骨骼肌兴奋收缩偶联与亲联蛋白
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摘要
背景:骨骼肌是人体的动力器官,其兴奋收缩偶联的结构和效率对运动者的活动能力和运动能力起关键作用。亲联蛋白的主要功能是维持三联管的超微结构和构成偶联膜复合体,从而为细胞膜到肌浆网之间的信号传导提供结构基础。目的:从骨骼肌的筋膜系统、三联管、兴奋收缩偶联方面和亲联蛋白分型、功能及与疾病的联系方面进行了归纳总结。方法:以"骨骼肌,筋膜,三联管,兴奋收缩偶联,亲联蛋白"和"skeletal muscles,fascia,the triad junction,Excitation-contraction Coupling,Junctophilins"为检索词,检索中国生物医学文献数据库(CBM)、CNKI数据库、PubMed及Elsevier数据库1987年9月至2018年4月期间收录的骨骼肌兴奋收缩偶联与亲联蛋白相关文章,排除与文章主题不相关的文献,最终纳入39篇文献进行综述。结果与结论:兴奋收缩偶联的结构基础是三联管,构成三联管的横管其实是筋膜系统的延伸,在三联管膜上有一些小分子蛋白,它们对三联管结构的维持和功能的发挥起关键作用,亲联蛋白就是连接三联管的横管和纵管系统的重要蛋白。亲联蛋白1是三联管膜上的重要因子,是偶联膜复合体的一部分,它连接肌细胞胞浆膜与肌浆网,使胞浆膜与肌浆网保持比较近的距离,保证了三联管的正常形态和数目,从而保证了钙信号的传导,保证了正常的兴奋收缩偶联过程。亲联蛋白受损与许多人类疾病有关,因而亲联蛋白有望成为这些疾病的靶向药物,为分子学干预措施提供思路。
BACKGROUND: Skeletal muscle is the power organ in human, and its excitation-contraction coupling structure and efficacy play important roles in movement and sport abilities of players. Junctophilin can sustain the ultrastructure of thribble and constitutes the coupling membrane complex, thus providing a structural basis for signal transduction between cell membrane and sarcoplasmic reticulum.OBJECTIVE: To summarize the fascia, thribble and excitation-contraction coupling of skeletal muscle, as well as type and function of junctophilin, and its association with diseases. METHODS: CBM, CNKI, PubMed and Elsevier databases were searched for the articles concerning excitation-contraction coupling of skeletal muscle and junctophilin published from September 1987 to April 2018. The keywords were "skeletal muscle, fascia, the triad junction, excitation-contraction coupling, junctophilins" in English and Chinese, respectively. Finally 39 eligible articles were enrolled after excluding irrelevant articles. RESULTS AND CONCLUSION: Thribble is the foundational structure for excitation-contraction coupling, whose transverse tubule is the extension of fascia. There are some small-molecule proteins on the thribble membrane, which are critical for sustaining the structure and function of thribble. Meanwhile, junctophilin is an important bridge between longitudinal and transverse tubules of thribble. Junctophilin 1 is an important factor on the membrane of thribble and a part of the coupling membrane complex, which connects the cytoplasmic membrane with sarcoplasmic reticulum, and thereby sustains the normal morphology and count of the thribble. Thereafter, calcium signal transduction remains normal, which ensures the process of excitation-contraction coupling. Junctophilin damage is related to various diseases, so it is a promising target for disease treatment and provides idea for molecular intervention.
