• 제목/요약/키워드: Skeletal Muscle Cells

검색결과 263건 처리시간 0.039초

Technical requirements for cultured meat production: a review

  • Ramani, Sivasubramanian;Ko, Deunsol;Kim, Bosung;Cho, Changjun;Kim, Woosang;Jo, Cheorun;Lee, Chang-Kyu;Kang, Jungsun;Hur, Sunjin;Park, Sungkwon
    • Journal of Animal Science and Technology
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    • 제63권4호
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    • pp.681-692
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    • 2021
  • Environment, food, and disease have a selective force on the present and future as well as our genome. Adaptation of livestock and the environmental nexus, including forest encroachment for anthropological needs, has been proven to cause emerging infectious diseases. Further, these demand changes in meat production and market systems. Meat is a reliable source of protein, with a majority of the world population consumes meat. To meet the increasing demands of meat production as well as address issues, such as current environmental pollution, animal welfare, and outbreaks, cellular agriculture has emerged as one of the next industrial revolutions. Lab grown meat or cell cultured meat is a promising way to pursue this; however, it still needs to resemble traditional meat and be assured safety for human consumption. Further, to mimic the palatability of traditional meat, the process of cultured meat production starts from skeletal muscle progenitor cells isolated from animals that proliferate and differentiate into skeletal muscle using cell culture techniques. Due to several lacunae in the current approaches, production of muscle replicas is not possible yet. Our review shows that constant research in this field will resolve the existing constraints and enable successful cultured meat production in the near future. Therefore, production of cultured meat is a better solution that looks after environmental issues, spread of outbreaks, antibiotic resistance through the zoonotic spread, food and economic crises.

Role of Dgat2 in Glucose Uptake and Fatty Acid Metabolism in C2C12 Skeletal Myotubes

  • So Young Bu
    • Journal of Microbiology and Biotechnology
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    • 제33권12호
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    • pp.1563-1575
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    • 2023
  • Acyl-coenzyme A (CoA):diacylglycerol acyltransferase 2 (DGAT2) catalyzes the last stage of triacylglycerol (TAG) synthesis, a process that forms ester bonds with diacylglycerols (DAG) and fatty acyl-CoA substrates. The enzymatic role of Dgat2 has been studied in various biological species. Still, the full description of how Dgat2 channels fatty acids in skeletal myocytes and the consequence thereof in glucose uptake have yet to be well established. Therefore, this study explored the mediating role of Dgat2 in glucose uptake and fatty acid partitioning under short interfering ribonucleic acid (siRNA)-mediated Dgat2 knockdown conditions. Cells transfected with Dgat2 siRNA downregulated glucose transporter type 4 (Glut4) messenger RNA (mRNA) expression and decreased the cellular uptake of [1-14C]-labeled 2-deoxyglucose up to 24.3% (p < 0.05). Suppression of Dgat2 deteriorated insulin-induced Akt phosphorylation. Dgat2 siRNA reduced [1-14C]-labeled oleic acid incorporation into TAG, but increased the level of [1-14C]-labeled free fatty acids at 3 h after initial fatty acid loading. In an experiment of chasing radioisotope-labeled fatty acids, Dgat2 suppression augmented the level of cellular free fatty acids. It decreased the level of re-esterification of free fatty acids to TAG by 67.6% during the chase period, and the remaining pulses of phospholipids and cholesteryl esters were decreased by 34.5% and 61%, respectively. Incorporating labeled fatty acids into beta-oxidation products increased in Dgat2 siRNA transfected cells without gene expression involving fatty acid oxidation. These results indicate that Dgat2 has regulatory function in glucose uptake, possibly through the reaction of TAG with endogenously released or recycled fatty acids.

랫드 근육세포에서 fagopyritol이 액틴 필라멘트 구조와 포도당 수송체 4에 미치는 영향 (Fagopyritol, a Derivative of D-chiro-inositol, Induces GLUT4 Translocation via Actin Filament Remodeling in L6-GLUT4myc Skeletal Muscle Cells)

