生长激素释放因子和血管活性肠肽对钙调蛋白依赖性肌球蛋白轻链激酶的抑制作用。
Inhibition of calmodulin-dependent myosin light-chain kinase by growth-hormone-releasing factor and vasoactive intestinal peptide.
作者信息
Shiraga H, Stallwood D, Ebadi M, Pfeiffer R, Landers D, Paul S
机构信息
Department of Anesthesiology, University of Nebraska Medical Center, Omaha 68198-6830.
出版信息
Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):901-5. doi: 10.1042/bj3000901.
In view of the ability of calmodulin to bind vasoactive intestinal peptide (VIP) and growth-hormone-releasing factor (GRF) with high affinity [Stallwood, Brugger, Baggenstoss, Stemmer, Shiraga, Landers and Paul (1992) J. Biol. Chem. 267, 19617-19621], the effects of these neuropeptides on a model calmodulin-dependent enzyme, myosin light-chain kinase (MLCK), were studied. Both peptides were potent inhibitors of MLCK activity. The inhibition of enzyme activity by VIP and GRF was progressively overcome with increasing calmodulin concentrations, with no inhibition observed at a saturating calmodulin concentration. Nanomolar concentrations of MLCK blocked the formation of calmodulin-[125I-Tyr10]VIP complexes. These data provide support for a functional role of VIP and GRF binding by calmodulin.
鉴于钙调蛋白能够以高亲和力结合血管活性肠肽（VIP）和生长激素释放因子（GRF）[斯托尔伍德、布鲁格、巴根斯托斯、施泰默、志贺、兰德斯和保罗（1992年）《生物化学杂志》267卷，19617 - 19621页]，研究了这些神经肽对一种典型的钙调蛋白依赖性酶——肌球蛋白轻链激酶（MLCK）的影响。两种肽都是MLCK活性的有效抑制剂。随着钙调蛋白浓度的增加，VIP和GRF对酶活性的抑制作用逐渐被克服，在钙调蛋白浓度饱和时未观察到抑制作用。纳摩尔浓度的MLCK可阻断钙调蛋白 - [125I - 酪氨酸10]VIP复合物的形成。这些数据为钙调蛋白结合VIP和GRF的功能作用提供了支持。
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