• Journal of Animal Science and Technology
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• 제52권4호
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• pp.329-336
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• 2010

본 연구는 소의 부위별 근육에 특이하게 발현하는 유전자 마커를 발굴하여 소고기의 부위를 과학적으로 판명할 수 있는 기술을 개발하고자 실시하였다. 이러한 연구 목표 아래 먼저 사태(Beef shank), 등심(Longissimus dorsi), 양지(Deep pectoral), 홍두깨(Semitendinosus) 부위의 근육조직에서 MSC (myogenic satellite cell, 근육줄기세포)를 순수 분리하고 이를 MFC (myotube-formed cell; 근관이 형성된 세포)로 분화시키거나 ALC (adipocyte-like cell; 지방세포와 유사한 세포)로 이형분화 시킨 후 3가지의 세포로 부터 각각의 RNA를 추출하였다. 이렇게 추출한 RNA는 24,000개의 bovine oligo-nucelotide (70 mer)가 집적된 microarray를 이용해 4개의 조직 중 1개의 조직에서만 MSC의 분화(MFC) 또는 이형분화 과정에서 mRNA의 발현이 증감을 보이는 유전자 135개를 먼저 발굴하였다. 135개의 유전자에 대해 microarray 분석에 사용한 동일한 RNA를 이용하여 real-time PCR 기술로 검증한 결과 총 29개의 유전자가 microarray 분석 결과와 유사함을 보였다. 29개의 유전자를 다시 4개 부위의 생체 조직에서 추출한 RNA를 이용해 real-time PCR 방법으로 분석한 결과 TS (thymi- dlyate synthase), TE (tropoelastin), RAD52(similar RAD52 motifcontaining protein 1), unknown gene), MLC2 (myosin light 2, regulatory cardiac, slow), TXNIP (thioredoxin-interating protein) 6개의 유전자만이 다른 부위에 비해 사태 부위에서 현저한 발현의 차이를 나타냈다. 결론적으로 본 연구를 통해 소 부위별 근육을 구분할 수 있는 과학적 기술의 토대를 확립하였다.

• Asian-Australasian Journal of Animal Sciences
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• 제27권5호
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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.

• 한국수산과학회지
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• 제29권6호
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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.

• 대한수의학회지
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• 제24권2호
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• pp.137-147
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• 1984

가토 자궁 근충에서 분리한 상피세포를 10% 송아지혈청, 3mM glutamine이 함유한 Basal Eagle 배지에서 배양한 결과 세포 성장 시간은 53시간이 소요되었고, estrogen에 insulin을 첨가했을 때는 40시간으로 감소하였다. Creatine kinase 활성 단위는 단백질 mg당 0.019 unit이었다. 활성의 30%가 이온상태가 높은 완충액에서 추출되었고, plasminogen 활성 인자는 세포 백만당 140 CTA unit였다.

• 현장농수산연구지
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• 제23권1호
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• pp.117-128
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• 2021

한우의 성장단계별 부위 근육발달을 이해하는 것은 도체율 개선에 따른 소득증대와 증체율 증가에 따른 생산효율 향상에 긍정적인 영향을 미친다. 본 연구에서는 한우의 등심과 사태 유래 근육위성세포를 분리 후 세포단위의 발달 및 분화를 비교하여 transcriptome 단위의 작용기전을 제시하였다. 한우의 부위별 근육 유래 근육위성세포의 근섬유의 양은 4일에 가장 높게 나타났고 이후 감소하였다. 한우의 근육위성세포의 발달 단계에 따라 발현되는 총 전사체 유전자의 종류는 사태근육 위성세포에서 높게 나타났다. 등심과 사태 근육 유래 위성세포의 발달단계에 따라 유의적인 차등 유전자 453개를 찾아냈고 이를 이용한 기능유 전체 분석이 필요하다. 등심과 사태유래 근육위성세포를 이용한 동일조건 분화 비교에서 사태유래 근육 위성세포의 분화 시 myosin complex, skeletal muscle contraction, troponin complex, skeletal muscle tissue development 와 같은 근섬유 형성관련 유전자의 발현이 높게 나타나는 것으로 보아 같은 개체의 근육조직에서도 부위별로 차등 발달이 되고 있다는 것을 알 수 있다. 기존 연구에서는 근육의 성장에 대한 이해를 위해 사양과 영양관련 시험이 많이 이루어졌다. 향후 세포단위의 연구들이 많이 이루어져 작용기작에 대한 생물정보 자료를 추가로 적용한다면 한우의 정밀사양을 적용할수 있는 바탕이 마련될 것이다. 또한 근육위성세포의 연구는 추후 동물실험 윤리제도 강화에 따른 비동물 전임상 screening 시험 활용과 대체단백질 산업의 주요 이슈인 배양육 소재 개발 연구와 같이 축산시험연구의 지속적인 확장성에 많은 영향을 미칠 것으로 생각된다.

• Reproductive and Developmental Biology
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• 제35권2호
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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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• 제34권6호
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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.

• 한국식품과학회지
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• 제18권3호
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• pp.226-233
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• 1986

근원섬유단백질의 열안정성에 대한 pH의 영향에 있어서 소의 근육의 경우에 fiber type에 따라 차이를 보이지 않으나, 닭의 근육의 경우에는 fiber type에 따라 안정 pH 범위에 차이를 나타내었다. 한편, 이온강도 및 유기용매의 농도변화에 따른 영향에 있어서는 이온강도가 증가함에 따라 그리고 유기용매의 농도가 증가함에 따라 변성속도가 증가하였으며, 또한 actomyosin의 열안정성이 myosin과 HMM의 열안정성보다 높은 것으로 나타났다. 열안정성에 대한 열역학량$(D\;value,Z\;value,\;{\Delta}H^{\ddag},\;{\Delta}S{\ddag},\;{\Delta}G^{\ddag})$은 red muscle과 white muscle 사이에 명백한 차이를 보였으며 white muscle이 red muscle보다 높은 열안정성을 나타내었으며, 동물의 종류에 따라서도 현저한 차이를 보였다.

• 한국축산식품학회지
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• 제29권3호
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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.

• 한국축산식품학회지
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• 제39권2호
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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.