메뉴 건너뛰기




Volumn 97, Issue 8, 2009, Pages 2277-2286

Tuning passive mechanics through differential splicing of titin during skeletal muscle development

Author keywords

[No Author keywords available]

Indexed keywords

3,5,3' TRI IODO LEVO THYRONINE; 3,5,3',5' TETRA IODO LEVO THYRONINE; CONNECTIN; LYSINE; PROLYLGLUTAMYLVALYLLYSINE; THYRONINE; UNCLASSIFIED DRUG;

EID: 70449124198     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2009.07.041     Document Type: Article
Times cited : (55)

References (36)
  • 1
    • 0029896830 scopus 로고    scopus 로고
    • Molecular diversity of myofibrillar proteins: Gene regulation and functional significance
    • Schiaffino, S., and C. Reggiani. 1996. Molecular diversity of myofibrillar proteins: gene regulation and functional significance. Physiol. Rev. 76:371-423.
    • (1996) Physiol. Rev. , vol.76 , pp. 371-423
    • Schiaffino, S.1    Reggiani, C.2
  • 2
    • 1842414218 scopus 로고    scopus 로고
    • Soleus muscle length, stretch reflex excitability, and the contractile properties of muscle in children and adults: A study of the functional joint angle
    • Lin, J. P., J. K. Brown, and E. G. Walsh. 1997. Soleus muscle length, stretch reflex excitability, and the contractile properties of muscle in children and adults: a study of the functional joint angle. Dev. Med. Child Neurol. 39:469-480.
    • (1997) Dev. Med. Child Neurol. , vol.39 , pp. 469-480
    • Lin, J.P.1    Brown, J.K.2    Walsh, E.G.3
  • 3
    • 0032845705 scopus 로고    scopus 로고
    • Passive dynamics of the knee joint in healthy children and children affected by spastic paresis
    • Lebiedowska, M. K., and J. R. Fisk. 1999. Passive dynamics of the knee joint in healthy children and children affected by spastic paresis. Clin. Biomech. (Bristol, Avon). 14:653-660.
    • (1999) Clin. Biomech. (Bristol, Avon) , vol.14 , pp. 653-660
    • Lebiedowska, M.K.1    Fisk, J.R.2
  • 5
    • 0028019009 scopus 로고
    • Effect of ageing on ultrastructure of slow and fast skeletal muscle tendon in rabbit Achilles tendons
    • Nakagawa, Y., T. Majima, and K. Nagashima. 1994. Effect of ageing on ultrastructure of slow and fast skeletal muscle tendon in rabbit Achilles tendons. Acta Physiol. Scand. 152:307-313.
    • (1994) Acta Physiol. Scand. , vol.152 , pp. 307-313
    • Nakagawa, Y.1    Majima, T.2    Nagashima, K.3
  • 6
    • 0025215287 scopus 로고
    • Elastic energy storage in tendons: Mechanical differences related to function and age
    • Shadwick, R. E. 1990. Elastic energy storage in tendons: mechanical differences related to function and age. J. Appl. Physiol. 68:1033-1040.
    • (1990) J. Appl. Physiol. , vol.68 , pp. 1033-1040
    • Shadwick, R.E.1
  • 7
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules, and intermediate filaments
    • Granzier, H. L., and T. C. Irving. 1995. Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments. Biophys. J. 68:1027-1044.
    • (1995) Biophys. J. , vol.68 , pp. 1027-1044
    • Granzier, H.L.1    Irving, T.C.2
  • 8
    • 0345276717 scopus 로고    scopus 로고
    • Resting tension characteristics in differentiating intact rat fast- and slow-twitch muscle fibers
    • Mutungi, G., J. Trinick, and K. W. Ranatunga. 2003. Resting tension characteristics in differentiating intact rat fast- and slow-twitch muscle fibers. J. Appl. Physiol. 95:2241-2247.
    • (2003) J. Appl. Physiol. , vol.95 , pp. 2241-2247
    • Mutungi, G.1    Trinick, J.2    Ranatunga, K.W.3
  • 9
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • Granzier, H. L., and S. Labeit. 2004. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ. Res. 94:284-295.
    • (2004) Circ. Res. , vol.94 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 10
    • 0023576830 scopus 로고
