• Journal of Animal Science and Technology
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• v.52 no.4
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• pp.329-336
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• 2010

Myogenic satellite cells (MSCs) are mononuclear, multipotent progenitors of adult skeletal muscle possessing a capacity of forming adipocyte-like cells (ALC). To identify the skeletal muscle type-specific myogenic and adipogenic genes during MSCs differentiation, total RNA was extracted from bovine MSCs, myotube-formed cell (MFC), and ALC from each of Beef shank, Longissimus dorsi, Deep pectoral, and Semitendinosus. DNA microarray analysis (24,000 oligo chip) comparing MSCs with MFC and ALC, respectively, revealed 135 differentially expressed genes (> 4 fold) among four cuts. Real-time PCR confirmed expression of 29 genes. Furthermore, the whole tissue sample RNAs analysis showed 6 differentially expressed genes in Beef shank. Among which, 1 gene in MSCs, 4 in MFC, and 1 in ALCs were highly expressed. This study will provide an insight for better understanding the molecular mechanism of differentiation of skeletal muscle type-specific MSCs. The identified genes may be used as marker to distinguish skeletal muscle types.

• Asian-Australasian Journal of Animal Sciences
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• v.27 no.5
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• pp.757-766
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• 2014

Postnatal muscle hypertrophy of beef cattle is the result of enhanced myofibrillar protein synthesis and reduced protein turnover. Skeletal muscle hypertrophy has been studied in cattle fed ${\beta}$-adrenergic agonists (${\beta}$-AA), which are receptor-mediated enhancers of protein synthesis and inhibitors of protein degradation. Feeding ${\beta}$-AA to beef cattle increases longissimus muscle cross-sectional area 6% to 40% compared to non-treated cattle. The ${\beta}$-AA have been reported to improve live animal performance, including average daily gain, feed efficiency, hot carcass weight, and dressing percentage. Treatment with ${\beta}$-AA increased mRNA concentration of the ${\beta}_2$ or ${\beta}_1$-adrenergic receptor and myosin heavy chain IIX in bovine skeletal muscle tissue. This review will examine the effects of skeletal muscle and adipose development with ${\beta}$-AA, and will interpret how the use of ${\beta}$-AA affects performance, body composition, and growth in beef cattle.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.29 no.6
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• pp.754-760
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• 1996

Effects of washing and additives on the texture of squid surimi gel which has been known to hard to gelation due to high protease activities and many water solubles were studied by SDS-PAGE, compression test, jelly strength and transmission electron microscopy analysis (TEM). Myosin (205 kDa) heavy chain was the major protein in water soluble fractions. It was impossible to make a gel after washing of the minced squid meat. These results suggested that squid (Todarodes pacificus) minced meat does not need a washing for good jelly products. $3.0\%$ of bovine plasma protein (BPP) produced the hardest gel ($16\%$ harder than the control) among the additives including egg white (EW), potato extracts (PE) and transglutaminase-K (TG-K) by compression test (P>0.05). Microstructure of control, $2\%$ EW and $4\%$ TG-K treated gels showed a sponge-like structure with more vacant space. Gels containing $3\%$ BPP formed the most rigid and arranged networks. Those results indicates that poor gel-network formation Was due to the degradation of myofibrillar proteins by proteases contained in the minced meat, which result in non-interlinkage.

• Korean Journal of Veterinary Research
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• v.24 no.2
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• pp.137-147
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• 1984

Cells with an epithelioid morphology were isolated from the rabbit myometrium and were grown in culture. The cells had a doubling time of 53 hours when grown in the presence of 10% fetal calf serum in Basal Eagle's medium with 3mM glutamine. In the presence of estrogen plus insulin, doubling time was reduced to 40 hours. Creatine kinase activity upon reaching confluency was determined to be 0.019 unit per mg protein. Approximately 30% of the activity was extractable only in high ionic strength buffer. Cells also contained plasminogen activator with a specific activity of 140 CTA units per million cells. Creatine kinase was mainly BB form. The cells contained a cross reactive protein against bovine smooth muscle uterine anti-myosin.

