P物质及其片段对大鼠大脑皮层突触体膜蛋白（突触素）内源性磷酸化的影响。

The influence of substance P and its fragments on endogenous phosphorylation of synaptosomal membrane protein (synapsin) from cerebral cortex of rat brain.

Hrabec Z, Szkudlarek J, Lachowicz L

II Department of Biochemistry, School of Medicine, Lodz, Poland.

Comp Biochem Physiol C Comp Pharmacol Toxicol. 1990;96(1):59-63. doi: 10.1016/0742-8413(90)90044-a.

Abstract

The effects of substance P and its fragments and analogue of a C-terminal fragment on cyclic AMP-dependent phosphorylation of synapsin I in synaptosomal membranes (SM) from cerebral cortex were investigated. 2. SP(I-II) and SP(1-4) at 10(-3) M caused a marked stimulation of synapsin I phosphorylation. 3. A C-terminal fragment of SP (SP6-11) had no effect on phosphorylation of synapsin 1. 4. Analogue of C-terminal fragment [(Tyr8)SP6-11] at 10(-3) M distinctly inhibits phosphorylation of synapsin I. 5. These data suggest that SPI-II and its C- and N-terminal fragments have a modulator function against the phosphorylation of some rat brain proteins.

摘要

研究了P物质及其片段和C末端片段类似物对大脑皮质突触体膜（SM）中突触素I的环磷酸腺苷依赖性磷酸化的影响。2. 10⁻³ M的SP（I-II）和SP（1-4）显著刺激了突触素I的磷酸化。3. SP的C末端片段（SP6-11）对突触素1的磷酸化没有影响。4. 10⁻³ M的C末端片段类似物[（Tyr8）SP6-11]明显抑制突触素I的磷酸化。5. 这些数据表明，SPI-II及其C末端和N末端片段对某些大鼠脑蛋白的磷酸化具有调节功能。