scholarly journals Muscle Fiber Typing in Bovine and Porcine Skeletal Muscles Using Immunofluorescence with Monoclonal Antibodies Specific to Myosin Heavy Chain Isoforms

2020 ◽  
Vol 40 (1) ◽  
pp. 132-144 ◽  
Author(s):  
Sumin Song ◽  
Chi-Hoon Ahn ◽  
Gap-Don Kim
Keyword(s):  
Monoclonal Antibodies ◽  
Myosin Heavy Chain ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Myosin Heavy Chain Isoforms

Muscle Fiber Types Expressing Different Myosin Heavy Chain Isoforms. Their Functional Properties and Adaptive Capacity

1990 ◽  
pp. 329-342 ◽  
Author(s):  
S. Schiaffino ◽  
L. Gorza ◽  
S. Ausoni ◽  
R. Bottinelli ◽  
C. Reggiani ◽  
...  
Keyword(s):  
Myosin Heavy Chain ◽  
Adaptive Capacity ◽  
Functional Properties ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Myosin Heavy Chain Isoforms ◽  
Muscle Fiber Types ◽  
Fiber Types

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

Pattern of Myosin Heavy Chain Isoforms in Different Fibre Types of Canine Trunk and Limb Skeletal Muscles

2004 ◽  
Vol 176 (4) ◽  
pp. 178-186 ◽  
Author(s):  
M. Štrbenc ◽  
V. Smerdu ◽  
M. Županc ◽  
N. Tozon ◽  
G. Fazarinc
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Myosin Heavy Chain Isoforms ◽  
Fibre Types

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.

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 Anti-myosin heavy chain monoclonal antibodies reveal two IIB (fast) fiber subtypes.

1989 ◽  
Vol 37 (11) ◽  
pp. 1721-1729 ◽  
Author(s):  
J F Marini ◽  
F Pons ◽  
M Anoal ◽  
J Leger ◽  
J J Leger
Keyword(s):  
Monoclonal Antibodies ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Gastrocnemius Muscle ◽  
Immunofluorescence Analysis ◽  
Plantaris Muscle ◽  
Fast Fiber ◽  
Age Dependent ◽  
Atpase Staining

Indirect immunofluorescence analysis of different rat skeletal muscles using anti-myosin heavy chain (MHC) monoclonal antibodies (MAb) revealed the presence of two immunologically distinct kinds of fibers within the IIB fibers, histochemically identified by myosin ATPase staining. Some IIB fibers (designated here as IIB1) were unreactive with one anti-fast MHC MAb, whereas they did react with another anti-fast MHC MAb; other IIB fibers (designated here as IIB2) reacted with both anti-fast MAbs. Neither of the two IIB fiber subtypes was significantly reactive with a neonatal MHC MAb. The number of each IIB fiber subtype was age-dependent, at least in the plantaris muscle. IIB1 fibers were observed only in the superficial portion of the plantaris and gastrocnemius muscle. The ratio of IIB1:IIB2 fibers was about the same throughout the extensor digitorum longus and extraocular muscles. Therefore, the two kinds of IIB fibers here observed have a different myosin heavy chain content. On the basis of their specific immunoreactivities, we suggest that IIB1 fibers contain the previously described MHCB. IIB2 fibers contain either a unique new MHC isoform or a mixture of at least two MHC, possibly composed of the MHCB and either the previously described MHCA or a new MHC isoform.

scholarly journals Evaluation of Myosin Heavy Chain Isoforms in Biopsied Longissimus Thoracis Muscle for Estimation of Meat Quality Traits in Live Pigs

Animals ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 9
Author(s):  
Min Young Park ◽  
Youn-Chul Ryu ◽  
Chung-Nam Kim ◽  
Kyung-Bo Ko ◽  
Jun-Mo Kim
Keyword(s):  
Myosin Heavy Chain ◽  
Meat Quality ◽  
Muscle Fiber ◽  
Heavy Chain ◽  
Rapid Identification ◽  
Poor Quality ◽  
Myosin Heavy Chain Isoforms ◽  
Type I ◽  
Fiber Number ◽  
Muscle Fiber Number

Estimating meat quality prior to slaughter will be beneficial for the rapid identification of specific traits or poor quality pork compared to a conventional assessment at postmortem. In this study, we identified and quantified myosin heavy chain (MHC) isoforms from a biopsied longissimus thoracis muscle of pigs, and determined their correlation with postmortem muscle fiber characteristics and meat quality. MHC slow and fast isoforms proportions from biopsied samples correlated with postmortem percentage of type I and type IIB muscle fibers, respectively (p < 0.05). The percentage of the biopsied MHC slow isoform showed a positive correlation with pH at 45 min postmortem, and negative correlations with filter-paper fluid uptake and drip loss in pork (p < 0.05). Furthermore, clustering the pigs into three groups based on the biopsied MHC isoform proportions was not only significantly associated with muscle fiber number and proportions of muscle fiber area, but also correlated with pH at 45 min postmortem and the National Pork Producers Council color score (p < 0.05). Collectively, our findings indicate that the biopsied MHC isoforms serve as parameter for estimating meat quality, with the association between the higher proportion of MHC slow isoforms and pH at 45 min postmortem in particular being indicative of better pork quality.

Myosin heavy chain isoforms expressed in bovine skeletal muscles

Meat Science ◽  
2004 ◽  
Vol 67 (1) ◽  
pp. 87-94 ◽  
Author(s):  
K Chikuni ◽  
S Muroya ◽  
I Nakajima
Keyword(s):  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Skeletal Muscles ◽  
Myosin Heavy Chain Isoforms
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