SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle

Gary C Sieck, W. Z. Zhan, Y.s. Prakash, M. J. Daood, J. F. Watchko

Research output: Contribution to journalArticle

93 Citations (Scopus)

Abstract

In the rat diaphragm muscle, the histochemical classification of type I, IIa, IIb, or IIx fibers was correlated with myosin heavy chain (MHC) immunoreactivity. Expression of MHC isoforms in single dissected fibers was also assessed electrophoretically. Most fibers (~86%) expressed a single MHC isoform, and when present, coexpression of MHC-2X and MHC-2B isoforms was most prevalent. Type I and IIa fibers were the smallest, type IIb fibers were the largest, and type IIx fibers were intermediate. Succinate dehydrogenase (SDH) and calcium-activated myosin adenosinetriphosphatase (actomyosin ATPase) activities were measured with quantitative histochemical procedures. Type I and IIa fibers had the highest SDH activities, followed in rank order by type IIx and IIb fibers. Type I fibers had the lowest actomyosin ATPase activity, followed in rank order by type IIa, IIx, and IIb fibers. Across all fibers, there was an inverse relationship between fiber SDH activity and cross-sectional area and a positive correlation between fiber actomyosin ATPase activity and cross-sectional area. The SDH and actomyosin ATPase activities of muscle fibers were also inversely correlated. These phenotypic differences in SDH and ATPase activities may be important in determining the contractile and fatigue properties of different fiber types in the rat diaphragm muscle.

Original languageEnglish (US)
Pages (from-to)1629-1639
Number of pages11
JournalJournal of Applied Physiology
Volume79
Issue number5
StatePublished - 1995

Fingerprint

Succinate Dehydrogenase
Myosin Heavy Chains
Myosins
Diaphragm
Muscles
Protein Isoforms
Fatigue
Adenosine Triphosphatases
Calcium

Keywords

  • adenosinetriphosphatase
  • histochemistry
  • immunohistochemistry
  • metabolic enzymes
  • morphometry
  • myosin heavy chain isoforms
  • succinate dehydrogenase

ASJC Scopus subject areas

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

Cite this

Sieck, G. C., Zhan, W. Z., Prakash, Y. S., Daood, M. J., & Watchko, J. F. (1995). SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle. Journal of Applied Physiology, 79(5), 1629-1639.

SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle. / Sieck, Gary C; Zhan, W. Z.; Prakash, Y.s.; Daood, M. J.; Watchko, J. F.

In: Journal of Applied Physiology, Vol. 79, No. 5, 1995, p. 1629-1639.

Research output: Contribution to journalArticle

Sieck, GC, Zhan, WZ, Prakash, YS, Daood, MJ & Watchko, JF 1995, 'SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle', Journal of Applied Physiology, vol. 79, no. 5, pp. 1629-1639.
Sieck, Gary C ; Zhan, W. Z. ; Prakash, Y.s. ; Daood, M. J. ; Watchko, J. F. / SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle. In: Journal of Applied Physiology. 1995 ; Vol. 79, No. 5. pp. 1629-1639.
@article{b10a9cebfcbe4094b493706dcdc56ffb,
title = "SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle",
abstract = "In the rat diaphragm muscle, the histochemical classification of type I, IIa, IIb, or IIx fibers was correlated with myosin heavy chain (MHC) immunoreactivity. Expression of MHC isoforms in single dissected fibers was also assessed electrophoretically. Most fibers (~86{\%}) expressed a single MHC isoform, and when present, coexpression of MHC-2X and MHC-2B isoforms was most prevalent. Type I and IIa fibers were the smallest, type IIb fibers were the largest, and type IIx fibers were intermediate. Succinate dehydrogenase (SDH) and calcium-activated myosin adenosinetriphosphatase (actomyosin ATPase) activities were measured with quantitative histochemical procedures. Type I and IIa fibers had the highest SDH activities, followed in rank order by type IIx and IIb fibers. Type I fibers had the lowest actomyosin ATPase activity, followed in rank order by type IIa, IIx, and IIb fibers. Across all fibers, there was an inverse relationship between fiber SDH activity and cross-sectional area and a positive correlation between fiber actomyosin ATPase activity and cross-sectional area. The SDH and actomyosin ATPase activities of muscle fibers were also inversely correlated. These phenotypic differences in SDH and ATPase activities may be important in determining the contractile and fatigue properties of different fiber types in the rat diaphragm muscle.",
keywords = "adenosinetriphosphatase, histochemistry, immunohistochemistry, metabolic enzymes, morphometry, myosin heavy chain isoforms, succinate dehydrogenase",
author = "Sieck, {Gary C} and Zhan, {W. Z.} and Y.s. Prakash and Daood, {M. J.} and Watchko, {J. F.}",
year = "1995",
language = "English (US)",
volume = "79",
pages = "1629--1639",
journal = "Journal of Applied Physiology",
issn = "8750-7587",
publisher = "American Physiological Society",
number = "5",

