Direct activation of calcium-activated, phospholipid-dependent protein kinase by tumor-promoting phorbol esters

M. Castagna, Y. Takai, K. Kaibuchi, K. Sano, U. Kikkawa, Y. Nishizuka

研究成果: Article査読

3521 被引用数 (Scopus)

抄録

Tumor-promoting phorbol esters such as 12-O-tetradecanoylphorbol-13-acetate (TPA) directly activate in vitro Ca2+-activated, phospholipid-dependent protein kinase (protein kinase C), which normally requires unsaturated diacylglycerol. Kinetic analysis indicates that TPA can substitute for diacylglycerol and greatly increases the affinity of the enzyme for Ca2+ as well as for phospholipid. Under physiological conditions, the activation of this enzyme appears to be linked to the receptor-mediated phosphatidylinositol breakdown which may be provoked by a wide variety of extracellular messengers, eventually leading to the activation of specific cellular functions or proliferation. Using human platelets as a model system, TPA is shown to enhance the protein kinase C-specific phosphorylation associated with the release reaction in the total absence of phosphatidylinositol breakdown. Various phorbol derivatives which have been shown to be active in tumor promotion are also capable of activating this protein kinase in in vitro systems.

本文言語English
ページ(範囲)7847-7851
ページ数5
ジャーナルJournal of Biological Chemistry
257
13
出版ステータスPublished - 1982
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 分子生物学
  • 細胞生物学

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