Mammal-specific, ERK-dependent, caldesmon phosphorylation in smooth muscle - Quantitation using novel anti-phosphopeptide antibodies
Mammal-specific, ERK-dependent, caldesmon phosphorylation in smooth muscle - Quantitation using novel anti-phosphopeptide antibodies
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DOI：
10.1074/jbc.274.42.30115
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发表时间：
1999-10-15
影响因子：
4.8
通讯作者：
Adam, LP
中科院分区：
文献类型：
--
作者：
D'Angelo, G;Graceffa, P;Adam, LP
在平滑肌刺激过程中，细胞外信号调节激酶 (ERK) 在两个位点（Ser(759) 和 Ser(789)）磷酸化肌动蛋白结合蛋白 caldesmon (h-CaD) 的高分子同工型。为了研究这些位点磷酸化的作用，针对类似于 Ser(759) 和 Ser(789) 周围序列的磷酸肽生成了抗体。亲和纯化的抗体具有磷酸化和序列特异性。猪颈动脉肌条中h-CaD的主要磷酸化位点为Ser(789)；然而，磷酸盐的量在 KCl 或佛波酯刺激下没有明显变化。 h-CaD Ser(759) 处的磷酸化几乎检测不到（
Extracellular signal-regulated kinases (ERKs) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-CaD) at two sites (Ser(759) and Ser(789)) during smooth muscle stimulation. To investigate the role of phosphorylation at these sites, antibodies were generated against phosphopeptides analogous to the sequences around Ser(759) and Ser(789). Affinity-purified antibodies were phosho- and sequence-specific. The major site of phosphorylation in h-CaD in porcine carotid arterial muscle strips was at Ser(789); however, the amount of phosphate did not vary appreciably with either KCl or phorbol ester stimulation. Phosphorylation at Ser(759) of h-CaD was almost undetectable (