• 제목/요약/키워드: myofibril

검색결과 68건 처리시간 0.031초

Knockdown of Archvillin by siRNA Inhibits Myofibril Assembly in Cultured Skeletal Myoblast

  • Lee, Yeong-Mi;Kim, Hyun-Suk;Choi, Jun-Hyuk;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.251-261
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    • 2007
  • A myofiber of skeletal muscle is composed of myofibrils, sarcolemma (plasma membrane), and constameres, which anchor the myofibrils to the sarcolemma. Achvillin is a recently identified F-actin binding muscle protein, co-isolates with dystrophin and caveolin-3 in low-density sarcolemma of striated muscle, and colocalizes with dystrophin at costameres, the specialized adhesion sites in muscle. Archvillin also binds to nebulin and localizes at myofibrillar Z-discs, the lateral boundaries of the sarcomere in muscle. However other roles of archvillin on the dynamics of myofibrillogenesis remain to be defined. The goal of this study is, by using siRNA-mediated gene silencing technique, to investigate the effect of archvillin on the dynamics of myofibrillogenesis in cell culture of a mouse skeletal myogenic cell line (C2C12), where presumptive myoblasts withdraw from the cell cycle, fuse, undergo de novo myofibrillogenesis, and differentiate into mature myotubes. The roles of archvillin in the assembly and maintenance of myofibril and during the progression of myofibrillogenesis induced in skeletal myoblast following gene silencing in the cell culture were investigated. Fluorescence microscopy demonstrated that the distribution of archvillin was changed along the course of myofibril assembly with nebulin, vinculin and F-actin and then located at Z-lines with nebulin. Fluorescence microscopy demonstrated that knockdown of mouse archvillin expression led to an impaired assembly of new myofibrillar clusters and delayed fusion and myofibrillogenesis although the mouse archvillin siRNA did not affect those expressions of archvillin binding proteins, such as nebulin and F-actin. This result is corresponded with that of RT-PCR and western blots. When the perturbed archvillin was rescued by co-transfection with GFP or Red tagged human archvillin construct, the inhibited cell fusion and myotube formation was recovered. By using siRNA technique, archvillin was found to be involved in early stage of myofibrillogenesis. Therefore, the current data suggest the idea that archvillin plays critical roles on cell fusion and dynamic myofibril assembly.

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근원섬유단백질에 관한 연구 -제3보 Troponin-Tropomyosin Complex의 변화- (Studies on the Myofibrillar Proteins -Part III. Post-mortem Changes in Troponin-Tropomyosin Complexes-)

  • 양융;이용규
    • 한국식품과학회지
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    • 제9권4호
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    • pp.295-305
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    • 1977
  • 근원성유로 부터 근수축조절단백질들을 추출정제하고 저장중의 변화를 연구하여 다음과 같은 결과를 얻었다. 1. ${\alpha}-actinin$은 그 분자형(分子形)이나 생물활성(生物活性)에 아무런 변화도 일으키지 않았다. 2. 근육저장중에 근원섬유의 troponin-troponin complex의 함량은 감소되고 있으며 troponin-tropomyosin complex의 troponin함유비(含有比)는 낮아지고 있다.

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골격근의 구조와 생역학에 관한 고찰 (A Review of Structure and Biomechanics of the Skeletal Muscle)

  • 공원태
    • 대한정형도수물리치료학회지
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    • 제13권1호
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    • pp.58-66
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    • 2007
  • The purpose of this study is to understand the structure and biomechanics of the skeletal muscle. The skeletal muscle takes 40 to 45% of the whole body. Stable posture requires a balance of muscle. However, when the muscle strength is unbalanced, movement initiates. The power generated by the muscle is a primary means to adjust the equilibrium of posture and movement. The structural unit of the skeletal muscle is a long cylindrical type muscle fiber which contains hundreds of nucleus. The thickness of muscle fiber is about $10-100{\mu}m$, and its length is about 1-50cm. Muscle fiber is composed of myofibril that is covered with plasma membrane which is called sarcolemma. In understanding the movement of human body, it is important to comprehend the movement of bone and joint and the tension of muscle. Understanding the structure and biomechanics of muscle also provides basic information on clinical treatment of patients.

