Skeletal muscle force and actomyosin ATPase activity reduced by nitric oxide donor

William J. Perkins, Young Soo Han, Gary C Sieck

Research output: Contribution to journalArticle

102 Citations (Scopus)

Abstract

Nitric oxide (NO) may exert direct effects on actin-myosin cross-bridge cycling by modulating critical thiols on the myosin head. In the present study, the effects of the NO donor sodium nitroprusside (SNP; 100 μM to 10 mM) on mechanical properties and actomyosin adenosinetriphosphatase (ATPase) activity of single permeabilized muscle fibers from the rabbit psoas muscle were determined: The effects of N-ethylmaleimide (NEM; 5-250 μM), a thiol- specific alkylating reagent, on mechanical properties of single fibers were also evaluated. Both NEM (≤25 μM) and SNP ≤1 mM) significantly inhibited isometric force and actomyosin ATPase activity. The unloaded shortening velocity of SNP-treated single fibers was decreased but to a lesser extent, suggesting that SNP effects on isometric force and actomyosin ATPase were largely due to decreased cross-bridge recruitment. The calcium sensitivity of SNP-treated single fibers was also decreased. The effects of SNP, but not NEM, on force and actomyosin ATPase activity were reversed by treatment with 10 mM DL-dithiothreitol, a thiol-reducing agent. We conclude that the NO donor SNP inhibits contractile function caused by reversible oxidation of contractile protein thiols.

Original languageEnglish (US)
Pages (from-to)1326-1332
Number of pages7
JournalJournal of Applied Physiology
Volume83
Issue number4
StatePublished - Oct 1997

Fingerprint

Nitric Oxide Donors
Myosins
Single Nucleotide Polymorphism
Skeletal Muscle
Sulfhydryl Compounds
Psoas Muscles
Contractile Proteins
Ethylmaleimide
Dithiothreitol
Reducing Agents
Nitroprusside
Actins
Nitric Oxide
Rabbits
Calcium
Muscles

Keywords

  • Adenosinetriphosphatase
  • Dithiothreitol
  • Ethylmaleimide
  • Pharmacology
  • Rabbit psoas
  • Sodium nitroprusside
  • Sulfhydryl reagents

ASJC Scopus subject areas

  • Physiology
  • Endocrinology
  • Orthopedics and Sports Medicine
  • Physical Therapy, Sports Therapy and Rehabilitation

Cite this

Skeletal muscle force and actomyosin ATPase activity reduced by nitric oxide donor. / Perkins, William J.; Han, Young Soo; Sieck, Gary C.

In: Journal of Applied Physiology, Vol. 83, No. 4, 10.1997, p. 1326-1332.

Research output: Contribution to journalArticle

Perkins, WJ, Han, YS & Sieck, GC 1997, 'Skeletal muscle force and actomyosin ATPase activity reduced by nitric oxide donor', Journal of Applied Physiology, vol. 83, no. 4, pp. 1326-1332.
Perkins, William J. ; Han, Young Soo ; Sieck, Gary C. / Skeletal muscle force and actomyosin ATPase activity reduced by nitric oxide donor. In: Journal of Applied Physiology. 1997 ; Vol. 83, No. 4. pp. 1326-1332.
@article{59d5b8826876450fa679219aa80b45bd,
title = "Skeletal muscle force and actomyosin ATPase activity reduced by nitric oxide donor",
abstract = "Nitric oxide (NO) may exert direct effects on actin-myosin cross-bridge cycling by modulating critical thiols on the myosin head. In the present study, the effects of the NO donor sodium nitroprusside (SNP; 100 μM to 10 mM) on mechanical properties and actomyosin adenosinetriphosphatase (ATPase) activity of single permeabilized muscle fibers from the rabbit psoas muscle were determined: The effects of N-ethylmaleimide (NEM; 5-250 μM), a thiol- specific alkylating reagent, on mechanical properties of single fibers were also evaluated. Both NEM (≤25 μM) and SNP ≤1 mM) significantly inhibited isometric force and actomyosin ATPase activity. The unloaded shortening velocity of SNP-treated single fibers was decreased but to a lesser extent, suggesting that SNP effects on isometric force and actomyosin ATPase were largely due to decreased cross-bridge recruitment. The calcium sensitivity of SNP-treated single fibers was also decreased. The effects of SNP, but not NEM, on force and actomyosin ATPase activity were reversed by treatment with 10 mM DL-dithiothreitol, a thiol-reducing agent. We conclude that the NO donor SNP inhibits contractile function caused by reversible oxidation of contractile protein thiols.",
keywords = "Adenosinetriphosphatase, Dithiothreitol, Ethylmaleimide, Pharmacology, Rabbit psoas, Sodium nitroprusside, Sulfhydryl reagents",
author = "Perkins, {William J.} and Han, {Young Soo} and Sieck, {Gary C}",
year = "1997",
month = "10",
language = "English (US)",
volume = "83",
pages = "1326--1332",
journal = "Journal of Applied Physiology",
issn = "8750-7587",
publisher = "American Physiological Society",
number = "4",

