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

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.

scholarly journals The intracompartmental sorting of myosin alkali light chain isoproteins reflects the sequence of developmental expression as determined by double epitope-tagging competition

1996 ◽  
Vol 109 (8) ◽  
pp. 2089-2099 ◽  
Author(s):  
M. Komiyama ◽  
T. Soldati ◽  
P. von Arx ◽  
J.C. Perriard
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Neonatal Rat ◽  
Developmental Expression ◽  
Fast Skeletal Muscle ◽  
Competition Assay ◽  
Epitope Tagging ◽  
Slow Skeletal Muscle ◽  
Vesicular Stomatitis ◽  
Cultured Cardiomyocytes

In order to compare within the same cell the various degrees of specificity of myosin alkali light chain (MLC) isoproteins sorting to sarcomeres, a competition assay was established using double epitope tagging. Various combinations of two different MLC isoform cDNAs tagged with either a vesicular stomatitis virus VSV-G (VSV) or a medium T (mT) protein epitope were co-expressed in cultured cardiomyocytes from adult and neonatal rat ventricles. Expressed isoproteins were detected by means of anti-VSV and anti-mT antibodies and their sorting patterns were analyzed by confocal microscopy. The sorting specificity of MLC isoforms to sarcomeric sites was shown to increase in the order MLC3nm, to ML1sa, to MLC1sb, to MLC1f and MLC3f following the sequence of developmental expression. Expressed fast skeletal muscle isoforms (MLC1f and MLC3f) were always localized at the A-bands of myofibrils, while nonmuscle type (MLC3nm) was distributed throughout the cytoplasm. The slow skeletal muscle type (MLC1sa) showed a weak sarcomeric pattern if it was co-expressed with MLC3nm, but it was distributed throughout the cytoplasm when expressed in combination with MLC1f, MLC3f or the slow skeletal/ventricular muscle isoform (MLC1sb). The MLC1sb was localized at the A-bands when it was co-expressed with MLC3nm or MLC1sa, while it was also distributed to the cytoplasm if co-expressed with MLC1f or MLC3f. Further, expression of chimeric cDNAs revealed that the N-terminal lobe of each isoprotein is responsible for the isoform-specific sorting pattern.

scholarly journals Two types of mRNA encoding myosin regulatory light chain in carp fast skeletal muscle differ in their 3' non-coding regions and expression patterns following temperature acclimation.

1998 ◽  
Vol 201 (20) ◽  
pp. 2815-2820 ◽  
Author(s):  
Y Hirayama ◽  
A Kobiyama ◽  
Y Ochiai ◽  
S Watabe
Keyword(s):  
Skeletal Muscle ◽  
Light Chain ◽  
Expression Patterns ◽  
Regulatory Light Chain ◽  
Amino Acid Sequences ◽  
Cdna Clones ◽  
Myosin Regulatory Light Chain ◽  
Fast Skeletal Muscle ◽  
Mrna Species ◽  
Mrna Transcripts

cDNA clones encoding the myosin regulatory light chain (RLC) were isolated from a cDNA library prepared from fast skeletal muscle of the carp Cyprinus carpio L. Two types of cDNA clone encoding carp RLC were found with identical deduced amino acid sequences. The two mRNAs differed in the number of polyadenylation signals prior to the poly(A) tail in the 3' non-coding region. The two mRNA species, with approximate sizes of 1.4 and 0.8 kilobases, were also observed in northern blot analysis. Carp were acclimated for a minimum of 5 weeks to either 10 degreesC or 30 degreesC (14 h:10 h light:dark photoperiod). The total levels of mRNA transcripts coding for the RLC and myosin heavy chain were, respectively, 3.3 and 3.9 times higher in cold- than in warm-acclimated fish. Differences in the levels of RLC in mRNA transcripts were largely due to the concentration of the 1.4 kilobase mRNA species.

scholarly journals Recapitulation of fast skeletal muscle development in zebrafish by transgenic expression of GFP under themylz2 promoter

2003 ◽  
Vol 227 (1) ◽  
pp. 14-26 ◽  
Author(s):  
Bensheng Ju ◽  
Shang Wei Chong ◽  
Jiangyan He ◽  
Xukun Wang ◽  
Yanfei Xu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Development ◽  
Skeletal Muscle Development ◽  
Fast Skeletal Muscle ◽  
Transgenic Expression

scholarly journals Key Genes Regulating Skeletal Muscle Development and Growth in Farm Animals

Animals ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 835
Author(s):  
Mohammadreza Mohammadabadi ◽  
Farhad Bordbar ◽  
Just Jensen ◽  
Min Du ◽  
Wei Guo
Keyword(s):  
Skeletal Muscle ◽  
Candidate Genes ◽  
Meat Quality ◽  
Muscle Development ◽  
Muscle Growth ◽  
Farm Animals ◽  
Meat Production ◽  
Skeletal Muscle Development ◽  
Extrinsic Factors ◽  
Myogenic Regulatory Factor

Farm-animal species play crucial roles in satisfying demands for meat on a global scale, and they are genetically being developed to enhance the efficiency of meat production. In particular, one of the important breeders’ aims is to increase skeletal muscle growth in farm animals. The enhancement of muscle development and growth is crucial to meet consumers’ demands regarding meat quality. Fetal skeletal muscle development involves myogenesis (with myoblast proliferation, differentiation, and fusion), fibrogenesis, and adipogenesis. Typically, myogenesis is regulated by a convoluted network of intrinsic and extrinsic factors monitored by myogenic regulatory factor genes in two or three phases, as well as genes that code for kinases. Marker-assisted selection relies on candidate genes related positively or negatively to muscle development and can be a strong supplement to classical selection strategies in farm animals. This comprehensive review covers important (candidate) genes that regulate muscle development and growth in farm animals (cattle, sheep, chicken, and pig). The identification of these genes is an important step toward the goal of increasing meat yields and improves meat quality.

Plectin regulates Wnt signaling mediated-skeletal muscle development by interacting with Dishevelled-2 and antagonizing autophagy

Gene ◽  
2021 ◽  
Vol 783 ◽  
pp. 145562
Author(s):  
Huadong Yin ◽  
Shunshun Han ◽  
Can Cui ◽  
Yan Wang ◽  
Diyan Li ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Wnt Signaling ◽  
Muscle Development ◽  
Skeletal Muscle Development
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