Lactate dehydrogenase expression at the onset of altered loading in rat soleus muscle

Tyrone A. Washington, James M. Reecy, Raymond W. Thompson, Larry L. Lowe, Joseph M. McClung, James Carson

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Both functional overload and hindlimb disuse induce significant energy-dependent remodeling of skeletal muscle. Lactate dehydrogenase (LDH), an important enzyme involved in anaerobic glycolysis, catalyzes the interconversion of lactate and pyruvate critical for meeting rapid high-energy demands. The purpose of this study was to determine rat soleus LDH-A and -B isoform expression, mRNA abundance, and enzymatic activity at the onset of increased or decreased loading in the rat soleus muscle. The soleus muscles from male Sprague-Dawley rats were functionally overloaded for up to 3 days by a modified synergist ablation or subjected to disuse by hindlimb suspension for 3 days. LDH mRNA concentration was determined by Northern blotting, LDH protein isoenzyme composition was determined by zymogram analysis, and LDH enzymatic activity was determined spectrophotometrically. LDH-A mRNA abundance increased by 372%, and LDH-B mRNA abundance decreased by 43 and 31% after 24 h and 3 days of functional overload, respectively, compared with that in control rats. LDH protein expression demonstrated a shift by decreasing LDH-B isoforms and increasing LDH-A isoforms. LDH-B activity decreased 80% after 3 days of functional overload. Additionally, LDH-A activity increased by 234% following 3 days of hindlimb suspension. However, neither LDH-A or LDH-B mRNA abundance was affected following 3 days of hindlimb suspension. In summary, the onset of altered loading induced a differential expression of LDH-A and -B in the rat soleus muscle, favoring rapid energy production. Long-term altered loading is associated with myofiber conversion; however, the rapid changes in LDH at the onset of altered loading may be involved in other physiological processes.

Original languageEnglish (US)
Pages (from-to)1424-1430
Number of pages7
JournalJournal of Applied Physiology
Volume97
Issue number4
DOIs
StatePublished - Oct 1 2004
Externally publishedYes

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L-Lactate Dehydrogenase
Skeletal Muscle
Hindlimb Suspension
Messenger RNA
Protein Isoforms
Physiological Phenomena
RNA Isoforms
Glycolysis
Hindlimb
Pyruvic Acid
Northern Blotting
Isoenzymes
Sprague Dawley Rats
lactate dehydrogenase 1
lactate dehydrogenase 5
Lactic Acid
Proteins
Enzymes

All Science Journal Classification (ASJC) codes

  • Physiology
  • Physiology (medical)

Cite this

Lactate dehydrogenase expression at the onset of altered loading in rat soleus muscle. / Washington, Tyrone A.; Reecy, James M.; Thompson, Raymond W.; Lowe, Larry L.; McClung, Joseph M.; Carson, James.

In: Journal of Applied Physiology, Vol. 97, No. 4, 01.10.2004, p. 1424-1430.

Research output: Contribution to journalArticle

Washington, Tyrone A. ; Reecy, James M. ; Thompson, Raymond W. ; Lowe, Larry L. ; McClung, Joseph M. ; Carson, James. / Lactate dehydrogenase expression at the onset of altered loading in rat soleus muscle. In: Journal of Applied Physiology. 2004 ; Vol. 97, No. 4. pp. 1424-1430.
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abstract = "Both functional overload and hindlimb disuse induce significant energy-dependent remodeling of skeletal muscle. Lactate dehydrogenase (LDH), an important enzyme involved in anaerobic glycolysis, catalyzes the interconversion of lactate and pyruvate critical for meeting rapid high-energy demands. The purpose of this study was to determine rat soleus LDH-A and -B isoform expression, mRNA abundance, and enzymatic activity at the onset of increased or decreased loading in the rat soleus muscle. The soleus muscles from male Sprague-Dawley rats were functionally overloaded for up to 3 days by a modified synergist ablation or subjected to disuse by hindlimb suspension for 3 days. LDH mRNA concentration was determined by Northern blotting, LDH protein isoenzyme composition was determined by zymogram analysis, and LDH enzymatic activity was determined spectrophotometrically. LDH-A mRNA abundance increased by 372{\%}, and LDH-B mRNA abundance decreased by 43 and 31{\%} after 24 h and 3 days of functional overload, respectively, compared with that in control rats. LDH protein expression demonstrated a shift by decreasing LDH-B isoforms and increasing LDH-A isoforms. LDH-B activity decreased 80{\%} after 3 days of functional overload. Additionally, LDH-A activity increased by 234{\%} following 3 days of hindlimb suspension. However, neither LDH-A or LDH-B mRNA abundance was affected following 3 days of hindlimb suspension. In summary, the onset of altered loading induced a differential expression of LDH-A and -B in the rat soleus muscle, favoring rapid energy production. Long-term altered loading is associated with myofiber conversion; however, the rapid changes in LDH at the onset of altered loading may be involved in other physiological processes.",
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