  • 남하진;황인구;정혜리;권승해;박옥규;서준교
    • 생명과학회지
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    • 제23권9호
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    • pp.1163-1169
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    • 2013
  • 인슐린은 근육세포 표면으로 포도당 수송체 4(glucose transporter 4, GLUT4)를 유도하여 혈액 속의 포도당을 세포 내로 유입시키도록 작용한다고 알려져 있다. Fagopyritol은 인슐린과 유사한 작용을 하는 것으로 알려져 있으므로, 본 연구에서는 혈당강하 효과가 있다고 알려진 fagopyritol을 랫드의 근육세포주(L6GLUT4myc 세포)에 처리하여, 아직 명확하게 밝혀지지 않은 fagopyritol의 혈당강하 기전을 규명하고자 수행하였다. Fagopyritol의 혈당강하 기전을 규명하기 위하여 근원세포(myoblast)와 근관세포(myotube)에 fagopyritol을 처리하여 액틴 필라멘트의 구조와 GLUT4에 미치는 영향을 분석하였다. Fagopyritol을 myoblast에 처리하였을 때, GLUT4가 처리군에서 대조군과 비교하여 유의 있게 원형질막 쪽으로 유도되는 것을 확인하였고, 액틴 필라멘트의 구조가 재조정되면서 GLUT4의 이동을 돕는 것으로 생각된다. 또한 fagopyritol이 인슐린과 유사한 작용 경로를 가지는지 확인하기 위하여, 인슐린 작용 경로에서 중요한 역할을 하는 것으로 알려진 phosphatidylinositol 3-kinase (PI3K)의 억제제인 LY294002를 fagopyritol과 함께 처리하였을 때 GLUT4가 원형질막 쪽으로 유도되지 않는 것을 확인하였다. Fagopyritol을 myotube에 처리하였을 때, myoblast에 처리하였을 때와 유사한 결과를 나타내었다. 이러한 결과를 종합하면 fagopyritol이 인슐린과 유사한 작용을 하여 액틴 필라멘트의 구조 변경과 GLUT4의 이동을 촉진시키는 것으로 사료된다.

가족성 저칼륨성 주기성 마비에서 세포외 칼륨농도가 지연성 정류형 채널을 형성하는 KCNQ3와 KCNQ5 단백질에 미치는 효과 (Effect of Extracellular Potassium on Delayed Rectifier Potassium Channel Proteins of KCNQ3 and KCNQ5 in Familial Hypokalemic Periodic Paralysis)

  • 김성조;김동현;김준범
    • 생명과학회지
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    • 제19권10호
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    • pp.1484-1488
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    • 2009
  • 가족성 저칼륨성 주기성 마비란 상염색체 우성 유전 질환으로 저칼륨혈증을 동반한 간헐적인 가역적 이완성 근육 마비를 특징으로 한다. 세포내 저류된 칼륨으로 인해 저칼륨혈증이 지속되고 근세포 활성이상으로 인해 마비가 발생하는 것으로 알려져 있다. 이러한 증상발현의 분자생물학적 기전을 확인하기 위해 세포 내 칼륨이온을 세포 밖으로 이동시키는 지연성 정류형 채널 단백질의 일종인 KCNQ3와 KCNQ5를 대상으로, 정상인과 환자에서 채취한 골격근 세포를 생리적 세포외 정상 칼륨농도인 4 mM과 탈분극 유도를 위한 고칼륨농도인 50mM에 노출시켜 단백질의 양적 변화 유무를 확인하였다. 유전자 발현양상을 확인하기 위해 mRNA의 양적 변화를 확인한 결과 모든 조건에서 유의한 변화가 관찰되지 않아 정상 칼륨조건과 고칼륨조건이 두 유전자발현의 변화를 야기하지 않음을 확인하였다. 그러나 단백질 양을 관찰한 결과 환자의 골격근 세포가 50 mM의 칼륨농도에 노출되는 경우 KCNQ3 단백질은 세포질 내에서 증가하고 세포막 내에서 감소하였다. 이는 환자의 골격근 세포가 고농도의 세포외 칼륨에 의해 탈분극 되는 경우 재분극에 중요한 기능을 담당하는 KCNQ3 채널 단백질이 세포질 내로 이동하여 재분극 형성의 장애를 초래하고 이로 인해 근세포 활성이 일어나지 않게 되어 마비를 유발할 수 있음을 시사하는 결과로 본 질환의 새로운 발병 기전을 설명할 수 있는 근거로 생각된다.