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홍삼의 Dexamethasone 유도 근감소증 모델 백서에 대한 효과 연구 (The Effect of Red Ginseng on Sarcopenic Rat)

  • 서윤정;류재환
    • 대한한방내과학회지
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    • 제39권6호
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    • pp.1168-1180
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    • 2018
  • Objective: As the number of sarcopenic patients worldwide is increasing, the need for the treatment of sarcopenia is increasing. Ginseng has been reported to be a major herbal supplement. We tested whether red ginseng would be effective for sarcopenia using red ginseng preparation which can be easily obtained locally in Korea. Methods: 30 rats were randomly divided into three groups: the control group (n=10) (Group C), the group with Dexamethasone -induced sarcopenia (n=10) (Group D), and the group to which red ginseng was administered group after induced sarcopenia with Dexamethasone (n=10) (Group DH). Dexamethasone was intraperitoneally administered to group D and group DH for 7 days to make sarcopenic model. After that, the red ginseng tablets prepared by Korea Ginseng Corporation were diluted in distilled water and administered orally to the DH group for 2 weeks. Body weight and grip strength were measured 8 times during the experiment. At the end of the experiment, blood was collected by cardiac puncture. In addition, the tibialis muscle was extracted, a myofibril cross section was measured by immunohistochemical staining and MyHC (myosin heavy chain) was quantified by Western blotting. Results: The ratio of the area on myofibril cross-section showed significant differences after administration of the red ginseng tablet. Conclusions: Red ginseng has a significant effect on the recovery of myofibril cross-section on sarcopenia. This experiment will be helpful for future clinical studies on drug effects in sarcopennia.

초음파처리가 노계 가슴육 근원섬유단백질의 수용화에 미치는 영향 (Effects of Sonication on the Water-solubilization of Myofibrillar Proteins from Breast Muscle of Spent Hen)

  • 조영준;이남혁;양승용;김영붕;김영호;임상동;전기홍;김기성
    • 한국축산식품학회지
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    • 제27권4호
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    • pp.457-462
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    • 2007
  • 본 연구에서는 노계 가슴육의 단백질 식품 소재로서 활용도를 높이기 위하여 초음파를 이용한 근원섬유 단백질의 수용화에 대하여 검토하였다. 근원섬유에 0.1-0.8 M NaCl, pH 6.0-8.0이 되도록 조절한 후 20 kHz에서 초음파 처리를 하였다. 그런 다음 이들의 용해도, SDS-PAGE, 점도, Ca- 및 Mg-ATPase 활성을 측정하였다. 각각의 처리 조건에서 용해도를 검토한 결과 초음파에 의해서 용해도는 증가하였으며 0.1 M NaCl, pH 8.0에서 약 90%를 나타내었다. 용해된 성분을 SDS-PAGE를 이용하여 검토한 결과 대부분 myosin heavy chain 및 actin에 상당하는 성분이 검출되었으며, 초음파에 의한 단백질의 분리는 근원 섬유 구조의 붕괴에 의한 것으로 사료되었다. 한편, 초음파에 의한 점도의 변화는 용해도가 높을수록 점도도 증가하였다. 그러나, Ca- 및 Mg-ATPase 활성은 초음파에 의해서 급격히 저하하였으며, 초음파에 의해서 분리되는 단백질은 대부분 변성이 진행된 상태인 것으로 사료되었다.

식이섬유 수준이 유색육용계의 육질에 미치는 영향 (Effect of Dietary Fiber Level on Meat Quality in Colored Broiler)

  • 김미숙;문윤희;임사비나;김대진
    • 생명과학회지
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    • 제7권4호
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    • pp.329-335
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    • 1997
  • This study was conducted to investigate the effect of dietary fiber(DF) levels on the meat quality in colored broiler. Colored broiler were fed on containing corn-soy basal diet(DF 5%) and high level(DF 6,7 and 8%) of dietary fiber diets for 7 weeks. Dietary fiber level of diet was make up by adding some alffalfa meal. Colored broiler meats were stored at 3$\circ$ for 24hr after skaughter, and used to analyze physico-chemical properties. Proximate component, pH, shear force value, myofibril fragmentation index, water holding capacity, cooking loss, protein extractability, fatty acid composition, Hunter's L, a value and palatability of cooked meat were not significantly affected by dietary fiber levels, whereas the Hunter's value of meat was significantly affected bty dietary fiber levels for the final period of feeding. Crude protein content, myofibril fragmentation index, water holding capacity, protein extractability and Hunter's b value of breast meat's were higher than thigh meat's, but crude fat content, pH, shear force value, cooking loss, palmitoleic acid, linolenic acid, and Hunter's a value were lower, regardless of dietary fiber level.

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Fine structure of the cardiac muscle cells in the orb-web spider Nephila clavata

  • Yan Sun;Hyo-Jeong Kim;Myung-Jin Moon
    • Applied Microscopy
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    • 제50권
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    • pp.9.1-9.8
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    • 2020
  • The fine structural characteristics of cardiac muscle cells and its myofibril organization in the orb web spider N. clavata were examined by transmission electron microscopy. Although myofibril striations are not remarkable as those of skeletal muscles, muscle fibers contain multiple myofibrils, abundant mitochondria, extensive sarcoplasmic reticulum and transverse tubules (T-tubules). Myofibrils are divided into distinct sarcomeres defined by Z-lines with average length of 2.0 ㎛, but the distinction between the A-band and the I-bands is not clear due to uniform striations over the length of the sarcomeres. Dyadic junction which consisted of a single T-tubule paired with a terminal cisterna of the sarcoplasmic reticulum is found mainly at the A-I level of sarcomere. Each cell is arranged to form multiple connections with neighboring cells through the intercalated discs. These specialized junctions include three types of intercellular junctions: gap junctions, fascia adherens and desmosomes for heart function. Our transmission electron microscopy (TEM) observations clearly show that spider's cardiac muscle contraction is controlled by neurogenic rather than myogenic mechanism since each cardiac muscle fiber is innervated by a branch of motor neuron through neuromuscular junctions.

