Phosphorylation of the small heat shock-related protein, HSP20, in vascular smooth muscles is associated with changes in the macromolecular associations of HSP20

Colleen M. Brophy, Mary Dickinson, David A Woodrum

Research output: Contribution to journalArticle

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Abstract

Cyclic nucleotide-dependent vasorelaxation is associated with increases in the phosphorylation of a small heat shock-related protein, HSP20. We hypothesized that phosphorylation of HSP20 in vascular smooth muscles is associated with alterations in the macromolecular associations of HSP20. Treatment of bovine carotid artery smooth muscles with the phosphodiesterase inhibitor, 3-isobutyl-1-methylxanthine, and the adenylate cyclase activator, forskolin, led to increases in the phosphorylation of HSP20 and dissociation of macromolecular aggregates of HSP20. However, 3-isobutyl-1-methylxanthine and forskolin treatment of a muscle that is uniquely refractory to cyclic nucleotide-dependent vasorelaxation, human umbilical artery smooth muscle, did not result in increases in the phosphorylation of HSP20 or to dissociation of macromolecular aggregates. HSP20 can be phosphorylated in vitro by the catalytic subunit of cAMP-dependent protein kinase (PKA) in both carotid and umbilical arteries and this phosphorylation of HSP20 is associated with dissociation of macromolecular aggregates of HSP20. Activation of cyclic nucleotide-dependent signaling pathways does not lead to changes in the macromolecular associations of another small heat shock protein, HSP27. Interestingly, the myosin light chains (MLC20) are in similar fractions as the HSP20, and phosphorylation of HSP20 is associated with changes in the macromolecular associations of MLC20. These data suggest that increases in the phosphorylation of HSP20 are associated with changes in the macromolecular associations of HSP20. HSP20 may regulate vasorelaxation through a direct interaction with specific contractile regulatory proteins.

Original languageEnglish (US)
Pages (from-to)6324-6329
Number of pages6
JournalJournal of Biological Chemistry
Volume274
Issue number10
DOIs
StatePublished - Mar 5 1999
Externally publishedYes

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Small Heat-Shock Proteins
Phosphorylation
Vascular Smooth Muscle
Muscle
Cyclic Nucleotides
Vasodilation
Proteins
1-Methyl-3-isobutylxanthine
Umbilical Arteries
Colforsin
Carotid Arteries
Smooth Muscle
Contractile Proteins
Myosin Light Chains
Phosphodiesterase Inhibitors
Cyclic AMP-Dependent Protein Kinases
Hot Temperature
Adenylyl Cyclases
Refractory materials
Catalytic Domain

ASJC Scopus subject areas

  • Biochemistry

Cite this

Phosphorylation of the small heat shock-related protein, HSP20, in vascular smooth muscles is associated with changes in the macromolecular associations of HSP20. / Brophy, Colleen M.; Dickinson, Mary; Woodrum, David A.

In: Journal of Biological Chemistry, Vol. 274, No. 10, 05.03.1999, p. 6324-6329.

Research output: Contribution to journalArticle

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