Cardiac and skeletal muscle expression of mutant β-myosin heavy chains, degree of functional impairment and phenotypic heterogeneity in hypertrophic cardiomyopathy

2012 ◽  
Vol 227 (10) ◽  
pp. 3471-3476 ◽  
Author(s):  
Marina Di Domenico ◽  
Rita Casadonte ◽  
Pietroantonio Ricci ◽  
Mario Santini ◽  
Giacomo Frati ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Hypertrophic Cardiomyopathy ◽  
Functional Impairment ◽  
Phenotypic Heterogeneity ◽  
Myosin Heavy Chains ◽  
Heavy Chains

Three Slow Myosin Heavy Chains Sequentially Expressed in Developing Mammalian Skeletal Muscle

1993 ◽  
Vol 158 (1) ◽  
pp. 183-199 ◽  
Author(s):  
Simon M. Hughes ◽  
Mildred Cho ◽  
Ilene Karsch-Mizrachi ◽  
Marilyn Travis ◽  
Laura Silberstein ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Mammalian Skeletal Muscle ◽  
Myosin Heavy Chains ◽  
Slow Myosin ◽  
Heavy Chains

scholarly journals Neonatal and adult myosin heavy chains form homodimers during avian skeletal muscle development.

1991 ◽  
Vol 113 (2) ◽  
pp. 303-310 ◽  
Author(s):  
S Lowey ◽  
G S Waller ◽  
E Bandman
Keyword(s):  
Skeletal Muscle ◽  
Muscle Development ◽  
Coiled Coil ◽  
Myosin Isoforms ◽  
Myosin Heavy Chains ◽  
Electron Microscopic ◽  
Hybrid Species ◽  
Heavy Chains ◽  
Stage Of Development ◽  
Microscopic Techniques

Myosin isoforms contribute to the heterogeneity and adaptability of skeletal muscle fibers. Besides the well-characterized slow and fast muscle myosins, there are those isoforms that appear transiently during the course of muscle development. At a stage of development when two different myosins are coexpressed, the possibility arises for the existence of heterodimers, molecules containing two different heavy chains, or homodimers, molecules with two identical heavy chains. The question of whether neonatal and adult myosin isoforms can associate to form a stable heterodimer was addressed by using stage-specific monoclonal antibodies in conjunction with immunological and electron microscopic techniques. We find that independent of the ratio of adult to neonatal myosin, depending on the age of the animal, the myosin heavy chains form predominantly homodimeric molecules. The small amount of hybrid species present suggests that either the rod portion of the two heavy chain isoforms differs too much in sequence to form a stable alpha-helical coiled coil, or that the biosynthesis of the heavy chains precludes the formation of heterodimeric molecules.

scholarly journals Incorporation of myosin heavy chains into the A‐bands of living skeletal muscle cells

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Joseph W Sanger ◽  
Jushuo Wang ◽  
Yingli Fan ◽  
Balraj Mittal ◽  
Jean M Sanger
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Myosin Heavy Chains ◽  
Heavy Chains

Effect of Hypophysectomy and Growth Hormone Administration on Myosin Heavy Chains in Rat Skeletal Muscle

2004 ◽  
Vol 36 (Supplement) ◽  
pp. S302
Author(s):  
Daniel A. Judelson ◽  
William J. Kraemer ◽  
Nicholas A. Demonaco ◽  
Barry A. Spiering ◽  
Ricardo Silvestre ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Growth Hormone ◽  
Myosin Heavy Chains ◽  
Rat Skeletal Muscle ◽  
Growth Hormone Administration ◽  
Heavy Chains ◽  
Hormone Administration

scholarly journals Role of myosin heavy chains from rabbit skeletal muscle in the heat-induced gelation mechanism.

1984 ◽  
Vol 48 (9) ◽  
pp. 2225-2232 ◽  
Author(s):  
Kunihiko SAMEJIMA ◽  
Hiroshi YAMAUCHI ◽  
Ali ASGHAR ◽  
Tsutomu YASUI
Keyword(s):  
Skeletal Muscle ◽  
Rabbit Skeletal Muscle ◽  
Myosin Heavy Chains ◽  
Gelation Mechanism ◽  
Heavy Chains

scholarly journals Myosin content of individual human muscle fibers isolated by laser capture microdissection

2016 ◽  
Vol 310 (5) ◽  
pp. C381-C389 ◽  
Author(s):  
Charles A. Stuart ◽  
William L. Stone ◽  
Mary E. A. Howell ◽  
Marianne F. Brannon ◽  
H. Kenton Hall ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Type I ◽  
Fiber Types ◽  
Myosin Heavy Chains ◽  
Heavy Chains ◽  
Slow Twitch ◽  
Type I Fibers ◽  
Fast Twitch ◽  
Laser Capture

Muscle fiber composition correlates with insulin resistance, and exercise training can increase slow-twitch (type I) fibers and, thereby, mitigate diabetes risk. Human skeletal muscle is made up of three distinct fiber types, but muscle contains many more isoforms of myosin heavy and light chains, which are coded by 15 and 11 different genes, respectively. Laser capture microdissection techniques allow assessment of mRNA and protein content in individual fibers. We found that specific human fiber types contain different mixtures of myosin heavy and light chains. Fast-twitch (type IIx) fibers consistently contained myosin heavy chains 1, 2, and 4 and myosin light chain 1. Type I fibers always contained myosin heavy chains 6 and 7 (MYH6 and MYH7) and myosin light chain 3 (MYL3), whereas MYH6, MYH7, and MYL3 were nearly absent from type IIx fibers. In contrast to cardiomyocytes, where MYH6 (also known as α-myosin heavy chain) is seen solely in fast-twitch cells, only slow-twitch fibers of skeletal muscle contained MYH6. Classical fast myosin heavy chains (MHC1, MHC2, and MHC4) were present in variable proportions in all fiber types, but significant MYH6 and MYH7 expression indicated slow-twitch phenotype, and the absence of these two isoforms determined a fast-twitch phenotype. The mixed myosin heavy and light chain content of type IIa fibers was consistent with its role as a transition between fast and slow phenotypes. These new observations suggest that the presence or absence of MYH6 and MYH7 proteins dictates the slow- or fast-twitch phenotype in skeletal muscle.

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