}

TY - JOUR

T1 - SDH and actomyosin ATPase activities of different fiber types in rat diaphragm muscle

AU - Sieck, Gary C

AU - Zhan, W. Z.

AU - Prakash, Y.s.

AU - Daood, M. J.

AU - Watchko, J. F.

PY - 1995

Y1 - 1995

N2 - In the rat diaphragm muscle, the histochemical classification of type I, IIa, IIb, or IIx fibers was correlated with myosin heavy chain (MHC) immunoreactivity. Expression of MHC isoforms in single dissected fibers was also assessed electrophoretically. Most fibers (~86%) expressed a single MHC isoform, and when present, coexpression of MHC-2X and MHC-2B isoforms was most prevalent. Type I and IIa fibers were the smallest, type IIb fibers were the largest, and type IIx fibers were intermediate. Succinate dehydrogenase (SDH) and calcium-activated myosin adenosinetriphosphatase (actomyosin ATPase) activities were measured with quantitative histochemical procedures. Type I and IIa fibers had the highest SDH activities, followed in rank order by type IIx and IIb fibers. Type I fibers had the lowest actomyosin ATPase activity, followed in rank order by type IIa, IIx, and IIb fibers. Across all fibers, there was an inverse relationship between fiber SDH activity and cross-sectional area and a positive correlation between fiber actomyosin ATPase activity and cross-sectional area. The SDH and actomyosin ATPase activities of muscle fibers were also inversely correlated. These phenotypic differences in SDH and ATPase activities may be important in determining the contractile and fatigue properties of different fiber types in the rat diaphragm muscle.

AB - In the rat diaphragm muscle, the histochemical classification of type I, IIa, IIb, or IIx fibers was correlated with myosin heavy chain (MHC) immunoreactivity. Expression of MHC isoforms in single dissected fibers was also assessed electrophoretically. Most fibers (~86%) expressed a single MHC isoform, and when present, coexpression of MHC-2X and MHC-2B isoforms was most prevalent. Type I and IIa fibers were the smallest, type IIb fibers were the largest, and type IIx fibers were intermediate. Succinate dehydrogenase (SDH) and calcium-activated myosin adenosinetriphosphatase (actomyosin ATPase) activities were measured with quantitative histochemical procedures. Type I and IIa fibers had the highest SDH activities, followed in rank order by type IIx and IIb fibers. Type I fibers had the lowest actomyosin ATPase activity, followed in rank order by type IIa, IIx, and IIb fibers. Across all fibers, there was an inverse relationship between fiber SDH activity and cross-sectional area and a positive correlation between fiber actomyosin ATPase activity and cross-sectional area. The SDH and actomyosin ATPase activities of muscle fibers were also inversely correlated. These phenotypic differences in SDH and ATPase activities may be important in determining the contractile and fatigue properties of different fiber types in the rat diaphragm muscle.

KW - adenosinetriphosphatase

KW - histochemistry

KW - immunohistochemistry

KW - metabolic enzymes

KW - morphometry

KW - myosin heavy chain isoforms

KW - succinate dehydrogenase

UR - http://www.scopus.com/inward/record.url?scp=0028871718&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028871718&partnerID=8YFLogxK

M3 - Article

C2 - 8594023

AN - SCOPUS:0028871718

VL - 79

SP - 1629

EP - 1639

JO - Journal of Applied Physiology

JF - Journal of Applied Physiology

SN - 8750-7587

IS - 5

ER -