BACKGROUND: Skeletal muscle is the power organ in human, and its excitation-contraction coupling structure and efficacy play important roles in movement and sport abilities of players. Junctophilin can sustain the ultrastructure of thribble and constitutes the coupling membrane complex, thus providing a structural basis for signal transduction between cell membrane and sarcoplasmic reticulum.OBJECTIVE: To summarize the fascia, thribble and excitation-contraction coupling of skeletal muscle, as well as type and function of junctophilin, and its association with diseases. METHODS: CBM, CNKI, PubMed and Elsevier databases were searched for the articles concerning excitation-contraction coupling of skeletal muscle and junctophilin published from September 1987 to April 2018. The keywords were "skeletal muscle, fascia, the triad junction, excitation-contraction coupling, junctophilins" in English and Chinese, respectively. Finally 39 eligible articles were enrolled after excluding irrelevant articles. RESULTS AND CONCLUSION: Thribble is the foundational structure for excitation-contraction coupling, whose transverse tubule is the extension of fascia. There are some small-molecule proteins on the thribble membrane, which are critical for sustaining the structure and function of thribble. Meanwhile, junctophilin is an important bridge between longitudinal and transverse tubules of thribble. Junctophilin 1 is an important factor on the membrane of thribble and a part of the coupling membrane complex, which connects the cytoplasmic membrane with sarcoplasmic reticulum, and thereby sustains the normal morphology and count of the thribble. Thereafter, calcium signal transduction remains normal, which ensures the process of excitation-contraction coupling. Junctophilin damage is related to various diseases, so it is a promising target for disease treatment and provides idea for molecular intervention.
引文
[1]Stecco A,Stern R,Fantoni I,et al.Fascial Disorders:Implications for Treatment.PM R.2016;8(2):161-168.
[2]常辉,李文惠.骨骼肌兴奋收缩偶联与细胞内的钙稳态[J].中国组织工程研究与临床康复,2010,14(50):9417-9420.
[3]马国震,李文惠,骆硕.骨骼肌三联管膜蛋白与兴奋收缩偶联[J].中国组织工程研究与临床康复,2011,15(2):347-350.
[4]张蓬,余跃,王世强.膜耦联的关键分子junctophilin.生理科学进展,2009,40(3):209-213.
[5]刘琳,黄强民,汤莉.肌筋膜疼痛触发点[J].中国组织工程研究,2014,18(46):7520-7527.
[6]刘琳,黄强民,刘庆广,等.肌筋膜触发点理论及其在运动康复临床实践中应用的研究进展[J].中国康复理论与实践,2016,22(10):1167-1170.
[7]Rossi D,Scarcella AM,Lorenzini S,et al.The Transmembrane Domain is Sufficient to Direct Junctophilin-1 Localization at the Junctional SR.Biophysical J.2016;10(3):98a.
[8]Takeshima H,Hoshijima M,Song LS.Ca2+microdomains organized by junctophilins.Cell Calcium.2015;(58):349-356.
[9]Daniela Rossi,Angela Maria Scarcella,Stefania Lorenzini.et al.Localization of Junctophilin-1 at the Junctional Sarcoplasmic Reticulum Requires a Sequence in the Transmembrane Domain.Biophysical J.2017;112(3).
[10]Sato D,Shannon TR,Bers DM.Sarcoplasmic Reticulum Structure and Functional Properties that Promote Long-Lasting Calcium Sparks.Biophysical J.2016;110(2):382-390.
[11]Mustroph J,Wagemann O,Lebek S,et al.SR Ca2+-leak and disordered excitation-contraction coupling as the basis for arrhythmogenic and negative inotropic effects of acute ethanol exposure.J Mol Cell Cardiol.2018;116:81-90.
[12]蔡斌,戴尅戎.评估肌肉疲劳的中枢和外周起源[J].医用生物力学,2015,30(2):192-196.
[13]李文惠,赵斌,闫万军.不同负荷间歇负重跑训练对老龄大鼠骨骼肌MG29蛋白的影响[J].体育科学,2010,30(9):73-81.
[14]Shinichiro Yamamoto,Tetsuo Yamazaki,Shinji Komazaki.Contribution of calumin to embryo genesis through participation in the endoplasmic reticulum-associated degradation activity.Developmental Biology.2014;393(1):33-43.
[15]王海.不同信号调节肌纤维类型转换的研究[J].体育科技,2014,35(5):74-75.
[16]武福云.Orai和STIM1相互作用机制研究[D].天津:南开大学,2014.
[17]Takeshima H,Komazaki S,NishiM,et al.Junctophilins:a novel family Of junctional membrane complex proteins.Mol Cell.2000;6:11-22.
[18]Landstrom AP,Beavers DL,Wehrens XH.The junctophilin family of proteins:from bench to bedside.Trends Mol Med.2014;20(6):353-362.