Osteonectin Interacts with Human Nebulin C-terminus in Skeletal Muscle

  • Park, Eun-Ran;Kim, Hyun-Suk;Choi, Jun-Hyuk;Lee, Yeong-Mi;Choi, Jae-Kyoung;Joo, Young-Mi;Ahn, Seung-Ju;Min, Byung-In;Kim, Chong-Rak
    • 대한의생명과학회지
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    • 제13권4호
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    • pp.263-272
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    • 2007
  • Nebulin is a giant actin binding protein (600-900 kDa) which is specific to skeletal muscle. This protein is known to regulate thin filaments length in sarcomere as a molecular template. The C-terminus of nebulin is located in the Z-disc of muscle sarcomere and is bound to other proteins such like myopalladin, titin, archvillin, and desmin. The N-terminus of nebulin binds to tropomodulin at the pointed ends of the thin filaments. In recent research, nebulin not only found in brain but also expressed in heart, stomach, and liver. So, the roles of nebulin in non-muscle tissue have been studied. However, lack of information or studies on nebulin binding proteins and nebulin function in brain are available so far. Therefore, the current study have investigated a novel binding partner of Nebulin C-terminus by using yeast two-hybrid screening with human brain cDNA library. Nebulin C-terminus, containing simple repeats, serine rich and SH3 domain, interacts with osteonectin C-terminal region. The specific interaction of nebulin and osteonectin were confirmed in vitro by using GST pull-down assay and reconfirmed in vivo by using transfected COS-7 cells with EGFP-tagged nebulin and DsRed-tagged osteonectin. Consequently, this study identified SH3 domain in nebulin C-terminus specifically binds to extracellular Ca-binding (EeC domain in osteonectin. Also, nebulin C-terminus fusion protein colocalized with osteonectin EC domain fusion protein in transfected COS-7 cells. The current study found the interaction between nebulin and osteonectin in human brain for the first time and suggested the nebulin in brain may be associated with osteonectin, as a regulator of cell cycle progression and mitosis.

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Far-infrared rays enhance mitochondrial biogenesis and GLUT3 expression under low glucose conditions in rat skeletal muscle cells

  • Seo, Yelim;Kim, Young-Won;Lee, Donghee;Kim, Donghyeon;Kim, Kyoungseo;Kim, Taewoo;Baek, Changyeob;Lee, Yerim;Lee, Junhyeok;Lee, Hosung;Jang, Geonwoo;Jeong, Wonyeong;Choi, Junho;Hwang, Doegeun;Suh, Jung Soo;Kim, Sun-Woo;Kim, Hyoung Kyu;Han, Jin;Bang, Hyoweon;Kim, Jung-Ha;Zhou, Tong;Ko, Jae-Hong
    • The Korean Journal of Physiology and Pharmacology
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    • 제25권2호
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    • pp.167-175
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    • 2021
  • Far-infrared rays (FIR) are known to have various effects on atoms and molecular structures within cells owing to their radiation and vibration frequencies. The present study examined the effects of FIR on gene expression related to glucose transport through microarray analysis in rat skeletal muscle cells, as well as on mitochondrial biogenesis, at high and low glucose conditions. FIR were emitted from a bio-active material coated fabric (BMCF). L6 cells were treated with 30% BMCF for 24 h in medium containing 25 or 5.5 mM glucose, and changes in the expression of glucose transporter genes were determined. The expression of GLUT3 (Slc2a3) increased 2.0-fold (p < 0.05) under 5.5 mM glucose and 30% BMCF. In addition, mitochondrial oxygen consumption and membrane potential (ΔΨm) increased 1.5- and 3.4-fold (p < 0.05 and p < 0.001), respectively, but no significant change in expression of Pgc-1a, a regulator of mitochondrial biogenesis, was observed in 24 h. To analyze the relationship between GLUT3 expression and mitochondrial biogenesis under FIR, GLUT3 was down-modulated by siRNA for 72 h. As a result, the ΔΨm of the GLUT3 siRNA-treated cells increased 3.0-fold (p < 0.001), whereas that of the control group increased 4.6-fold (p < 0.001). Moreover, Pgc-1a expression increased upon 30% BMCF treatment for 72 h; an effect that was more pronounced in the presence of GLUT3. These results suggest that FIR may hold therapeutic potential for improving glucose metabolism and mitochondrial function in metabolic diseases associated with insufficient glucose supply, such as type 2 diabetes.

A New Insight into the Role of Calpains in Post-mortem Meat Tenderization in Domestic Animals: A review

  • Lian, Ting;Wang, Linjie;Liu, Yiping
    • Asian-Australasian Journal of Animal Sciences
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    • 제26권3호
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    • pp.443-454
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    • 2013
  • Tenderness is the most important meat quality trait, which is determined by intracellular environment and extracellular matrix. Particularly, specific protein degradation and protein modification can disrupt the architecture and integrity of muscle cells so that improves the meat tenderness. Endogenous proteolytic systems are responsible for modifying proteinases as well as the meat tenderization. Abundant evidence has testified that calpains (CAPNs) including calpain I (CAPN1) and calpastatin (CAST) have the closest relationship with tenderness in livestock. They are involved in a wide range of physiological processes including muscle growth and differentiation, pathological conditions and post-mortem meat aging. Whereas, Calpain3 (CAPN3) has been established as an important activating enzyme specifically expressed in livestock's skeletal muscle, but its role in domestic animals meat tenderization remains controversial. In this review, we summarize the role of CAPN1, calpain II (CAPN2) and CAST in post-mortem meat tenderization, and analyse the relationship between CAPN3 and tenderness in domestic animals. Besides, the possible mechanism affecting post-mortem meat aging and improving meat tenderization, and current possible causes responsible for divergence (whether CAPN3 contributes to animal meat tenderization or not) are inferred. Only the possible mechanism of CAPN3 in meat tenderization has been confirmed, while its exact role still needs to be studied further.