}

TY - JOUR

T1 - Skeletal muscle force and actomyosin ATPase activity reduced by nitric oxide donor

AU - Perkins, William J.

AU - Han, Young Soo

AU - Sieck, Gary C

PY - 1997/10

Y1 - 1997/10

N2 - Nitric oxide (NO) may exert direct effects on actin-myosin cross-bridge cycling by modulating critical thiols on the myosin head. In the present study, the effects of the NO donor sodium nitroprusside (SNP; 100 μM to 10 mM) on mechanical properties and actomyosin adenosinetriphosphatase (ATPase) activity of single permeabilized muscle fibers from the rabbit psoas muscle were determined: The effects of N-ethylmaleimide (NEM; 5-250 μM), a thiol- specific alkylating reagent, on mechanical properties of single fibers were also evaluated. Both NEM (≤25 μM) and SNP ≤1 mM) significantly inhibited isometric force and actomyosin ATPase activity. The unloaded shortening velocity of SNP-treated single fibers was decreased but to a lesser extent, suggesting that SNP effects on isometric force and actomyosin ATPase were largely due to decreased cross-bridge recruitment. The calcium sensitivity of SNP-treated single fibers was also decreased. The effects of SNP, but not NEM, on force and actomyosin ATPase activity were reversed by treatment with 10 mM DL-dithiothreitol, a thiol-reducing agent. We conclude that the NO donor SNP inhibits contractile function caused by reversible oxidation of contractile protein thiols.

AB - Nitric oxide (NO) may exert direct effects on actin-myosin cross-bridge cycling by modulating critical thiols on the myosin head. In the present study, the effects of the NO donor sodium nitroprusside (SNP; 100 μM to 10 mM) on mechanical properties and actomyosin adenosinetriphosphatase (ATPase) activity of single permeabilized muscle fibers from the rabbit psoas muscle were determined: The effects of N-ethylmaleimide (NEM; 5-250 μM), a thiol- specific alkylating reagent, on mechanical properties of single fibers were also evaluated. Both NEM (≤25 μM) and SNP ≤1 mM) significantly inhibited isometric force and actomyosin ATPase activity. The unloaded shortening velocity of SNP-treated single fibers was decreased but to a lesser extent, suggesting that SNP effects on isometric force and actomyosin ATPase were largely due to decreased cross-bridge recruitment. The calcium sensitivity of SNP-treated single fibers was also decreased. The effects of SNP, but not NEM, on force and actomyosin ATPase activity were reversed by treatment with 10 mM DL-dithiothreitol, a thiol-reducing agent. We conclude that the NO donor SNP inhibits contractile function caused by reversible oxidation of contractile protein thiols.

KW - Adenosinetriphosphatase

KW - Dithiothreitol

KW - Ethylmaleimide

KW - Pharmacology

KW - Rabbit psoas

KW - Sodium nitroprusside

KW - Sulfhydryl reagents

UR - http://www.scopus.com/inward/record.url?scp=0030863027&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030863027&partnerID=8YFLogxK

M3 - Article

C2 - 9338443

AN - SCOPUS:0030863027

VL - 83

SP - 1326

EP - 1332

JO - Journal of Applied Physiology

JF - Journal of Applied Physiology

SN - 8750-7587

IS - 4

ER -