scholarly journals Expression of myosin light chains during fetal development of human skeletal muscle

1987 ◽  
Vol 243 (2) ◽  
pp. 425-430 ◽  
Author(s):  
F Pons ◽  
A Damadei ◽  
J J Leger
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Slow Light ◽  
Minor Component ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Fetal Life ◽  
Fetal Period ◽  
Adult Muscle ◽  
A Minor

The expression of myosin light chains (MLCs) during the development of human skeletal muscle was investigated by using two different two-dimensional electrophoretic techniques. In both electrophoretic systems the predominant light chain 1 (LC1) expressed during the whole fetal period was found to co-migrate with the adult fast LC1 (LC1F). The main LC2 expressed during the whole fetal period was found to be different from the main fast LC2 (LC2F) and slow LC2 (LC2S) usually present in adult muscle, but co-migrated with a minor component often present in adult muscle. This fetal LC2 was phosphorylatable, and the phosphorylated form co-migrated with the main component of LC2F expressed in the adult. The adult fast LC3 appeared as early as week 20 of gestation, whereas the adult slow light chains (LC1S and LC2S) appeared only during the late fetal period. A minor component of LC1, previously described in humans as an ‘embryonic LC’ (LCemb.) [Strohman, Micou-Eastwood, Glass & Matsuda (1983) Science 221, 955-957], was only expressed in the early fetal period and was found to co-migrate with atrial LC1 (ALC1). We discuss the expression of these specific developmental forms of MLCs co-existing with immature myosin heavy chains during fetal life.

scholarly journals Structure and function of fish fast skeletal muscle myosin light chains

2002 ◽  
Vol 68 (sup2) ◽  
pp. 1499-1502 ◽  
Author(s):  
SHOICHIRO ISHIZAKI ◽  
YASUYUKI MASUDA ◽  
MUNEHIKO TANAKA ◽  
SHUGO WATABE
Keyword(s):  
Skeletal Muscle ◽  
Structure And Function ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Fast Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
And Function ◽  
Muscle Myosin

Glucose transporter expression in human skeletal muscle fibers

2000 ◽  
Vol 279 (3) ◽  
pp. E529-E538 ◽  
Author(s):  
M. Gaster ◽  
A. Handberg ◽  
H. Beck-Nielsen ◽  
H. D. Schrøder
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Glucose Transporter ◽  
Muscle Fibers ◽  
Muscle Cells ◽  
Glut 1 ◽  
Adult Muscle ◽  
Glut 4 ◽  
Skeletal Muscle Fibers ◽  
Transporter Expression

The present study was initiated to investigate GLUT-1 through -5 expression in developing and mature human skeletal muscle. To bypass the problems inherent in techniques using tissue homogenates, we applied an immunocytochemical approach, employing the sensitive enhanced tyramide signal amplification (TSA) technique to detect the localization of glucose transporter expression in human skeletal muscle. We found expression of GLUT-1, GLUT-3, and GLUT-4 in developing human muscle fibers showing a distinct expression pattern. 1) GLUT-1 is expressed in human skeletal muscle cells during gestation, but its expression is markedly reduced around birth and is further reduced to undetectable levels within the first year of life; 2) GLUT-3 protein expression appears at 18 wk of gestation and disappears after birth; and 3) GLUT-4 protein is diffusely expressed in muscle cells throughout gestation, whereas after birth, the characteristic subcellular localization is as seen in adult muscle fibers. Our results show that GLUT-1, GLUT-3, and GLUT-4 seem to be of importance during muscle fiber growth and development. GLUT-5 protein was undetectable in fetal and adult skeletal muscle fibers. In adult muscle fibers, only GLUT-4 was expressed at significant levels. GLUT-1 immunoreactivity was below the detection limit in muscle fibers, indicating that this glucose transporter is of minor importance for muscle glucose supply. Thus we hypothesize that GLUT-4 also mediates basal glucose transport in muscle fibers, possibly through constant exposure to tonal contraction and basal insulin levels.

Skeletal muscle myosin light chains are essential for physiological speeds of shortening

Nature ◽  
1993 ◽  
Vol 365 (6445) ◽  
pp. 454-456 ◽  
Author(s):  
Susan Lowey ◽  
Guillermina S. Waller ◽  
Kathleen M. Trybus
Keyword(s):  
Skeletal Muscle ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Skeletal Muscle Myosin ◽  
Muscle Myosin

Immunocytochemical Localization of Myosin Light Chains in the Abdominal Superficial Flexor Muscles of the American Lobster, Homarus Americanus

1998 ◽  
Vol 4 (S2) ◽  
pp. 1118-1119
Author(s):  
Lisa D. Brown ◽  
Marie E. Cantino
Keyword(s):  
Skeletal Muscle ◽  
Molecular Weight ◽  
Spatial Distribution ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Homarus Americanus ◽  
Light Chains ◽  
Myosin Light Chains ◽  
Flexor Muscle ◽  
Electron Microscopic

Myosin is composed of two high-molecular weight heavy chains and four low-molecular weight hght chains. In both vertebrate and invertebrate skeletal muscle, each myosin heavy chain is associated with two myosin light chains. In skeletal muscle myosins studied by X-ray diffraction, each myosin heavy chain binds one of each of two distinct classes of hght chains. Thus, while isoform distributions may vary within and between fibers, the spatial distribution of each class of light chain should be uniform within the A band and between sarcomeres and fibers. Since no such study exists for crustacean myosin, we investigated the spatial distribution of the hght chains within the superficial flexor muscle (SFM) of the lobster, Homarus americanus, using immunoelectron microscopy. The SFM contains two classes of myosin hght chains, termed “alpha” (Mr = 21,000 to 23,500) and “beta” (Mr = 18,000 to 18,500). Immunocytochemical electron microscopic results suggest that the alpha light chains are not uniformly distributed at the subsarcomere level.

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