• Journal of Practical Agriculture & Fisheries Research
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• v.23 no.1
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• pp.117-128
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• 2021

The skeletal muscle development of Hanwoo steer has been processed in the prenatal and postnatal periods. Bovine satellite cell located in perimysium of muscle tissues has differentially distributed in peripheral tissues. The study of postnatal development of satellite cells can help understand the genetic and functional regulation of meat characteristics. Factors affecting muscle size increase are related to the accumulation of DNA or synthesis of RNA proteins. In this study, we observed muscle development and differentiation after culturing bovine satellite cells derived from longissimus dorsi and semimembranosus regions of Hanwoo muscle tissue. In addition, RNA sequencing data were analyzed for differentially expressed genes (DEG) involved in intracellular muscle development and growth. The DEG of the two muscle tissues were compared according to 1day, 2day, 4day, and 7day. The overall gene expression level was confirmed by the heat map. Gene Ontology (GO) classification method was used to compare the expression level of gene groups affecting LD and SM development. The histology of GO was consistent with the time-cause change of LD and SM cell morphology. SM showed more active skeletal muscle development than LD. Even within the same time, SM expressed more genes than LD, thus synthesizing more muscle fibers

• Reproductive and Developmental Biology
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• v.35 no.2
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• pp.151-157
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• 2011

Clinical arthritis is typically divided into rheumatoid arthritis (RA) and osteoarthritis (OA). Arthritis-induced muscle weakness is a major problem in aged people, leading to a disturbance of balance during the gait cycle and frequent falls. The purposes of the present study were to confirm fiber type-dependent expression of muscle atrophy markers induced by arthritis and to identify the relationship between clinical signs and expression of muscle atrophy markers. Mice were divided into four experimental groups as follows: (1) negative control (normal), (2) positive control (CFA+acetic acid), (3) RA group (CFA+acetic acid+type II collagen), and (4) aging-induced OA group. DBQA/1J mice (8 weeks of age) were injected with collagen (50 ${\mu}g/kg$), and physiological (body weight) and pathological (arthritis score and paw thickness) parameters were measured once per week. The gastrocnemius muscle from animals in each group was removed, and the expression of muscle atrophy markers (MAFbx and MuRF1) and myosin heavy chain isoforms were analyzed by reverse transcription-polymerase chain reaction. No significant change in body weight occurred between control groups and collagen-induced RA mice at week 10. However, bovine type II collagen induced a dramatic increase in clinical score or paw thickness at week 10 (p<0.01). Concomitantly, the expression of the muscle atrophy marker MAFbx was upregulated in the RA and OA groups (p<0.01). A dramatic reduction in myosin heavy chain (MHC)-$I{\beta}$ was seen in the gastrocnemius muscles from RA and OA mice, while only a slight decrease in MHC-IIb was seen. These results suggest that muscle atrophy gene expression occurred in a fiber type-specific manner in both RA- and OA-induced mice. The present study suggests evidence regarding why different therapeutic interventions are required between RA and OA.

• BMB Reports
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• v.34 no.6
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• pp.509-516
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• 2001

A genomic DNA fragment that contains the gene, which codes for a novel extracellular serine protease in Burkholderia pseudomallei, was cloned by using pQE40 as a vector. It was maintained in Escherichia coli JM109. The expression of the gene(s) resulted in the production of a 52 kDa protease. The recombinant protease was purified from the culture filtrate via ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography. The purified protease had an optimum pH and temperature of pH 8.9 and $38^{\circ}C$, respectively. The protease activity was inhibited by EGTA, EDTA, and PMSF, but not 1,10-phenanthroline. The first 11 amino acid residues from the N-terminus of the purified protease were identified as LAPNDPYYYGY. PNDPYY was found to show homology to the Bacillus cereus microbial serine protease and B. subtilis PD498 serine protease. These results indicate that the protease that was purified in this study is an extracellular calcium-dependent serine protease. The purified protease was able to digest the human serum 19A, IgG, albumin, and transferrin, as well as bovine muscle actin and myosin. Furthermore, it was able to promote or cause dermonecrosis in experimental rabbits. These results propose the possible role of a novel B. pseudomallei extracellular calcium-dependent serine protease in the virulence of the pathogen.