[19]Komazaki S,Ito K,Takeshima H,et al.Deficiency of triad formation in developing skeletal muscle cells lacking junctophilin type 1.FEBS Lett.2002;524(1-3):225-229.
[20]Hirata Y,Brotto M,Weisleder N,et al.Uncoupling Store-Operated Ca2+Entry and Altered Ca2+Release from Sarcoplasmic Reticulum through Silencing of Junctophilin Genes.Biophys J.2006;90(12):4418-4427.
[21]谢玉平,陈必义,王烈成.心肌肥厚或心肌衰竭中JUNCTOPHLIN-2和CAVEOLIN-3的表达变化[J].安徽医科大学学报,2011;46(7):623-626.
[22]Azad M,Khaledi N,Hedayati M.Effect of acute and chronic eccentric exercise on FOXO1 mRNA expression as fiber type transition factor in rat skeletal muscles.Gene.2016;584(2):17-19.
[23]Komazaki S,Nishi M,Takeshima H.Abnormal junctional membrane structures in cardiac myocytes expressing ectopic junctophilin type 1.Febs Letters.2003;542(1-3):69-73.
[24]梁星光,吴博文,张维晨.Junctophilin 1在小鼠胚胎干细胞定向分化心肌细胞及大鼠胚胎心肌发生中的表征[J].浙江大学学报(医学版),2012,41(4):359-365.
[25]郭文静.JPH2敲减抑制小鼠心肌细胞SK2蛋白的表达[D].郑州:郑州大学,2014.
[26]李妙龄,欧贤红,李涛.U慢性心房颤动降低Junctophilin-2在心房中的表达研究[J].重庆医学,2016,45(22):3046-3048.
[27]Reynolds JO,Quick AP,Wang Q,et al.Junctophilin-2 gene therapy rescues heart failure by normalizing RyR2-mediated Ca2+release.Int J Cardiol.2016;225:371-380.
[28]潘宗富.Junctophilin 3和4在胚胎干细胞神经分化早期作用研究[D].浙江:浙江大学,2016.
[29]Hai-Bo Zhang,Rong-Chang Li,Ming Xu,et al.Ultrastructural uncoupling between T-tubulesand sarco--plasmic reticulum in human heart failure,Cardiovasc.Res.2013;98(2):269-276.
[30]Matsushita Y,Furukawa T,Kasanuki H,et al.Mutation of junctophilin type 2 associated with Hypertrophic cardiomyopathy.J HumanGenet.2007;52:543-548.
[31]Landstrom AP,WeislederN,BataldenK B,et al.Mutations in JPH-2 encoded junctophilin-2 associated with hypertrophic cardiomyopathy in humans.J Mol Cell Cardiol.2007;42:1026-1035.
[32]Landstrom AP,Kellen CA,Dixit SS,et al.Junctophilin-2expression silencing causes cardiocyte hypertrophy and abnormal intracellular calcium-handling,Circ.Heart Fail.2011;(4):214-223.
[33]Zhang C,Chen B,Guo A,et al.Microtubule-mediated defects in junctophilin-2 traffick-ing contribute to myocyte transverse-tubule remodeling and Ca2+handlingdysfunction in heart failure.Circulation.2014;(129):1742-1750.
[34]Seixas AI,Holmes SE,Takeshima H,et al.Loss of junctophilin-3 con-tributes to Huntington disease-like 2pathogenesis,Ann.Neurol.2012;(71):245-257.
[35]Shannon H.Romer,Melissa Bautista,Daniel E.Hutcherson,et al.Architecture of Transverse Tubules and Triads in Huntington's Disease Skeletal Muscle.Biophysical J.2018;114(3):469a.
[36]Quick AP,Landstrom AP,Wang Q,et al.Novel Junctophilin-2Mutation A405S Is Associated With Basal Septal Hypertrophy and Diastolic Dysfunction.JACC Basic Transl Sci.2017;2(1):56-67.
[37]Quick AP,Landstrom AP,Wehrens XH.Novel JunJunctophilin-2 at the intersection of arrhythmia and pathologic cardiac remodeling.Heart Rhythm.2016;13(3):753-754.
