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J Biol Chem, Vol. 274, Issue 16, 11344-11351, April 16, 1999
From the Departments of c Surgery, a Medicine
(Institute for Molecular Medicine and Genetics), d Cell Biology
and Anatomy, and f Biochemistry and Molecular Biology, Medical
College of Georgia, Augusta, Georgia 30912, the b Augusta
Veterans Administration Medical Center, Augusta, Georgia 30912, the
g Department of Biochemistry, Institute for Developmental
Research, Human Service Center, Kasugai, Aichi 480-03, Japan, and the
h Department of Molecular Biology, Yokohama City University
School of Medicine, Yokohama 236, Japan
The small heat shock-related protein 20 (HSP20)
is present in four isoforms in bovine carotid artery smooth muscles.
Three of the isoforms are phosphorylated and one is not. Increases in the phosphorylation of two isoforms of HSP20 (isoform 3, pI 5.9; and 8, pI 5.7) are associated with cyclic nucleotide-dependent relaxation of bovine carotid artery smooth muscles. Increases in the
phosphorylation of another isoform (isoform 4, pI 6.0) are associated
with phorbol ester-induced contraction of bovine carotid artery smooth
muscles. In this investigation we determined that isoforms 3 and 8 are
phosphorylated on Ser16 of the HSP20 molecule during
activation of cAMP-dependent signaling pathways.
Phosphorylation state-specific antibodies produced against a peptide
containing phosphorylated Ser16 recognized isoforms 3 and 8 but not isoform 4. In human vascular tissue, only isoform 3 is present.
Incubation of transiently permeabilized strips of bovine carotid artery
smooth muscle with synthetic peptides in which Ser16 is
phosphorylated, inhibits contractile responses to high extracellular KCl and to serotonin. These data suggest that phosphorylation of HSP20
on Ser16 modulates cAMP-dependent vasorelaxation.
The Small Heat Shock-related Protein, HSP20, Is Phosphorylated on
Serine 16 during Cyclic Nucleotide-dependent
Relaxation
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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