂而非V2的拮抗剂，抑制了AVP诱导的MAP激酶激活，这表明AVP通过V1受体激活MAP激酶。用佛波酯（TPA）长时间处理细胞会导致MAP激酶部分激活，表明存在不依赖蛋白激酶C（PKC）的途径。该途径被渥曼青霉素（一种PI3激酶抑制剂）抑制。结果表明，诸如PI3激酶等对渥曼青霉素敏感的分子，参与了V1受体介导的MAP激酶途径的激活，且不依赖于对TPA敏感的PKC。
