Literature DB >> 15750847

Myosin light chain isoform expression among single mammalian skeletal muscle fibers: species variations.

Sabahattin Bicer1, Peter J Reiser.   

Abstract

Extensive heterogeneity in myosin heavy chain and light chain (MLC) isoform expression in skeletal muscle has been well documented in several mammalian species. The initial objective of this study was to determine the extent of heterogeneity in myosin isoform expression among single fibers in limb muscles of dogs, a species for which relatively little has been reported. Fibers were isolated from muscles that have different functions with respect to limb extension and limb flexion and were analyzed on SDS gels, with respect to myosin isoform composition. The results of this part of the study indicate that there are at least four distinct fiber types in dog limb and diaphragm muscles, on the basis of MLC isoform expression: conventional fast (expressing fast-type isoforms of MLC1 (MLC1F) and MLC2 (MLC2F), plus MLC3), conventional slow (expressing slow-type MLC1 (MLC1S) and MLC2 (MLC2S)), hybrid (expressing MLC1S, MLC1F, MLC2S, MLC2F and MLC3) and a second slow fiber type, designated as S1F. S1F fibers express MLC1F, along with MLC1S and MLC2S and relatively low levels of MLC3. The fraction of slow fibers that are S1F fibers varies among dog limb muscles, being greater in limb extensors than flexors. Furthermore, the mean level of MLC1F in S1F fibers is greater in extensors than flexors (mean levels range from approximately 3% to 50% of total MLC1). The study was, therefore, extended to include six additional species, spanning a broad range in adult body size to more thoroughly characterize heterogeneity in MLC isoform expression among mammals. The results indicate that there are distinct patterns in MLC isoform expression among fast and slow fibers among different species. Specifically, large-size mammals have two distinct types of slow fibers, based upon MLC isoform composition (conventional and S1F fibers), whereas small mammals exhibit variations in MLC isoforms between different types of fast fibers, including a fast fiber type that expresses MLC1S (designated as F1S fibers). S1F fibers were absent in rodent muscles and F1S fibers were not found in large mammals. We conclude that extensive variation exists in MLC isoform expression in mammalian skeletal muscle fibers, yet there are distinct patterns among different species and among muscles within an individual species.

Entities:  

Mesh:

Substances:

Year:  2005        PMID: 15750847     DOI: 10.1007/s10974-004-5070-9

Source DB:  PubMed          Journal:  J Muscle Res Cell Motil        ISSN: 0142-4319            Impact factor:   2.698


  33 in total

Review 1.  Fine tuning the myosin motor: the role of the essential light chain in striated muscle myosin.

Authors:  David J Timson
Journal:  Biochimie       Date:  2003-07       Impact factor: 4.079

2.  Preparation of myosin and its subfragments from rabbit skeletal muscle.

Authors:  S S Margossian; S Lowey
Journal:  Methods Enzymol       Date:  1982       Impact factor: 1.600

3.  Heterogeneity of 27,000 dalton-light chain of cardiac ventricular myosin.

Authors:  S Ueda; Y Yazaki
Journal:  J Biochem       Date:  1981-08       Impact factor: 3.387

4.  Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species.

Authors:  P J Reiser; W O Kline
Journal:  Am J Physiol       Date:  1998-03

5.  Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres.

Authors:  R Bottinelli; R Betto; S Schiaffino; C Reggiani
Journal:  J Physiol       Date:  1994-07-15       Impact factor: 5.182

Review 6.  Tuning smooth muscle contraction by molecular motors.

Authors:  Ingo Morano
Journal:  J Mol Med (Berl)       Date:  2003-07-22       Impact factor: 4.599

7.  The multiplicity of combinations of myosin light chains and heavy chains in histochemically typed single fibres. Rabbit soleus muscle.

Authors:  R S Staron; D Pette
Journal:  Biochem J       Date:  1987-05-01       Impact factor: 3.857

8.  Myosin essential light chain isoforms modulate the velocity of shortening propelled by nonphosphorylated cross-bridges.