건조방법과 한약재 추출물 첨가가 육포의 미세구조에 미치는 영향 (Effects of Drying Method and Medicinal Herb Extract Addition on the Microstructure of Beef Jerky)

  • 박추자;김미림;박찬성
    • 한국식품저장유통학회지
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    • 제16권6호
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    • pp.875-883
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    • 2009
  • 본 연구의 목적은 육포의 제조방법이 품질특성에 미치는 영향을 규명하기 위하여 기본 양념(간장, 물엿, 참기름, 정종, 마늘, 양파, 배즙)에 설탕(A), 감초(B), 3종류의 향신료(정향;C, 회향;D, 청양고추;E) 추출물과 여러 추출물을 혼합 첨가(F)한 6군으로 나누어 쇠고기를 절인후, 열풍건조와 송풍건조하는 육포의 제조과정에서 근육의 미세구조 변화를 주사전자현미경(SEM)과 투과전자현미경(TEM)으로 관찰하였다. 투과전자현미경(TEM)으로 관찰한 결과, 쇠고기는 액틴과 미오신의 근육라인과 근원섬유가 평행으로 발달되어 있었고 세포의 미토콘드리아와 내막을 볼 수 있었으나 절임과정에서 근섬유가 절단되고 근육라인의 분해 및 세포 구조물들의 퇴행이 일어났다. 주사전자현미경(SEM)으로 관찰한 결과, 자연건조한 한약재 추출물 첨가 육포는 근원 섬유와 공간구조가 남아있고 육질이 보존되어 있었으나 열풍건조한 육포는 근원섬유의 배열과 공간구조가 전혀 관찰되지 않았다. 이상의 주사전자현미경과 투과전자현미경으로 육포의 미세구조를 관찰한 결과에서 한약재 추출물은 근섬유의 결을 보존하는데 도움이 되며 송풍건조는 열풍 건조에 비하여 육포의 물성을 좋게 함으로써 품질을 향상시킬 수 있는 건조방법으로 생각된다.

a해산어의 부분동결에 의한 $Ca^{2+}\;및\;Mg^{2+}$ -dependent Adenosin Triphosphatase 활성 및 근섬유의 미세구조 변화 III. 저온저장 과정중 방어 근육조직의 미세구조의 변화 (Changes in the $Ca^{2+}\;and\;Mg^{2+}$ - dependent Adenosine Triphosphatase Activity and Ultrastructure of Marine Fishes by Partial Freezing III. Changes in the Ultrastructure of Muscle Tissues of Yellowtail during Low-temperature Preservation)

  • 최경호;박찬성
    • 한국식품영양과학회지
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    • 제20권6호
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    • pp.629-636
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    • 1991
  • 방어를 공시어로 하여 빙장($0^{\circ}C$), PF저장($-3^{\circ}C$) 및 동결저장($-20^{\circ}C$)하면서 자장과정중 일어나는 근육 조직의 변화를 현미경적으로 관찰하여 다음과 같은 결과를 얻었다. 빙장의 경우에는 저장 3일째에 glycogen이 소실되고 mitochondria 내막이 퇴행되었으며 근원섬유도 절단되었다. 근원섬유의 절단면은 동근 형태를 나타내었다. PF저장시에도 glycogen이 소실되고 mitochondria가 퇴행되었으나 그 정도는 빙장에 비하여 경미하였다. 저장 3일째에 빙결정이 생성되어 저장기간이 길어질수록 크기와 숫자가 증가되었으나 빙결정의 모양이 둥근 모습이었으며 주된 생성부위가 섬유속 사이로서 myofibril의 손상은 경미하였다. 동결저장시에는 저장 14일까지 glycogen입자가 관찰 되었고 mitochondria도 내막구조를 유지하였으나 저장 3일째부터 섬유속 내부에까지 빙결정이 생성되었으며 이로 인하여 myofibril이 손상되었다. 절단된 섬유속의 선단은 빙장의 경우와는 달리 불규칙한 모습이었다. 이상의 결과로부터 PF저장법이 단기간(약 2주)의 생선저장에는 빙장에 비하여 효소활성이 억제되고 동결저장에 비하여 빙결정에 의한 myofibril의 손상이 적은 효과적인 방법으로 판정되었다.

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