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J Biol Chem, Vol. 274, Issue 42, 30115-30121, October 15, 1999

Mammal-specific, ERK-dependent, Caldesmon Phosphorylation in Smooth Muscle
QUANTITATION USING NOVEL ANTI-PHOSPHOPEPTIDE ANTIBODIES

Gerard D'Angelo, Philip Graceffa, C.-L. Albert Wang, John Wrangle, and Leonard P. Adam

From the  Boston Biomedical Research Institute and the  Harvard Medical School, Boston, Massachusetts 02114

Extracellular signal-regulated kinases (ERKs) phosphorylate the high molecular mass isoform of the actin-binding protein caldesmon (h-CaD) at two sites (Ser⁷⁵⁹ and Ser⁷⁸⁹) during smooth muscle stimulation. To investigate the role of phosphorylation at these sites, antibodies were generated against phosphopeptides analogous to the sequences around Ser⁷⁵⁹ and Ser⁷⁸⁹. Affinity-purified antibodies were phosho- and sequence-specific. The major site of phosphorylation in h-CaD in porcine carotid arterial muscle strips was at Ser⁷⁸⁹; however, the amount of phosphate did not vary appreciably with either KCl or phorbol ester stimulation. Phosphorylation at Ser⁷⁵⁹ of h-CaD was almost undetectable (<0.005 mol of phosphate/mol of protein). Moreover, phosphorylation of the low molecular mass isoform of the protein (l-CaD) at the site analogous to Ser⁷⁸⁹ was greater in serum-stimulated cultured smooth muscle cells than in serum-starved cells. Serum-stimulated l-CaD phosphorylation was attenuated by the protein kinase inhibitor PD98059. These data 1) identify Ser⁷⁸⁹ of h-CaD as the major site of ERK-dependent phosphorylation in carotid arteries; 2) show that the level of phosphorylation at Ser⁷⁸⁹ is relatively constant following carotid arterial muscle stimulation, despite an increase in total protein phosphate content; and 3) suggest a functional role for ERK-dependent l-CaD phosphorylation in cell division.

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