The expression of myosin heavy chain isoforms in normal and hypertrophied chicken slow muscle

Hypertrophy was produced in the anterior latissimus dorsi (ALD) muscle of 5-wk-old chickens by application of a load to the humerus. After 4 wk, hypertrophied ALD muscles were >2.5 times heavier than contralateral control ALD muscles. Two isomyosins are distinguishable in normal ALD muscles by th...

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Bibliographic Details
Published in:The Journal of cell biology 1986-09, Vol.103 (3), p.977-983
Main Authors: Kennedy, J.M, Kamel, S, Tambone, W.W, Vrbova, G, Zak, R
Format: Article
Language:English
Subjects:
AILE
ALAS
Animals
Antibodies
Biological and medical sciences
CHICKENS
Cross Reactions
ELECTROFORESIS
ELECTROPHORESE
ELECTROPHORESIS
Fluorescent Antibody Technique
Fundamental and applied biological sciences. Psychology
Gels
GLOBULINAS
GLOBULINE
GLOBULINS
HYPERTROFIA
HYPERTROPHIE
HYPERTROPHY
Monoclonal antibodies
MUSCLE
Muscle fibers
MUSCLES
Muscles - metabolism
Muscles - pathology
MUSCULOS
Myosins - biosynthesis
Myosins - immunology
POLLO
POULET
Protein isoforms
Skeletal muscle
Stress, Mechanical
Striated muscle. Tendons
Vertebrates: osteoarticular system, musculoskeletal system
WINGS
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Description
Summary:Hypertrophy was produced in the anterior latissimus dorsi (ALD) muscle of 5-wk-old chickens by application of a load to the humerus. After 4 wk, hypertrophied ALD muscles were >2.5 times heavier than contralateral control ALD muscles. Two isomyosins are distinguishable in normal ALD muscles by their different electrophoretic mobilities. It is shown here that the faster migrating SM-1 isomyosin decreases in abundance with age and that the application of an overload enhances both the rate and extent of this process. Monoclonal antibodies were selected by an immunotransfer technique that were specific for the heavy chains associated with either SM-1 or SM-2, or cross-reacted with both isoforms. The cellular distribution of the SM-1 and SM-2 isomyosins was analyzed by immunofluorescent technique using these antibodies. Anti-SM-1 and anti-SM-2 antibodies reacted with separate populations of cells, whereas the third antibody reacted with all myocytes in the normal ALD muscle. These data suggest that there is an exclusive cellular distribution of myosin heavy chains associated with SM-1 and SM-2 proteins. Immunofluorescent analysis of hypertrophied muscle showed the anti-SM-2-specific antibody reacting with all myocytes, whereas the anti-SM-1-specific antibody reacted with none. This is consistent with the elimination of the SM-1 isoform in hypertrophied muscles.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.103.3.977