scholarly journals Muscle fiber type diversity revealed by anti‐myosin heavy chain antibodies

FEBS Journal ◽  
2018 ◽  
Vol 285 (20) ◽  
pp. 3688-3694 ◽  
Author(s):  
Stefano Schiaffino
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Fiber Type ◽  
Muscle Fiber Type

Muscle Fiber Type Composition, Myosin Heavy Chain Isoforms, And Enzyme Activities In Leptin Transgenic Mice

2005 ◽  
Vol 37 (Supplement) ◽  
pp. S287
Author(s):  
Sadayoshi Taguchi ◽  
Shin Nohara ◽  
Shinya Masuda ◽  
Miwa Nishimori ◽  
Takeshi Hashimoto ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Enzyme Activities ◽  
Fiber Type ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Fiber Type ◽  
Type Composition ◽  
Muscle Fiber Type Composition

scholarly journals Muscle fiber type characterization and myosin heavy chain (MyHC) isoform expression in Mediterranean buffaloes

Meat Science ◽  
2011 ◽  
Vol 88 (3) ◽  
pp. 535-541 ◽  
Author(s):  
C.L. Francisco ◽  
A.M. Jorge ◽  
M. Dal-Pai-Silva ◽  
F.R. Carani ◽  
L.C. Cabeço ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Fiber Type ◽  
Muscle Fiber Type ◽  
Isoform Expression

Muscle Fiber Type Composition, Myosin Heavy Chain Isoforms, And Enzyme Activities In Leptin Transgenic Mice

2005 ◽  
Vol 37 (Supplement) ◽  
pp. S287
Author(s):  
Sadayoshi Taguchi ◽  
Shin Nohara ◽  
Shinya Masuda ◽  
Miwa Nishimori ◽  
Takeshi Hashimoto ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Enzyme Activities ◽  
Fiber Type ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Fiber Type ◽  
Type Composition ◽  
Muscle Fiber Type Composition

scholarly journals Divergent effects of cold water immersion versus active recovery on skeletal muscle fiber type and angiogenesis in young men

2018 ◽  
Vol 314 (6) ◽  
pp. R824-R833 ◽  
Author(s):  
Randall F. D’Souza ◽  
Nina Zeng ◽  
James F. Markworth ◽  
Vandre C. Figueiredo ◽  
Llion A. Roberts ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Cold Water ◽  
Fiber Type ◽  
Water Immersion ◽  
Group Versus ◽  
Cold Water Immersion ◽  
Muscle Fiber Type ◽  
Active Recovery

Resistance training (RT) increases muscle fiber size and induces angiogenesis to maintain capillary density. Cold water immersion (CWI), a common postexercise recovery modality, may improve acute recovery, but it attenuates muscle hypertrophy compared with active recovery (ACT). It is unknown if CWI following RT alters muscle fiber type expression or angiogenesis. Twenty-one men strength trained for 12 wk, with either 10 min of CWI ( n = 11) or ACT ( n = 10) performed following each session. Vastus lateralis biopsies were collected at rest before and after training. Type IIx myofiber percent decreased ( P = 0.013) and type IIa myofiber percent increased with training ( P = 0.012), with no difference between groups. The number of capillaries per fiber increased from pretraining in the CWI group ( P = 0.004) but not the ACT group ( P = 0.955). Expression of myosin heavy chain genes ( MYH1 and MYH2), encoding type IIx and IIa fibers, respectively, decreased in the ACT group, whereas MYH7 (encoding type I fibers) increased in the ACT group versus CWI ( P = 0.004). Myosin heavy chain IIa protein increased with training ( P = 0.012) with no difference between groups. The proangiogenic vascular endothelial growth factor protein decreased posttraining in the ACT group versus CWI ( P < 0.001), whereas antiangiogenic Sprouty-related, EVH1 domain-containing protein 1 protein increased with training in both groups ( P = 0.015). Expression of microRNAs that regulate muscle fiber type (miR-208b and -499a) and angiogenesis (miR-15a, -16, and -126) increased only in the ACT group ( P < 0.05). CWI recovery after each training session altered the angiogenic and fiber type-specific response to RT through regulation at the levels of microRNA, gene, and protein expression.

Automated muscle fiber type population analysis with ImageJ of whole rat muscles using rapid myosin heavy chain immunohistochemistry

2016 ◽  
Vol 54 (2) ◽  
pp. 292-299 ◽  
Author(s):  
Konstantin D. Bergmeister ◽  
Marion Gröger ◽  
Martin Aman ◽  
Anna Willensdorfer ◽  
Krisztina Manzano-Szalai ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Fiber Type ◽  
Population Analysis ◽  
Muscle Fiber Type ◽  
Type Population

Age-Related Alterations in Myosin Heavy Chain Isoforms in Rat Intrinsic Laryngeal Muscles

2002 ◽  
Vol 111 (11) ◽  
pp. 962-967 ◽  
Author(s):  
Tatsutoshi Suzuki ◽  
Diane M. Bless ◽  
Nadine P. Connor ◽  
Charles N. Ford ◽  
Kyungah Lee ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Fiber Type ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Myosin Heavy Chain Isoforms ◽  
Laryngeal Muscles ◽  
Age Related ◽  
Posterior Cricoarytenoid

Deficits in voice and swallowing are found in the elderly, but the underlying neuromuscular mechanisms are unclear. A potential mechanism may be denervation-induced muscle fiber transformation to a slower-contracting type of muscle fiber. This study examined young, old, and denervated rat laryngeal muscles (lateral thyroarytenoid, lateral cricoarytenoid, and posterior cricoarytenoid) to examine differences in myosin heavy chain (MHC) composition. Results of sodium dodecyl sulfate–polyacrylamide gel electrophoresis analyses indicated that all muscles were composed predominately of type IIB MHC. With aging and denervation, type IIB was reduced and type IIX, a slower-contracting isoform, was increased in the lateral thyroarytenoid and lateral cricoarytenoid muscles. In the posterior cricoarytenoid muscle, the MHC composition was relatively unchanged. These findings suggest that aging may affect laryngeal adductory function by altering muscle fiber type composition to a slower-contracting isoform, in a manner similar to that observed with denervation.

Sign in / Sign up

Export Citation Format

Share Document