Blumberg P M, König B, Sharkey N A, Leach K L, Jaken S, Jeng A Y
IARC Sci Publ. 1984(56):139-56.
Specific phorbol ester receptors are found in the particulate fraction of cells. In addition, cytosol contains a phorbol ester apo-receptor, which requires phospholipids for reconstitution. The apo-receptor corresponds to protein kinase C, and the quantitatively major membrane receptor appears to be a protein kinase C-phospholipid complex. The ability to reconstitute the phorbol ester apo-receptor into different lipid domains now makes it possible to begin elucidation of the role of the lipid domain in phorbol ester action. Studies reviewed here indicate that diglycerides competitively inhibit phorbol ester binding, consistent with their being the postulated endogenous phorbol ester analogues. Highly lipophilic phorbol esters inhibit effectively only if they are incorporated into the lipid phase, indicating that it is the membrane-dissolved form of the ligand which is recognized. The binding affinity of 3H-phorbol 12,13-dibutyrate for holo-receptor depends markedly (greater than 20-fold range) on the phospholipid environment, and heterogeneous phorbol ester binding (i.e., curved Scatchard plots) can be generated by use of heterogeneous lipid environments in the reconstitution. The possible existence of other phorbol ester receptors in addition to protein kinase C-phospholipid complexes remains to be resolved.
在细胞的微粒部分发现了特异性佛波酯受体。此外，胞质溶胶中含有佛波酯脱辅基受体，其重组需要磷脂。脱辅基受体对应于蛋白激酶C，并且在数量上占主要的膜受体似乎是蛋白激酶C-磷脂复合物。现在，将佛波酯脱辅基受体重组到不同脂质结构域的能力使得开始阐明脂质结构域在佛波酯作用中的作用成为可能。此处综述的研究表明，甘油二酯竞争性抑制佛波酯结合，这与其作为假定的内源性佛波酯类似物一致。高度亲脂性的佛波酯只有在掺入脂质相时才有效抑制，这表明被识别的是配体的膜溶解形式。3H-佛波醇12,13-二丁酸酯对全受体的结合亲和力明显（大于20倍范围）取决于磷脂环境，并且通过在重组中使用异质脂质环境可以产生异质佛波酯结合（即曲线形Scatchard图）。除了蛋白激酶C-磷脂复合物之外，其他佛波酯受体的可能存在仍有待解决。