    • The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: Evidence for the role of titin filaments
    • Horowits, R., and R. J. Podolsky. 1987. The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: evidence for the role of titin filaments. J. Cell Biol. 105:2217-2223.
    • (1987) J. Cell Biol. , vol.105 , pp. 2217-2223
    • Horowits, R.1    Podolsky, R.J.2
  • 11
    • 0032559640 scopus 로고    scopus 로고
    • Titin extensibility in situ: Entropic elasticity of permanently folded and permanently unfolded molecular segments
    • DOI 10.1083/jcb.140.4.853
    • Trombitas, K., M. Greaser, S. Labeit, J. P. Jin, M. Kellermayer, et al. 1998. Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments. J. Cell Biol. 140:853-859. (Pubitemid 28141223)
    • (1998) Journal of Cell Biology , vol.140 , Issue.4 , pp. 853-859
    • Trombitas, K.1    Greaser, M.2    Labeit, S.3    Jin, J.-P.4    Kellermayer, M.5    Helmes, M.6    Granzier, H.7
  • 12
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang, M. L., T. Centner, F. Fornoff, A. J. Geach, M. Gotthardt, et al. 2001. The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ. Res. 89:1065-1072.
    • (2001) Circ. Res. , vol.89 , pp. 1065-1072
    • Bang, M.L.1    Centner, T.2    Fornoff, F.3    Geach, A.J.4    Gotthardt, M.5
  • 13
    • 34547629201 scopus 로고    scopus 로고
    • Functional genomics of chicken, mouse, and human titin supports splice diversity as an important mechanism for regulating biomechanics of striated muscle
    • Granzier, H., M. Radke, J. Royal, Y. Wu, T. C. Irving, et al. 2007. Functional genomics of chicken, mouse, and human titin supports splice diversity as an important mechanism for regulating biomechanics of striated muscle. Am. J. Physiol. Regul. Integr. Comp. Physiol. 293:R557-R567.
    • (2007) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.293
    • Granzier, H.1    Radke, M.2    Royal, J.3    Wu, Y.4    Irving, T.C.5
  • 14
    • 1242281665 scopus 로고    scopus 로고
    • Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium
    • Lahmers, S., Y. Wu, D. R. Call, S. Labeit, and H. Granzier. 2004. Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium. Circ. Res. 94:505-513.
    • (2004) Circ. Res. , vol.94 , pp. 505-513
    • Lahmers, S.1    Wu, Y.2    Call, D.R.3    Labeit, S.4    Granzier, H.5
  • 15
    • 33746861905 scopus 로고    scopus 로고
    • 2+ sensitivity due to titin and troponin-I isoform switching are not critically triggered by birth
    • 2+ sensitivity due to titin and troponin-I isoform switching are not critically triggered by birth. Am. J. Physiol. Heart Circ. Physiol. 291:H496-H506.
    • (2006) Am. J. Physiol. Heart Circ. Physiol. , vol.291
    • Kruger, M.1    Kohl, T.2    Linke, W.A.3
  • 17
    • 41949113903 scopus 로고    scopus 로고
    • Thyroid hormone regulates developmental titin isoform transitions via the phosphatidylinositol-3-kinase/ AKT pathway
    • Kruger, M., C. Sachse, W. H. Zimmermann, T. Eschenhagen, S. Klede, et al. 2008. Thyroid hormone regulates developmental titin isoform transitions via the phosphatidylinositol-3-kinase/ AKT pathway. Circ. Res. 102:439-447.
    • (2008) Circ. Res. , vol.102 , pp. 439-447
    • Kruger, M.1    Sachse, C.2    Zimmermann, W.H.3    Eschenhagen, T.4    Klede, S.5
  • 18
    • 34547094568 scopus 로고    scopus 로고
    • Structural and regulatory roles of muscle ankyrin repeat protein family in skeletal muscle
    • Barash, I. A., M. L. Bang, L. Mathew, M. L. Greaser, J. Chen, et al. 2007. Structural and regulatory roles of muscle ankyrin repeat protein family in skeletal muscle. Am. J. Physiol. Cell Physiol. 293:C218-C227.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.293
    • Barash, I.A.1    Bang, M.L.2    Mathew, L.3    Greaser, M.L.4    Chen, J.5
