Analysis of Myosin Heavy Chain Isoforms from Longissimus Thoracis Muscle of Hanwoo Steer by Electrophoresis and LC-MS/MS

Kim, Gap-Don

doi:10.5851/kosfa.2014.34.5.656

Cited by 4 publications

(5 citation statements)

References 23 publications

(34 reference statements)

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“…Previously, three fiber types, I, IIA, and IIX (or IIB), were observed in bovine muscles (Hwang et al, 2010;Kim et al, 2016;Ozawa et al, 2000), whereas hybrid fiber types were not frequently identified (Moreno-Sanchez et al, 2008;Greenwood et al, 2009). Fiber type IIB and hybrid type IIX+IIB were not detected in bovine muscle because of the lack of MHC 2b in major bovine muscles (LT, PM, and SM), as previously reported (Kim, 2014;Kim et al, 2016). Muscle fiber composition showed a similar trend to the results of previous reports (Hwang et al, 2010;Ozawa et al, 2000).…”

Section: Muscle Fiber Characteristicssupporting

confidence: 85%

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

Song¹,

Ahn²,

Kim³

2020

Food Sci Anim Resour

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The aim of this study was to optimize staining procedures for muscle fiber typing efficiently and rapidly in bovine and porcine skeletal muscles, such as longissimus thoracis, psoas major, semimembranosus, and semitendinosus muscles. The commercially available monoclonal anti-myosin heavy chain (MHC) antibodies and fluorescent dyeconjugated secondary antibodies were applied to immunofluorescence histology. Two different procedures, such as cocktail and serial staining, were adopted to immunofluorescence analysis. In bovine muscles, three pure types (I, IIA, and IIX) and one hybrid type, IIA+IIX, were identified by the cocktail procedure with a combination of BA-F8, SC-71, BF-35, and 6H1 anti-MHC antibodies. Porcine muscle fibers were typed into four pure types (I, IIA, IIX, and IIB) and two hybrid types (IIA+IIX and IIX+IIB) by a serial procedure with a combination of BA-F8, SC-71, BF-35, and BF-F3. Unlike for bovine muscle, the cocktail procedure was not recommended in porcine muscle fiber typing because of the abnormal reactivity of SC-71 antibody under cocktail procedure. Within the four antibodies, combinations of two or more anti-MHC antibodies allowed us to distinguish pure fiber types or all fiber types including hybrid types. Application of other secondary antibodies conjugated with different fluorescent dyes allowed us to get improved image resolution that clearly distinguished hybrid fibers. Muscle fiber characteristics differed depending on species and muscle types.

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Section: Muscle Fiber Characteristicssupporting

confidence: 85%

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

Song¹,

Ahn²,

Kim³

2020

Food Sci Anim Resour

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“…More recently, Moran et al and Gagaoua and co-workers from two different studies , found that the MyHC IIb isoform is present in very few animals only within very different groups of rearing practices and production systems. Using a proteomics-based approach following in-gel digestion with trypsin by LC-MS/MS mass spectrometry, Kim identified peptides specific to MyHC I, IIa, and IIx but did not identify a unique peptide of MyHC IIb in Longissimus thoracis muscle of Korean native steers. It is worthy to note that the protocol of Picard et al allowed a good separation of adult MyHCs but not of fetal and developmental MyHC isoforms (Figure b,c) compared to earlier protocols. , …”

Section: Techniques Allowing the Classification Of Muscle Fibersmentioning

confidence: 98%

“…As stated above, the contractile properties of a muscle could be further analyzed through electrophoretic separation (SDS-PAGE) of the different MyHC isoforms according to their molecular weights. However, these four different isoforms of MyHCs have close amino acid composition and consequently molecular weights (223.900, 224.243, 223.875, and 224.026 kDa for bovine MyHC I, IIa, IIx, IIb, respectively); hence, there is a difficulty to separate them with a high reproducibility . To avoid this, an accurate protocol was first proposed by Picard et al and another one recently by Scheffler et al to separate the different bovine MyHC isoforms in miniature polyacrylamide gels (Figure ).…”

Section: Techniques Allowing the Classification Of Muscle Fibersmentioning

confidence: 99%

“…From the large literature, earlier investigations on muscle fiber heterogeneity targeted two specific diversities that are the metabolism and the contractile response, which are known to differ depending on the type of the muscle and the species . In livestock species, the relationships between muscle properties and meat qualities were largely described over three decades. − These properties are acquired during fetal life and evolved during all of the life of the animal. − …”

Section: Introductionmentioning

confidence: 99%

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Muscle Fiber Properties in Cattle and Their Relationships with Meat Qualities: An Overview

Picard

Gagaoua

2020

J. Agric. Food Chem.

134

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The control of meat quality traits constitutes an important target for any farm animal production, including cattle. Therefore, better understanding of the biochemical properties that drive muscle development and final outcomes constitutes one of the main challenging topics of animal production and meat science. Accordingly, this review has focused on skeletal muscle fibers in cattle and their relationships with beef qualities. It aimed to describe the chemical and structural properties of muscle fibers as well as a comprehensive review of their contractile and metabolic characteristics during the life of the animal. The existing methods for the classification of muscle fibers were reviewed, compared, and discussed. Then, the different stages of myogenesis in cattle were defined. The main factors regulating fetal and postnatal growth and the plasticity of muscle fibers were evidenced, especially the role of myostatin growth factor and the impact of nutritional factors. This review highlights that the knowledge about muscle fibers is paramount for a better understanding of how to control the muscle properties throughout the life of the animal for better management of the final eating qualities of beef. Accordingly, the associations between bovine muscle fibers and different meat eating qualities such as tenderness, pH decline, and color traits were further presented.

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“…In our previous report, three myosin isoforms (myosin-1, -2, and -7) were identified from bovine longissimus muscle by analysis of LC-MS/MS ( Kim, 2014 ). However, additional analyses were needed because it was not confirmed whether myosin-4 existed in this muscle.…”

Section: Resultsmentioning

confidence: 99%

Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis

Jeong

Jung

Jeong

et al. 2016

Korean Journal for Food Science of Animal Resources

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The purpose of this study was to analyze oxidized methionines in the myosin isoforms of porcine longissimus thoracis, psoas major, and semimembranosus muscles by liquid chromatography (LC) and mass spectrometry (MS). A total of 836 queries matched to four myosin isoforms (myosin-1, -2, -4, and -7) were analyzed and each myosin isoform was identified by its unique peptides (7.3-13.3). Forty-four peptides were observed from all three muscles. Seventeen peptides were unique to the myosin isoform and the others were common peptides expressed in two or more myosin isoforms. Five were identified as oxidized peptides with one or two methionine sulfoxides with 16 amu of mass modification. Methionines on residues 215 (215), 438 (438), 853 (851), 856 (854), 1071 (1069), and 1106 (1104) of myosin-1 (myosin-4) were oxidized by the addition of oxygen. Myosin-2 had two oxidized methionines on residues 215 and 438. No queries matched to myosin-7 were observed as oxidized peptides. LC-MS/MS allows analysis of the oxidation of specific amino acids on specific residue sites, as well as in specific proteins in the food system.

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Analysis of Myosin Heavy Chain Isoforms from Longissimus Thoracis Muscle of Hanwoo Steer by Electrophoresis and LC-MS/MS

Cited by 4 publications

References 23 publications

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

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

Muscle Fiber Properties in Cattle and Their Relationships with Meat Qualities: An Overview

Analysis of Methionine Oxidation in Myosin Isoforms in Porcine Skeletal Muscle by LC-MS/MS Analysis

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