scholarly journals Fast Skeletal Muscle Isoforms Exhibit the Highest Incorporation Level into Myofibrils and Stress Fibers among Members of Myosin Alkali Light Chain Isoform Family.

2000 ◽  
Vol 25 (3) ◽  
pp. 141-148 ◽  
Author(s):  
Masatoshi Komiyama ◽  
Muhammad Mujahid Khan ◽  
Naoji Toyota ◽  
Yutaka Shimada
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Stress Fibers ◽  
Fast Skeletal Muscle ◽  
Muscle Isoforms

scholarly journals A comparison between mammalian and avian fast skeletal muscle alkali myosin light chain genes: regulatory implications

1985 ◽  
Vol 13 (13) ◽  
pp. 4623-4643 ◽  
Author(s):  
Philippe Daubas ◽  
Benoit Robert ◽  
Ian Garner ◽  
Margaret Buckingham
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Fast Skeletal Muscle

The expression of the regulatory myosin light chain 2 gene during mouse embryogenesis

Development ◽  
1993 ◽  
Vol 118 (3) ◽  
pp. 919-929 ◽  
Author(s):  
A. Faerman ◽  
M. Shani
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Fast Skeletal Muscle ◽  
Mouse Embryogenesis ◽  
Skeletal Muscle Myosin ◽  
Adult Mice ◽  
Regulatory Myosin Light Chain ◽  
Myosin Light Chain 2 ◽  
Muscle Groups

The fast skeletal muscle myosin light chain 2 (MLC2) gene is expressed specifically in skeletal muscles of newborn and adult mice, and has no detectable sequence homology with any of the other MLC genes including the slow cardiac MLC2 gene. The expression of the fast skeletal muscle MLC2 gene during early mouse embryogenesis was studied by in situ hybridization. Serial sections of embryos from 8.5 to 12.5 days post coitum (d.p.c.) were hybridized to MLC2 cRNA and to probes for the myogenic regulatory genes MyoD1 and myogenin. The results revealed different temporal and spatial patterns of hybridization for different muscle groups. MLC2 transcripts were first detected 9.5 d.p.c. in the myotomal regions of rostral somites, already expressing myogenin. Surprisingly, at the same stage, a weak MLC2 signal was also detected in the cardiomyocytes. The cardiac expression was transient and could not be detected at later stages while the myotomal signal persisted and spread to the more caudal somites, very similar to the expression of myogenin. Beginning from 10.5 d.p.c., several extramyotomal premuscle cells masses have been demarcated by MyoD1 expression. MLC2 transcripts were detected in only one of these cell masses. Although, transcripts of myogenin were detected in all these cell masses, the number of expressing cells was significantly lower than that observed for MyoD1. By 11.5 d.p.c., all three hybridization signals colocalized in most extramyotomal muscle-forming regions, with the exception of the diaphragm and the hindlimb buds, where only few cells expressed MLC2 and more cells expressed MyoD1 than myogenin. At 12.5 d.p.c., all three studied genes displayed a similar spatial pattern of expression in most muscle-forming regions. However, in some muscles, the MyoD1 signal spread over more cells compared to myogenin or MLC2. Our results are consistent with the suggestion that multiple myogenic programs exist for myoblasts differentiating in the myotome and extramyotomal regions.

Isolation and sequencing of porcine fast skeletal muscle alkali myosin light chain 3 cDNA

1997 ◽  
Vol 8 (2) ◽  
pp. 179-185 ◽  
Author(s):  
R. Davoli ◽  
L. Fontanesi ◽  
E. Costosi ◽  
P. Zambonelli ◽  
V. Russo
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Myosin Light Chain ◽  
Fast Skeletal Muscle

scholarly journals The effects of the interaction of myosin essential light chain isoforms with actin in skeletal muscles.

2002 ◽  
Vol 49 (3) ◽  
pp. 709-719 ◽  
Author(s):  
Hanna Nieznańska ◽  
Krzysztof Nieznański ◽  
Dariusz Stepkowski
Keyword(s):  
Skeletal Muscle ◽  
Atpase Activity ◽  
Light Chain ◽  
Light Chains ◽  
Ionic Character ◽  
Myofibrillar Atpase ◽  
Fast Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Essential Light Chain ◽  
Slow Skeletal Muscle

In order to compare the ability of different isoforms of myosin essential light chain to interact with actin, the effect of the latter protein on the proteolytic susceptibility of myosin light chains (MLC-1S and MLC-1V - slow specific and same as ventricular isoform) from slow skeletal muscle was examined. Actin protects both slow muscle essential light chain isoforms from papain digestion, similarly as observed for fast skeletal muscle myosin (Nieznanska et al., 1998, Biochim. Biophys. Acta 1383: 71). The effect of actin decreases as ionic strength rises above physiological values for both fast and slow skeletal myosin, confirming the ionic character of the actin-essential light chain interaction. To better understand the role of this interaction, we examined the effect of synthetic peptides spanning the 10-amino-acid N-terminal sequences of myosin light chain 1 from fast skeletal muscle (MLC-1F) (MLCFpep: KKDVKKPAAA), MLC-1S (MLCSpep: KKDVPVKKPA) and MLC-1V (MLCVpep: KPEPKKDDAK) on the myofibrillar ATPase of fast and slow skeletal muscle. In the presence of MLCFpep, we observed an about 19% increase, and in the presence of MLCSpep about 36% increase, in the myofibrillar ATPase activity of fast muscle. On the other hand, in myofibrillar preparations from slow skeletal muscle, MLCSpep as well as MLCVpep caused a lowering of the ATPase activity by about 36%. The above results suggest that MLCSpep induces opposite effects on ATPase activity, depending on the type of myofibrils, but not through its specific N-terminal sequence - which differs from other MLC N-terminal peptides. Our observations lead to the conclusion that the action of different isoforms of long essential light chain is similar in slow and fast skeletal muscle. However the interaction of essential light chains with actin leads to different physiological effects probably depending on the isoforms of other myofibrillar proteins.

Fast skeletal muscle regulatory light chain is required for fast and slow skeletal muscle development

2007 ◽  
Vol 21 (9) ◽  
pp. 2205-2214 ◽  
Author(s):  
Yingcai Wang ◽  
Danuta Szczesna-Cordary ◽  
Roger Craig ◽  
Zoraida Diaz-Perez ◽  
Georgianna Guzman ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Muscle Development ◽  
Regulatory Light Chain ◽  
Skeletal Muscle Development ◽  
Fast Skeletal Muscle ◽  
Slow Skeletal Muscle
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