Authors:  J D Matthew; A S Khromov; K M Trybus; A P Somlyo; A V Somlyo
Journal:  J Biol Chem       Date:  1998-11-20       Impact factor: 5.157

9.  Functional significance of cardiac myosin essential light chain isoform switching in transgenic mice.

Authors:  J G Fewell; T E Hewett; A Sanbe; R Klevitsky; E Hayes; D Warshaw; D Maughan; J Robbins
Journal:  J Clin Invest       Date:  1998-06-15       Impact factor: 14.808

10.  Skeletal muscle expression and abnormal function of beta-myosin in hypertrophic cardiomyopathy.

Authors:  G Cuda; L Fananapazir; W S Zhu; J R Sellers; N D Epstein
Journal:  J Clin Invest       Date:  1993-06       Impact factor: 14.808

View more
  13 in total

1.  Subcellular proteomics of mice gastrocnemius and soleus muscles.

Authors:  Rui Vitorino; Rita Ferreira; Maria Neuparth; Sofia Guedes; Jason Williams; Kenneth B Tomer; Pedro M Domingues; Hans J Appell; José A Duarte; Francisco M L Amado
Journal:  Anal Biochem       Date:  2007-04-12       Impact factor: 3.365

2.  Influence of fast and slow alkali myosin light chain isoforms on the kinetics of stretch-induced force transients of fast-twitch type IIA fibres of rat.

Authors:  Oleg Andruchov; Stefan Galler
Journal:  Pflugers Arch       Date:  2007-10-25       Impact factor: 3.657

3.  Complex tropomyosin and troponin T isoform expression patterns in orbital and global fibers of adult dog and rat extraocular muscles.

Authors:  Sabahattin Bicer; Peter J Reiser
Journal:  J Muscle Res Cell Motil       Date:  2013-05-23       Impact factor: 2.698

4.  Heterogeneous activation of a slow myosin gene in proliferating myoblasts and differentiated single myofibers.

Authors:  Jing-Hua Wang; Qiao-Jing Wang; Chao Wang; Brad Reinholt; Alan L Grant; David E Gerrard; Shihuan Kuang
Journal:  Dev Biol       Date:  2015-03-17       Impact factor: 3.582

5.  Dependence of cross-bridge kinetics on myosin light chain isoforms in rabbit and rat skeletal muscle fibres.

Authors:  Oleg Andruchov; Olena Andruchova; Yishu Wang; Stefan Galler
Journal:  J Physiol       Date:  2005-12-15       Impact factor: 5.182

6.  Altered fast- and slow-twitch muscle fibre characteristics in female mice with a (S248F) knock-in mutation of the brain neuronal nicotinic acetylcholine receptor.

Authors:  David J Cannata; David I Finkelstein; Ilse Gantois; Yaroslav Teper; John Drago; Jan M West
Journal:  J Muscle Res Cell Motil       Date:  2009-04-29       Impact factor: 2.698

7.  Nucleotide and protein sequences for dog masticatory tropomyosin identify a novel Tpm4 gene product.

Authors:  Elizabeth A Brundage; Brandon J Biesiadecki; Peter J Reiser
Journal:  J Muscle Res Cell Motil       Date:  2015-09-23       Impact factor: 2.698

8.  Differential expression of sarcolipin protein during muscle development and cardiac pathophysiology.

Authors:  Gopal J Babu; Poornima Bhupathy; Cynthia A Carnes; George E Billman; Muthu Periasamy
Journal:  J Mol Cell Cardiol       Date:  2007-05-18       Impact factor: 5.000

9.  Induction of muscle weakness by local inflammation: an experimental animal model.

Authors:  S Bicer; P J Reiser; S Ching; N Quan
Journal:  Inflamm Res       Date:  2009-04       Impact factor: 4.575

10.  Inferring the transcriptional landscape of bovine skeletal muscle by integrating co-expression networks.

Authors:  Nicholas J Hudson; Antonio Reverter; YongHong Wang; Paul L Greenwood; Brian P Dalrymple
Journal:  PLoS One       Date:  2009-10-01       Impact factor: 3.240

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.