[38]Roberts R.JPH2 Mutant Gene Causes Familial Hypertrophic Cardiomyopathy:A Possible Model to Unravel the Subtlety of Calcium-Regulated Contractility.JACC Basic Transl Sci.2017;2(1):68-70.
[39]Ujihara Y,Mohri S,Katanosaka Y.Effects of induced Na+/Ca2+exchanger overexpression on the spatial distribution of L-type Ca2+channels and junctophilin-2 in pressure-overloaded hearts.Biochem Biophys Res Commun.2016;480(4):564-569.
[2]常辉,李文惠.骨骼肌兴奋收缩偶联与细胞内的钙稳态[J].中国组织工程研究与临床康复,2010,14(50):9417-9420.
[3]马国震,李文惠,骆硕.骨骼肌三联管膜蛋白与兴奋收缩偶联[J].中国组织工程研究与临床康复,2011,15(2):347-350.
[4]张蓬,余跃,王世强.膜耦联的关键分子junctophilin.生理科学进展,2009,40(3):209-213.
[5]刘琳,黄强民,汤莉.肌筋膜疼痛触发点[J].中国组织工程研究,2014,18(46):7520-7527.
[6]刘琳,黄强民,刘庆广,等.肌筋膜触发点理论及其在运动康复临床实践中应用的研究进展[J].中国康复理论与实践,2016,22(10):1167-1170.
[7]Rossi D,Scarcella AM,Lorenzini S,et al.The Transmembrane Domain is Sufficient to Direct Junctophilin-1 Localization at the Junctional SR.Biophysical J.2016;10(3):98a.
[8]Takeshima H,Hoshijima M,Song LS.Ca2+microdomains organized by junctophilins.Cell Calcium.2015;(58):349-356.
[9]Daniela Rossi,Angela Maria Scarcella,Stefania Lorenzini.et al.Localization of Junctophilin-1 at the Junctional Sarcoplasmic Reticulum Requires a Sequence in the Transmembrane Domain.Biophysical J.2017;112(3).
[10]Sato D,Shannon TR,Bers DM.Sarcoplasmic Reticulum Structure and Functional Properties that Promote Long-Lasting Calcium Sparks.Biophysical J.2016;110(2):382-390.
[11]Mustroph J,Wagemann O,Lebek S,et al.SR Ca2+-leak and disordered excitation-contraction coupling as the basis for arrhythmogenic and negative inotropic effects of acute ethanol exposure.J Mol Cell Cardiol.2018;116:81-90.
[12]蔡斌,戴尅戎.评估肌肉疲劳的中枢和外周起源[J].医用生物力学,2015,30(2):192-196.
[13]李文惠,赵斌,闫万军.不同负荷间歇负重跑训练对老龄大鼠骨骼肌MG29蛋白的影响[J].体育科学,2010,30(9):73-81.
[14]Shinichiro Yamamoto,Tetsuo Yamazaki,Shinji Komazaki.Contribution of calumin to embryo genesis through participation in the endoplasmic reticulum-associated degradation activity.Developmental Biology.2014;393(1):33-43.
[15]王海.不同信号调节肌纤维类型转换的研究[J].体育科技,2014,35(5):74-75.
[16]武福云.Orai和STIM1相互作用机制研究[D].天津:南开大学,2014.
[17]Takeshima H,Komazaki S,NishiM,et al.Junctophilins:a novel family Of junctional membrane complex proteins.Mol Cell.2000;6:11-22.
[18]Landstrom AP,Beavers DL,Wehrens XH.The junctophilin family of proteins:from bench to bedside.Trends Mol Med.2014;20(6):353-362.
[19]Komazaki S,Ito K,Takeshima H,et al.Deficiency of triad formation in developing skeletal muscle cells lacking junctophilin type 1.FEBS Lett.2002;524(1-3):225-229.
[20]Hirata Y,Brotto M,Weisleder N,et al.Uncoupling Store-Operated Ca2+Entry and Altered Ca2+Release from Sarcoplasmic Reticulum through Silencing of Junctophilin Genes.Biophys J.2006;90(12):4418-4427.
