Sugiya H, Putney J W
Calcium Regulation Section, National Institute of Environmental Health Sciences, Research Triangle Park, NC 27709.
Biochem J. 1988 Dec 1;256(2):677-80. doi: 10.1042/bj2560677.
Substance P-induced inositol trisphosphate (InsP3) formation was inhibited by 1 microM-4 beta-phorbol 12,13-dibutyrate (PDBu) in rat parotid acinar cells. The inhibitory effect of PDBu was reversed by the protein kinase C inhibitors H-7 or K252a. Substance P also elicits a persistent desensitization of subsequent substance P-stimulated InsP3 formation. However, this desensitization was not inhibited by H-7. In addition, H-7 had no effect on the time course of substance P-induced InsP3 formation. These results suggest that, although activation of protein kinase C by phorbol esters can inhibit the substance P receptor-linked phospholipase C pathway, this mechanism apparently plays little, if any, role in regulating this system after activation by substance P.
在大鼠腮腺腺泡细胞中，1微摩尔4β-佛波醇12,13-二丁酸酯（PDBu）可抑制P物质诱导的肌醇三磷酸（InsP3）生成。蛋白激酶C抑制剂H-7或K252a可逆转PDBu的抑制作用。P物质还会引发对后续P物质刺激的InsP3生成的持续性脱敏。然而，H-7并不能抑制这种脱敏。此外，H-7对P物质诱导的InsP3生成的时间进程没有影响。这些结果表明，尽管佛波酯激活蛋白激酶C可抑制P物质受体相关的磷脂酶C途径，但在P物质激活该系统后，这一机制在调节该系统中似乎作用甚微（如果有作用的话）。