  • 19
    • 33845605523 scopus 로고    scopus 로고
    • Hypothyroidism leads to increased collagen-based stiffness and re-expression of large cardiac titin isoforms with high compliance
    • Wu, Y., J. Peng, K. B. Campbell, S. Labeit, and H. Granzier. 2007. Hypothyroidism leads to increased collagen-based stiffness and re-expression of large cardiac titin isoforms with high compliance. J. Mol. Cell. Cardiol. 42:186-195.
    • (2007) J. Mol. Cell. Cardiol. , vol.42 , pp. 186-195
    • Wu, Y.1    Peng, J.2    Campbell, K.B.3    Labeit, S.4    Granzier, H.5
  • 20
    • 0038219368 scopus 로고    scopus 로고
    • Vertical agarose gel electrophoresis and electroblotting of high-molecular-weight proteins
    • Warren, C. M., P. R. Krzesinski, and M. L. Greaser. 2003. Vertical agarose gel electrophoresis and electroblotting of high-molecular-weight proteins. Electrophoresis. 24:1695-1702.
    • (2003) Electrophoresis , vol.24 , pp. 1695-1702
    • Warren, C.M.1    Krzesinski, P.R.2    Greaser, M.L.3
  • 21
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • Labeit, S., and B. Kolmerer. 1995. The complete primary structure of human nebulin and its correlation to muscle structure. J. Mol. Biol. 248:308-315.
    • (1995) J. Mol. Biol. , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 22
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S., and B. Kolmerer. 1995. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science. 270:293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 23
    • 15244348075 scopus 로고    scopus 로고
    • Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner
    • Fukuda, N., Y. Wu, P. Nair, and H. L. Granzier. 2005. Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner. J. Gen. Physiol. 125:257-271.
    • (2005) J. Gen. Physiol. , vol.125 , pp. 257-271
    • Fukuda, N.1    Wu, Y.2    Nair, P.3    Granzier, H.L.4
  • 24
    • 0030014385 scopus 로고    scopus 로고
    • Effects of thyroid hormone on the androgenic expression of KAP gene in mouse kidney
    • Sole, E., R. Calvo, M. J. Obregon, and A. Meseguer. 1996. Effects of thyroid hormone on the androgenic expression of KAP gene in mouse kidney. Mol. Cell. Endocrinol. 119:147-159.
    • (1996) Mol. Cell. Endocrinol. , vol.119 , pp. 147-159
    • Sole, E.1    Calvo, R.2    Obregon, M.J.3    Meseguer, A.4
  • 25
    • 0031691961 scopus 로고    scopus 로고
    • PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10
    • Trombitas, K., M. Greaser, G. French, and H. Granzier. 1998. PEVK extension of human soleus muscle titin revealed by immunolabeling with the anti-titin antibody 9D10. J. Struct. Biol. 122:188-196.
    • (1998) J. Struct. Biol. , vol.122 , pp. 188-196
    • Trombitas, K.1    Greaser, M.2    French, G.3    Granzier, H.4
  • 26
    • 0022079716 scopus 로고
    • Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils
    • Wang, S. M., and M. L. Greaser. 1985. Immunocytochemical studies using a monoclonal antibody to bovine cardiac titin on intact and extracted myofibrils. J. Muscle Res. Cell Motil. 6:293-312.
    • (1985) J. Muscle Res. Cell Motil. , vol.6 , pp. 293-312
    • Wang, S.M.1    Greaser, M.L.2
  • 27
    • 0142247618 scopus 로고    scopus 로고
    • The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules
    • Miller, M. K., M. L. Bang, C. C. Witt, D. Labeit, C. Trombitas, et al. 2003. The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules. J. Mol. Biol. 333:951-964.
    • (2003) J. Mol. Biol. , vol.333 , pp. 951-964
    • Miller, M.K.1    Bang, M.L.2    Witt, C.C.3    Labeit, D.4    Trombitas, C.5
  • 28
    • 0036098270 scopus 로고    scopus 로고
    • Carp, a cardiac ankyrin-repeated protein, and its new homologue, Arpp, are differentially expressed in heart, skeletal muscle, and rhabdomyosarcomas