[21]谢玉平,陈必义,王烈成.心肌肥厚或心肌衰竭中JUNCTOPHLIN-2和CAVEOLIN-3的表达变化[J].安徽医科大学学报,2011;46(7):623-626.
[22]Azad M,Khaledi N,Hedayati M.Effect of acute and chronic eccentric exercise on FOXO1 mRNA expression as fiber type transition factor in rat skeletal muscles.Gene.2016;584(2):17-19.
[23]Komazaki S,Nishi M,Takeshima H.Abnormal junctional membrane structures in cardiac myocytes expressing ectopic junctophilin type 1.Febs Letters.2003;542(1-3):69-73.
[24]梁星光,吴博文,张维晨.Junctophilin 1在小鼠胚胎干细胞定向分化心肌细胞及大鼠胚胎心肌发生中的表征[J].浙江大学学报(医学版),2012,41(4):359-365.
[25]郭文静.JPH2敲减抑制小鼠心肌细胞SK2蛋白的表达[D].郑州:郑州大学,2014.
[26]李妙龄,欧贤红,李涛.U慢性心房颤动降低Junctophilin-2在心房中的表达研究[J].重庆医学,2016,45(22):3046-3048.
[27]Reynolds JO,Quick AP,Wang Q,et al.Junctophilin-2 gene therapy rescues heart failure by normalizing RyR2-mediated Ca2+release.Int J Cardiol.2016;225:371-380.
[28]潘宗富.Junctophilin 3和4在胚胎干细胞神经分化早期作用研究[D].浙江:浙江大学,2016.
[29]Hai-Bo Zhang,Rong-Chang Li,Ming Xu,et al.Ultrastructural uncoupling between T-tubulesand sarco--plasmic reticulum in human heart failure,Cardiovasc.Res.2013;98(2):269-276.
[30]Matsushita Y,Furukawa T,Kasanuki H,et al.Mutation of junctophilin type 2 associated with Hypertrophic cardiomyopathy.J HumanGenet.2007;52:543-548.
[31]Landstrom AP,WeislederN,BataldenK B,et al.Mutations in JPH-2 encoded junctophilin-2 associated with hypertrophic cardiomyopathy in humans.J Mol Cell Cardiol.2007;42:1026-1035.
[32]Landstrom AP,Kellen CA,Dixit SS,et al.Junctophilin-2expression silencing causes cardiocyte hypertrophy and abnormal intracellular calcium-handling,Circ.Heart Fail.2011;(4):214-223.
[33]Zhang C,Chen B,Guo A,et al.Microtubule-mediated defects in junctophilin-2 traffick-ing contribute to myocyte transverse-tubule remodeling and Ca2+handlingdysfunction in heart failure.Circulation.2014;(129):1742-1750.
[34]Seixas AI,Holmes SE,Takeshima H,et al.Loss of junctophilin-3 con-tributes to Huntington disease-like 2pathogenesis,Ann.Neurol.2012;(71):245-257.
[35]Shannon H.Romer,Melissa Bautista,Daniel E.Hutcherson,et al.Architecture of Transverse Tubules and Triads in Huntington's Disease Skeletal Muscle.Biophysical J.2018;114(3):469a.
[36]Quick AP,Landstrom AP,Wang Q,et al.Novel Junctophilin-2Mutation A405S Is Associated With Basal Septal Hypertrophy and Diastolic Dysfunction.JACC Basic Transl Sci.2017;2(1):56-67.
[37]Quick AP,Landstrom AP,Wehrens XH.Novel JunJunctophilin-2 at the intersection of arrhythmia and pathologic cardiac remodeling.Heart Rhythm.2016;13(3):753-754.
[38]Roberts R.JPH2 Mutant Gene Causes Familial Hypertrophic Cardiomyopathy:A Possible Model to Unravel the Subtlety of Calcium-Regulated Contractility.JACC Basic Transl Sci.2017;2(1):68-70.
[39]Ujihara Y,Mohri S,Katanosaka Y.Effects of induced Na+/Ca2+exchanger overexpression on the spatial distribution of L-type Ca2+channels and junctophilin-2 in pressure-overloaded hearts.Biochem Biophys Res Commun.2016;480(4):564-569.