» Articles » PMID: 15750847

Myosin Light Chain Isoform Expression Among Single Mammalian Skeletal Muscle Fibers: Species Variations

Overview
Specialties Cell Biology
Physiology
Date 2005 Mar 8
PMID 15750847
Citations 16
Authors
Affiliations
Soon will be listed here.
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.

Citing Articles

The Acute, Short-, and Long-Term Effects of Endurance Exercise on Skeletal Muscle Transcriptome Profiles.

Beiter T, Zugel M, Hudemann J, Schild M, Fragasso A, Burgstahler C Int J Mol Sci. 2024; 25(5).

PMID: 38474128 PMC: 10932090. DOI: 10.3390/ijms25052881.


Myosin essential light chain 1sa decelerates actin and thin filament gliding on β-myosin molecules.

Osten J, Mohebbi M, Uta P, Matinmehr F, Wang T, Kraft T J Gen Physiol. 2022; 154(10).

PMID: 36053243 PMC: 9441736. DOI: 10.1085/jgp.202213149.


Thick Filament Protein Network, Functions, and Disease Association.

Wang L, Geist J, Grogan A, Hu L, Kontrogianni-Konstantopoulos A Compr Physiol. 2018; 8(2):631-709.

PMID: 29687901 PMC: 6404781. DOI: 10.1002/cphy.c170023.


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

Brundage E, Biesiadecki B, Reiser P J Muscle Res Cell Motil. 2015; 36(4-5):339-347.

PMID: 26400443 PMC: 4787561. DOI: 10.1007/s10974-015-9425-1.


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

Wang J, Wang Q, Wang C, Reinholt B, Grant A, Gerrard D Dev Biol. 2015; 402(1):72-80.

PMID: 25794679 PMC: 4435531. DOI: 10.1016/j.ydbio.2015.02.025.


References
1.
Ueda S, Yazaki Y . Heterogeneity of 27,000 dalton-light chain of cardiac ventricular myosin. J Biochem. 1981; 90(2):555-8. DOI: 10.1093/oxfordjournals.jbchem.a133505. View

2.
Reiser P, Kline W . Electrophoretic separation and quantitation of cardiac myosin heavy chain isoforms in eight mammalian species. Am J Physiol. 1998; 274(3):H1048-53. DOI: 10.1152/ajpheart.1998.274.3.H1048. View

3.
Timson D . Fine tuning the myosin motor: the role of the essential light chain in striated muscle myosin. Biochimie. 2003; 85(7):639-45. DOI: 10.1016/s0300-9084(03)00131-7. View

4.
Margossian S, LOWEY S . Preparation of myosin and its subfragments from rabbit skeletal muscle. Methods Enzymol. 1982; 85 Pt B:55-71. DOI: 10.1016/0076-6879(82)85009-x. View

5.
Cuda G, Fananapazir L, Zhu W, Sellers J, Epstein N . Skeletal muscle expression and abnormal function of beta-myosin in hypertrophic cardiomyopathy. J Clin Invest. 1993; 91(6):2861-5. PMC: 443355. DOI: 10.1172/JCI116530. View