Yamaguchi T, Winsky L, Jacobowitz D M
Laboratory of Clinical Science, NIMH, Bethesda, MD 20892.
Neurosci Lett. 1991 Sep 30;131(1):79-82. doi: 10.1016/0304-3940(91)90341-p.
The neuronal calcium binding protein calretinin was studied for possible effects on brain protein phosphorylation. Calretinin (100 nM) inhibited the appearance of a calcium stimulated 39 kDa phosphoprotein within a synaptic membrane fraction following sucrose density centrifugation. Calmodulin or a specific protein kinase C inhibitor had no effect on either the phosphorylation of the 39 kDa protein or the inhibition produced by calretinin. At the same concentration, calretinin produced a slight increase in the phosphorylation of several other synaptic membrane proteins which appeared additive with the stimulation produced by either calmodulin or phosphatidylserine in the presence of calcium.
对神经元钙结合蛋白钙视网膜蛋白进行了研究，以探讨其对脑蛋白磷酸化可能产生的影响。钙视网膜蛋白（100 nM）抑制了蔗糖密度离心后突触膜组分中钙刺激的39 kDa磷蛋白的出现。钙调蛋白或特异性蛋白激酶C抑制剂对39 kDa蛋白的磷酸化或钙视网膜蛋白产生的抑制均无影响。在相同浓度下，钙视网膜蛋白使其他几种突触膜蛋白的磷酸化略有增加，这与钙调蛋白或磷脂酰丝氨酸在钙存在下产生的刺激呈累加效应。
