STIMULATION OF CA2+-DEPENDENT NEUROTRANSMITTER RELEASE AND PRESYNAPTIC NERVE-TERMINAL PROTEIN-PHOSPHORYLATION BY CALMODULIN AND A CALMODULIN-LIKE PROTEIN ISOLATED FROM SYNAPTIC VESICLES
STIMULATION OF CA2+-DEPENDENT NEUROTRANSMITTER RELEASE AND PRESYNAPTIC NERVE-TERMINAL PROTEIN-PHOSPHORYLATION BY CALMODULIN AND A CALMODULIN-LIKE PROTEIN ISOLATED FROM SYNAPTIC VESICLES
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DOI:
10.1073/pnas.76.4.1838
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发表时间:
1979-01-01
影响因子:
11.1
通讯作者:
MAURER, SC
中科院分区:
文献类型:
--
作者:
DELORENZO, RJ;FREEDMAN, SD;MAURER, SC
Synaptic vesicles have a Ca2+-dependent protein kinase system that may play a role in mediating Ca2+-stimulated neurotransmitter release and vesicle function. The ability of Ca2+ to initiate norepinephrine release and protein phosphorylation in synaptic vesicle preparations was stimulated by the presence of an endogenous heat-stable vesicle protein fraction. The heat stability and characteristics of this endogenous vesicle fraction were similar to those of calmodulin (Ca2+-dependent regular protein) isolated from rat and bovine brain. Calmodulin, like endogenous heat-stable vesicle factor, restored the ability to stimulate vesicle neurotransmitter release and protein kinase activity. Calmodulin-like vesicle protein and purified calmodulin were equally effective in stimulating cyclic nucleotide-dependent phosphodiesterase, further indicating that these 2 proteins are functionally equivalent. Depolarization-dependent Ca2+ uptake in intact synaptosomes simultaneously stimulated release of neurotransmitter and phosphorylationof particular synaptic vesicle proteins that were shown in the isolated vesicle preparation to be dependent on Ca2+ and calmodulin. The effects of Ca on neurotransmitter release and presynaptic nerve terminal protein phosphorylation may be mediated by endogenous calmodulin-like proteins.