• Korean Journal of Food Science and Technology
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• v.18 no.3
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• pp.226-233
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• 1986

Myofibrillar proteins were prepared from red muscle and white muscle, and their thermostabilities were compared. Rate constants of inactivation of myofibrillar proteins were increased as the ionic strength of reaction mixture increased and also dielectric constant of reaction mixture decreased. Thermodynamic data forinactivation of myofibrillar proteins, such as $D-value,\;{\Delta}H^{\ddag},\;{\Delta}G{\ddag}\;and\;{\Delta}S^{\ddag$, revealed that thermostabilities of myofibrillar proteins from white muscle were higher than those from red muscle, and that myofibrillar proteins from chicken muscle were more heatlabile than from bovine muscle.

• Food Science of Animal Resources
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• v.29 no.3
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• pp.317-324
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• 2009

In order to reduce the increased hardness of beef bulgogi due to hydrostatic pressure (HP), kiwifruit (Actinidia chinensis) was applied. To understand the changes of shear force in beef bulgogi with kiwifruit induced by HP, changes in chemical properties of myofibril (Mf) with 10% kiwifruit induced by HP were investigated. From the SDS-PAGE patterns of Mf with 10% kiwifruit, there was an observed increase in the degradation of myosin heavy chain (MHC) by HP (300-500 MPa) to that by 0.1 MPa. This result indicates that HP may enhance enzyme action from a kiwifruit for the degradation of MHC, and the similar phenomenon occurred in the beef bulgogi with kiwifruit induced by HP. The shear force of beef bulgogi without a kiwifruit induced by 400 and 500 MPa significantly increased compared to that by 0.1 MPa (p<0.05). However, in the beef bulgogi with 10% or 20% kiwifruit, the shear force induced by 400 or 500 MPa was similar or slightly lower than that by 0.1 MPa. Consequently, adding kiwifruit to bulgogi could reduce the hardness of HP-induced beef bulgogi due to the enzyme action in the kiwifruit accelerated by HP.

• Food Science of Animal Resources
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• v.39 no.2
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• pp.229-239
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• 2019

The objectives of this study were to determine the interaction between porcine myofibrillar proteins and various gelatins (bovine hide, porcine skin, fish skin, and duck skin gelatins) and their impacts on gel properties of porcine myofibrillar proteins. Porcine myofibrillar protein was isolated from pork loin muscle (M. longissimus dorsi thoracis et lumborum). Control was prepared with only myofibrillar protein (60 mg/mL), and gelatin treatments were formulated with myofibrillar protein and each gelatin (9:1) at the same protein concentration. The myofibrillar protein-gelatin mixtures were heated from $10^{\circ}C$ to $75^{\circ}C$ ($2^{\circ}C/min$). Little to no impacts of gelatin addition on pH value and color characteristics of heat-induced myofibrillar protein gels were observed (p>0.05). The addition of gelatin slightly decreased cooking yield of heat-induced myofibrillar protein gels, but the gels showed lower centrifugal weight loss compared to control (p<0.05). The addition of gelatin significantly decreased hardness, cohesiveness, gumminess, and chewiness of heat-induced myofibrillar gels. Further, sodium dodecyl poly-acrylamide gel electrophoresis (SDS-PAGE) showed no interaction between myofibrillar proteins and gelatin under non-thermal conditions. Only a slight change in the endothermic peak (probably myosin) of myofibrillar protein-gelatin mixtures was found. The results of this study show that the addition of gelatin attenuated the water-holding capacity and textural properties of heat-induced myofibrillar protein gel. Thus, it could be suggested that well-known positive impacts of gelatin on quality characteristics of processed meat products may be largely affected by the functional properties of gelatin per se, rather than its interaction with myofibrillar proteins.