    • Ishiguro, N., T. Baba, T. Ishida, K. Takeuchi, M. Osaki, et al. 2002. Carp, a cardiac ankyrin-repeated protein, and its new homologue, Arpp, are differentially expressed in heart, skeletal muscle, and rhabdomyosarcomas. Am. J. Pathol. 160:1767-1778.
    • (2002) Am. J. Pathol. , vol.160 , pp. 1767-1778
    • Ishiguro, N.1    Baba, T.2    Ishida, T.3    Takeuchi, K.4    Osaki, M.5
  • 29
    • 0031874411 scopus 로고    scopus 로고
    • Effect of propylthiouracil-induced hypothyroidism on the onset of skeletal muscle necrosis in dystrophin-deficient mdx mice
    • McArdle, A., T. R. Helliwell, G. J. Beckett, M. Catapano, A. Davis, et al. 1998. Effect of propylthiouracil-induced hypothyroidism on the onset of skeletal muscle necrosis in dystrophin-deficient mdx mice. Clin. Sci. (Lond.). 95:83-89.
    • (1998) Clin. Sci. (Lond.) , vol.95 , pp. 83-89
    • McArdle, A.1    Helliwell, T.R.2    Beckett, G.J.3    Catapano, M.4    Davis, A.5
  • 30
    • 0035342456 scopus 로고    scopus 로고
    • Identification of new repeating motifs in titin
    • Greaser, M. 2001. Identification of new repeating motifs in titin. Proteins. 43:145-149.
    • (2001) Proteins , vol.43 , pp. 145-149
    • Greaser, M.1
  • 31
    • 0345686607 scopus 로고    scopus 로고
    • Calcium-dependent molecular spring elements in the giant protein titin
    • Labeit, D., K. Watanabe, C. Witt, H. Fujita, Y. Wu, et al. 2003. Calcium-dependent molecular spring elements in the giant protein titin. Proc. Natl. Acad. Sci. USA. 100:13716-13721.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13716-13721
    • Labeit, D.1    Watanabe, K.2    Witt, C.3    Fujita, H.4    Wu, Y.5
  • 33
    • 0037192845 scopus 로고    scopus 로고
    • Molecular mechanics of cardiac titin's PEVK and N2B spring elements
    • Watanabe, K., P. Nair, D. Labeit, M. S. Kellermayer, M. Greaser, et al. 2002. Molecular mechanics of cardiac titin's PEVK and N2B spring elements. J. Biol. Chem. 277:11549-11558.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11549-11558
    • Watanabe, K.1    Nair, P.2    Labeit, D.3    Kellermayer, M.S.4    Greaser, M.5
  • 34
    • 1842830381 scopus 로고    scopus 로고
    • Developmentally regulated switching of titin size alters myofibrillar stiffness in the perinatal heart
    • Opitz, C. A., M. C. Leake, I. Makarenko, V. Benes, and W. A. Linke. 2004. Developmentally regulated switching of titin size alters myofibrillar stiffness in the perinatal heart. Circ. Res. 94:967-975.
    • (2004) Circ. Res. , vol.94 , pp. 967-975
    • Opitz, C.A.1    Leake, M.C.2    Makarenko, I.3    Benes, V.4    Linke, W.A.5
  • 35
    • 34548221216 scopus 로고    scopus 로고
    • The serum triiodothyronine to thyroxine (T3/T4) ratio in various thyroid disorders and after Levothyroxine replacement therapy
    • Mortoglou, A., and H. Candiloros. 2004. The serum triiodothyronine to thyroxine (T3/T4) ratio in various thyroid disorders and after Levothyroxine replacement therapy. Hormones (Athens). 3:120-126.
    • (2004) Hormones (Athens) , vol.3 , pp. 120-126
    • Mortoglou, A.1    Candiloros, H.2
  • 36
    • 30944459664 scopus 로고    scopus 로고
    • Low thyroid function leads to cardiac atrophy with chamber dilatation, impaired myocardial blood flow, loss of arterioles, and severe systolic dysfunction
    • Tang, Y. D., J. A. Kuzman, S. Said, B. E. Anderson, X. Wang, et al. 2005. Low thyroid function leads to cardiac atrophy with chamber dilatation, impaired myocardial blood flow, loss of arterioles, and severe systolic dysfunction. Circulation. 112:3122-3130.
    • (2005) Circulation , vol.112 , pp. 3122-3130
    • Tang, Y.D.1    Kuzman, J.A.2    Said, S.3    Anderson, B.E.4    Wang, X.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.