Tyrosine phosphorylation and regulation of swine carotid artery contraction.
Tyrosine phosphorylation and regulation of swine carotid artery contraction.
复制标题
酪氨酸磷酸化和猪颈动脉收缩的调节。
DOI：
10.1159/000159196
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发表时间：
1997
影响因子：
1.7
通讯作者：
Weaver,BA
中科院分区：
文献类型：
--
作者：
Rembold,CM;Weaver,BA
平滑肌中肌球蛋白磷酸化的[Ca 2 +] i的调节和[Ca 2 +]敏感性的调节可能涉及酪氨酸残基上的一种或多种蛋白质的磷酸化。我们通过测量从猪颈动脉提取并通过SDS凝胶电泳分离的蛋白质的酪氨酸磷酸化来验证这一假设。酪氨酸磷酸化估计的结合antiphosphotyrosine抗体的蛋白质在SDS凝胶。我们发现四个条带的分子量约为120，110，85和75 kD，其中酪氨酸磷酸化增加组胺刺激后1分钟。组胺洗脱后，这四个条带中的蛋白质的去磷酸化以比松弛慢的速率发生。这四条蛋白带的酪氨酸磷酸化与激动剂或高[K+]刺激后肌球蛋白磷酸化的[Ca 2 +]i敏感性无关。佛波醇二丁酸酯刺激也诱导这四个蛋白条带的酪氨酸磷酸化。这些数据表明，酪氨酸磷酸化的蛋白质在这四个带可能参与了猪颈动脉收缩的初始阶段。然而，有，在最多的，只有一个轻微的参与酪氨酸磷酸化的这四个蛋白带在持续阶段的收缩或在调节肌球蛋白磷酸化的[Ca 2 +]i的敏感性在猪颈动脉。这些数据并不排除其他丰度较低的酪氨酸磷蛋白在调节持续收缩或肌球蛋白磷酸化的[Ca 2 +]i敏感性中的作用。
Regulation of [Ca2+]iand modulation of the [Ca2+]isensitivity of myosin phosphorylation in smooth muscles may involve phosphorylation of one or more proteins on tyrosine residues. We tested this hypothesis by measuring tyrosine phosphorylation of proteins extracted from swine carotid artery and separated by SDS gel electrophoresis. Tyrosine phosphorylation was estimated by the binding of antiphosphotyrosine antibodies to proteins in SDS gels. We found four bands with approximate molecular weights of 120, 110, 85 and 75 kD in which tyrosine phosphorylation increased 1 min after histamine stimulation. After washout of histamine, dephosphorylation of the proteins in these four bands occurred at a slower rate than relaxation. Tyrosine phosphorylation of these four protein bands did not correlate with the [Ca2+]i sensitivity of myosin phosphorylation following agonist or high [K+]ostimulation. Phorbol dibutyrate stimulation also induced tyrosine phosphorylation of these four protein bands. These data suggest that tyrosine phosphorylation of the proteins in these four bands may be involved in the initial phase of swine carotid artery contraction. However, there was, at most, only a minor involvement of tyrosine phosphorylation of these four protein bands in the sustained phase of contraction or in the regulation of [Ca2+]i sensitivity of myosin phosphorylation in the swine carotid artery. These data do not rule out a role for other, less abundant tyrosine phosphoproteins in the regulation of sustained contraction or the [Ca2+]i sensitivity of myosin phosphorylation.