Nakajo S, Inagami T
Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee 37232.
Arch Biochem Biophys. 1993 Mar;301(2):320-4. doi: 10.1006/abbi.1993.1150.
The effect of atrial natriuretic factor (ANF) on the phosphorylation of the calmodulin-binding protein in vascular smooth muscle cells was investigated. Several phosphorylated calmodulin-binding proteins ranging in molecular weight from 205,000 to 50,000 were detected. Among them, we have found that the phosphorylation of a 52-kDa protein present mainly in the cytosolic fraction is stimulated by ANF and that the elevation of the phosphorylation is both time- and dose-dependent. Furthermore, the stimulation was mimicked by 8-bromo-cyclic GMP but not by 8-bromo-cyclic AMP. Endothelin induced significant inhibition of the phosphorylation. These results indicate that 52-kDa protein phosphorylation may be responsible for the regulation of vascular smooth muscle tone.
研究了心房利钠因子（ANF）对血管平滑肌细胞中钙调蛋白结合蛋白磷酸化的影响。检测到几种分子量在205,000至50,000之间的磷酸化钙调蛋白结合蛋白。其中，我们发现主要存在于胞质部分的一种52-kDa蛋白的磷酸化受到ANF的刺激，并且磷酸化的升高具有时间和剂量依赖性。此外，8-溴环鸟苷酸可模拟这种刺激，而8-溴环腺苷酸则不能。内皮素可显著抑制这种磷酸化。这些结果表明，52-kDa蛋白的磷酸化可能参与血管平滑肌张力的调节。