Differential Effects of Two Period Genes on the Physiology and Proteomic Profiles of Mouse Anterior Tibialis Muscles

  • Bae, Kiho;Lee, Kisoo;Seo, Younguk;Lee, Haesang;Kim, Dongyong;Choi, Inho
    • Molecules and Cells
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    • 제22권3호
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    • pp.275-284
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    • 2006
  • The molecular components that generate and maintain circadian rhythms of physiology and behavior in mammals are present both in the brain (suprachiasmatic nucleus; SCN) and in peripheral tissues. Examination of mice with targeted disruptions of either mPer1 or mPer2 has shown that these two genes have key roles in the SCN circadian clock. Here we show that loss of the clock gene mPer2 affects forced locomotor performance in mice without altering muscle contractility. A proteomic analysis revealed that the anterior tibialis muscles of the mPer2 knockout mice had higher levels of glycolytic enzymes such as triose phosphate isomerase and enolase than those of either the wild type or mPer1 knockout mice. In addition, the level of expression of HSP90 in the mPer2 mutant mice was also significantly higher than in wildtype mice. These results suggest that the reduced locomotor endurance of the mPer2 knockout mice reflects a greater dependence on anaerobic metabolism under stress conditions, and that the two canonical clock genes, mPer1 and mPer2, play distinct roles in the physiology of skeletal muscle.

고압맥동전류 자극이 흰쥐의 탈신경근 섬유 형태에 미치는 영향 (Effects of High Voltage Pulsed Galvanic Stimulation on Skeletal Muscle in Rats)

  • 박환진
    • The Journal of Korean Physical Therapy
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    • 제14권2호
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    • pp.145-152
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    • 2002
  • 고압맥동전류가 탈신경근의 형태에 미치는 영향을 알아보기 위하여 조직화학적 방법과 투과전자현미경적 관찰을 하였다. 웅성 흰쥐를 정상군, 탈신경군으로 각각 8마리씩 나누어 2주와 4주 후에 희생시켜 실험한 결과 다음과 같은 결과를 얻었다. 1. 조직화학적으로 형태를 관찰 한 결과 대조 1주군부터 근속과 근섬유사이에 염증세포가 관찰되고 핵이 근섬유속에 위치하는 것도 자주 관찰되었다. 2. 대조군도 비슷한 양상을 보였으나 4주군은 근괴사와 염증세포가 더욱 증가하였다. 3. 당원 1주군에서 실험군, 대조군 모두 정상근과 비슷한 양상을 보이나 4주군에서는 섬유를 구별할 수 없는 형태로 관찰되었다. 4. NADH-TR반응에서 적색섬유가 2주군에서 약간 증가하였고 그 후로는 구별이 불가능하였다. 5. 미세구조적으로 양쪽군 모두 근섬유가 굽어있고 mitochondria의 파괴로 인한 공포가 많이 관찰되었으나 전기자극 2주군에서는 일부에서 mitochondria증가를 관찰 하였다.

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Sasa borealis extract exerts an antidiabetic effect via activation of the AMP-activated protein kinase

  • Nam, Jung Soo;Chung, Hee Jin;Jang, Min Kyung;Jung, In Ah;Park, Seong Ha;Cho, Su In;Jung, Myeong Ho
    • Nutrition Research and Practice
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    • 제7권1호
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    • pp.15-21
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    • 2013
  • Leaf of Sasa borealis, a species of bamboo, has been reported to exhibit anti-hyperglycemic effect. However, its antidiabetic mechanism is not fully understood. In this study, we examined whether an extract of S. borealis activates AMP-activated protein kinase (AMPK) and exerts anti-hyperglycemic effects. Treatment with the S. borealis extract increased insulin signaling and phosphorylation of AMPK and stimulated the expression of its downstream targets, including $PPAR{\alpha}$, ACO, and CPT-1 in C2C12 cells and $PPAR{\alpha}$ in HepG2 cells. However, inhibition of AMPK activation attenuated insulin signaling and prevented the stimulation of AMPK target genes. The S. borealis extract increased glucose uptake in C2C12 cells and suppressed expression of the gluconeogenic gene, PEPCK in HepG2 cells. The extract significantly reduced blood glucose and triglyceride levels in STZ-induced diabetic mice. The extract enhanced AMPK phosphorylation and increased Glut-4 expression in the skeletal muscle of the mice. These findings demonstrated that the S. borealis extract exerts its anti-hyperglycemic effect through activation of AMPK and enhancement of insulin signaling.