Mn2+ activates skinned smooth muscle cells in the absence of myosin light chain phosphorylation

Phyllis E. Hoar, W. Glenn L. Kerrick

Research output: Contribution to journalArticle

16 Scopus citations

Abstract

Two effects of Mn2+ on skinned fibers from chicken gizzard smooth muscle were observed, dependent on the presence of absence of dithiothreitol (DTT) reducing agent. One involves protein oxidation (in the absence of DTT) with production of a "latch"-like state, and the other involves direct Mn2+ activation of contractile proteins. Cells activated by Mn2+ in the presence of ATP and the absence of Ca2+, Mg2+ and DTT did not relax when transferred to normal relaxing solutions. In contrast, when 5 mM DTT was included in the Mn2+ contracting solution to prevent protein oxidation by Mn2+, the cells still contracted when exposed to Mn2+, but relaxed rapidly when the Mn2+ was removed. In the presence of DTT both the Mn2+ activation and the relaxation following removal of Mn2+ were more rapid than normal Ca2+-activated contractions and relaxations. The skinned fibers activated by Mn2+ in the absence of DTT showed little active shortening unless DTT was added. This rigor-like state is probably due to oxidation of contractile proteins since the cells relaxed when exposed to a relaxing solution containing DTT (50mM) and then contracted again in response to Ca2+ and relaxed normally. The Mn2+ activation was not associated with myosin light chain phosphorylation, in contrast to Ca2+-activated contractions.

Original languageEnglish (US)
Pages (from-to)225-230
Number of pages6
JournalPflügers Archiv European Journal of Physiology
Volume412
Issue number3
DOIs
StatePublished - Aug 1 1988

    Fingerprint

Keywords

  • Mn
  • Oxidation
  • Skinned smooth muscle

ASJC Scopus subject areas

  • Physiology

Cite this