Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle

Martin Flück, James Carson, Scott E. Gordon, Andrew Ziemiecki, Frank W. Booth

Research output: Contribution to journalArticle

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Abstract

Components of signaling pathways for mechanotransduction during load- induced enlargement of skeletal muscle have not been completely defined. We hypothesized that loading of skeletal muscle would result in an adaptive increase in the expression of two focal adhesion complex (FAC)-related proteins, focal adhesion kinase (FAK) and paxillin, as well as increased FAK activity. FAK protein was immunolocalized to the sarcolemmal region of rooster anterior latissimus dorsi (ALD) myofibers in the middle of the ALD muscle. FAK (77 and 81%) and paxillin (206 and 202%) protein concentrations per unit of total protein in Western blots increased significantly after 1.5 and 7 days, but not after 13 days, of stretch-induced hypertrophy-hyperplasia of the ALD muscle. FAK autokinase activity in immunoprecipitates was increased after 1.5, 7, and 13 days in stretched ALD muscles. To determine whether increased FAK and paxillin protein concentrations are associated with hypertrophy and/or new fiber formation, two additional experiments were performed. First, during formation of primary chicken myotubes (a model of new fiber formation), FAK protein concentration (63%), FAK activity (157%), and paxillin protein concentration (97%) increased compared with myoblasts. Second, FAK (112% and 611%) and paxillin (87% and 431%) protein concentrations per unit of total protein in the soleus muscle increased at 1 and 8 days after surgical ablation of the synergistic gastrocnemius muscle (a model of hypertrophy without hyperplasia). Thus increases in components of the FAC occur in hypertrophying muscle of animals and in newly formed muscle fibers in culture. Furthermore, increased FAK activity suggests a possible convergence of signaling at the FAC in load-induced growth of skeletal muscle.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Cell Physiology
Volume277
Issue number1 46-1
StatePublished - Aug 5 1999
Externally publishedYes

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Paxillin
Focal Adhesion Protein-Tyrosine Kinases
Focal Adhesions
Protein Kinases
Skeletal Muscle
Superficial Back Muscles
Proteins
Muscles
Hypertrophy
Hyperplasia
Focal Adhesion Kinase 2
Myoblasts
Skeletal Muscle Fibers
Chickens
Western Blotting

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cell Biology

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Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle. / Flück, Martin; Carson, James; Gordon, Scott E.; Ziemiecki, Andrew; Booth, Frank W.

In: American Journal of Physiology - Cell Physiology, Vol. 277, No. 1 46-1, 05.08.1999.

Research output: Contribution to journalArticle

Flück, Martin ; Carson, James ; Gordon, Scott E. ; Ziemiecki, Andrew ; Booth, Frank W. / Focal adhesion proteins FAK and paxillin increase in hypertrophied skeletal muscle. In: American Journal of Physiology - Cell Physiology. 1999 ; Vol. 277, No. 1 46-1.
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abstract = "Components of signaling pathways for mechanotransduction during load- induced enlargement of skeletal muscle have not been completely defined. We hypothesized that loading of skeletal muscle would result in an adaptive increase in the expression of two focal adhesion complex (FAC)-related proteins, focal adhesion kinase (FAK) and paxillin, as well as increased FAK activity. FAK protein was immunolocalized to the sarcolemmal region of rooster anterior latissimus dorsi (ALD) myofibers in the middle of the ALD muscle. FAK (77 and 81{\%}) and paxillin (206 and 202{\%}) protein concentrations per unit of total protein in Western blots increased significantly after 1.5 and 7 days, but not after 13 days, of stretch-induced hypertrophy-hyperplasia of the ALD muscle. FAK autokinase activity in immunoprecipitates was increased after 1.5, 7, and 13 days in stretched ALD muscles. To determine whether increased FAK and paxillin protein concentrations are associated with hypertrophy and/or new fiber formation, two additional experiments were performed. First, during formation of primary chicken myotubes (a model of new fiber formation), FAK protein concentration (63{\%}), FAK activity (157{\%}), and paxillin protein concentration (97{\%}) increased compared with myoblasts. Second, FAK (112{\%} and 611{\%}) and paxillin (87{\%} and 431{\%}) protein concentrations per unit of total protein in the soleus muscle increased at 1 and 8 days after surgical ablation of the synergistic gastrocnemius muscle (a model of hypertrophy without hyperplasia). Thus increases in components of the FAC occur in hypertrophying muscle of animals and in newly formed muscle fibers in culture. Furthermore, increased FAK activity suggests a possible convergence of signaling at the FAC in load-induced growth of skeletal muscle.",
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