Sarcomeric Protein Mutations in Dilated Cardiomyopathy

Heart Failure Reviews - Tập 10 Số 3 - Trang 225-235 - 2005
Audrey N. Chang1, James D. Potter2
1Department of Molecular and Cellular Pharmacology, Miller School of Medicine, University of Miami, Miami
2Department of Molecular and Cellular Pharmacology, Miller School of Medicine, University of Miami, Miami, Florida 33136

Tóm tắt

Từ khóa


Tài liệu tham khảo

Richardson P, et al., Report of the 1995 world health organization/international society and federation of cardiology task force on the definition and classification of cardiomyopathies. Circulation 1996;93(5):841–842.

Kamisago M, et al., Mutations in sarcomere protein genes as a cause of dilated cardiomyopathy. N Engl J Med 2000;343(23):1688–1696.

Mestroni L, et al., Familial dilated cardiomyopathy: Evidence for genetic and phenotypic heterogeneity. Heart Muscle Disease Study Group. J Am Coll Cardiol 1999;34(1):181–190.

Harada K, Potter JD. Familial hypertrophic cardiomyopathy mutations from different functional regions of troponin T result in different effects on the pH and Ca2+ sensitivity of cardiac muscle contraction. J Biol Chem 2004;279(15):14488–14495.

Knollmann BC, et al., Inotropic stimulation induces cardiac dysfunction in transgenic mice expressing a troponin T (I79N) mutation linked to familial hypertrophic cardiomyopathy. J Biol Chem 2001;276(13):10039–10048.

Szczesna D, et al., Altered regulation of cardiac muscle contraction by troponin T mutations that cause familial hypertrophic cardiomyopathy. J Biol Chem 2000;275(1):624–630.

Venkatraman G, et al., Characterization of troponin T dilated cardiomyopathy mutations in the fetal troponin isoform. J Biol Chem, 2004.

Venkatraman G, et al., Different functional properties of troponin T mutants that cause dilated cardiomyopathy. J Biol Chem 2003;278(43):41670–41676.

Daehmlow S, et al., Novel mutations in sarcomeric protein genes in dilated cardiomyopathy. Biochem Biophys Res Commun 2002;298(1):116–120.

Nanni L, et al., Hypertrophic cardiomyopathy: Two homozygous cases with “typical” hypertrophic cardiomyopathy and three new mutations in cases with progression to dilated cardiomyopathy. Biochem Biophys Res Commun 2003;309(2):391–398.

Villard E, et al., Mutation screening in dilated cardiomyopathy: Prominent role of the beta myosin heavy chain gene. Eur Heart J 2005;26(8):794–803.

Karkkainen S, et al., Two novel mutations in the beta-myosin heavy chain gene associated with dilated cardiomyopathy. Eur J Heart Fail 2004;6(7):861–868.

Hartzell HC, Sale WS. Structure of C protein purified from cardiac mus cle. J Cell Biol 1985;100(1):208–215.

Swan RC, Fischman DA. Electron microscopy of C-protein molecules from chicken skeletal muscle. J Muscle Res Cell Motil 1986;7(2):160–166.

Gautel M, et al., Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: A modulator of cardiac contraction? Embo J 1995;14(9):1952–1960.

Weisberg A, Winegrad S. Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proc Natl Acad Sci USA, 1996. 93(17):8999–9003.

Harris SP, et al., Hypertrophic cardiomyopathy in cardiac myosin binding protein-C knockout mice. Circ Res 2002;90(5):594–601.

Konno T, et al., A novel missense mutation in the myosin binding protein-C gene is responsible for hypertrophic cardiomyopathy with left ventricular dysfunction and dilation in elderly patients. J Am Coll Cardiol 2003;41(5):781–786.

Shimizu M, et al., Gene mutations in adult Japanese patients with dilated cardiomyopathy. Circ J 2005;69(2):150–153.

Rayment I, et al., Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy. Proc Natl Acad Sci USA, 1995;92(9):3864–3868.

Olson TM, et al., Actin mutations in dilated cardiomyopathy, a heritable form of heart failure. Science 1998;280(5364):750–752.

Geeves MA, Holmes KC. Structural mechanism of muscle contraction. Annu Rev Biochem, 1999;68:687–728.

Olson TM, et al., Mutations that alter the surface charge of alpha-tropomyosin are associated with dilated cardiomyopathy. J Mol Cell Cardiol, 2001;33(4):723–732.

Regitz-Zagrosek V, et al., Novel mutation in the alpha-tropomyosin gene and transition from hypertrophic to hypocontractile dilated cardiomyopathy. Circulation 2000;102(17):E112–E116.

Golitsina N, et al., Effects of two familial hypertrophic cardiomyopathy- causing mutations on alpha-tropomyosin structure and function. Biochemistry 1997;36(15):4637–4642.

Golitsina N, et al., Effects of two familial hypertrophic cardiomyopathy- causing mutations on alpha-tropomyosin structure and function. Biochemistry 1999;38(12):3850.

Prabhakar R, et al., A familial hypertrophic cardiomyopathy alpha-tropomyosin mutation causes severe cardiac hypertrophy and death in mice. J Mol Cell Cardiol 2001;33(10):1815–1528.

Bing W, et al., Effect of hypertrophic cardiomyopathy mutations in human cardiac muscle alpha -tropomyosin (Asp175Asn and Glu180Gly) on the regulatory properties of human cardiac troponin determined by in vitro motility assay. J Mol Cell Cardiol 2000;32(8):1489–1498.

Wernicke D, et al., alpha-Tropomyosin mutations Asp(175)Asn and Glu(180)Gly affect cardiac function in transgenic rats in different ways. Am J Physiol Regul Integr Comp Physiol 2004;287(3):R685–R695.

Gomes AV, Potter JD. Molecular and cellular aspects of troponin cardiomyopathies. Ann N Y Acad Sci 2004;1015:214–224.

Potter JD, Sheng Z, Pan B, Zhao J. A direct regulatory role for troponin T and a dual role for troponin C in the Ca2+ regulation of muscle contraction. The Journal of Biological Chemistry 1995;270(6):2557–2562.

Zhang R, et al., Cardiac troponin I phosphorylation increases the rate of cardiac muscle relaxation. Circ Res, 1995;76(6):1028–1035.

Zhang R, Zhao J, Potter JD. Phosphorylation of both serine residues in cardiac troponin I is required to decrease the Ca2+ affinity of cardiac troponin C. J Biol Chem 1995;270(51):30773–30780.

Noland TA, Jr., et al., Cardiac troponin I mutants. Phosphorylation by protein kinases C and A and regulation of Ca(2+)-stimulated MgATPase of reconstituted actomyosin S-1. J Biol Chem 1995;270(43):25445–25454.

Noland TA, Jr, et al., Differential regulation of cardiac actomyosin S-1 MgATPase by protein kinase C isozyme-specific phosphorylation of specific sites in cardiac troponin I and its phosphorylation site mutants. Biochemistry 1996;35(47):14923–14931.

Noland TA, Jr, Raynor RL, Kuo JF. Identification of sites phosphorylated in bovine cardiac troponin I and troponin T by protein kinase C and comparative substrate activity of synthetic peptides containing the phosphorylation sites. J Biol Chem 1989;264(34):20778–20785.

Bowling N, et al., Increased protein kinase C activity and expression of Ca2+-sensitive isoforms in the failing human heart. Circulation 1999;99(3):384–391.

Sumandea MP, et al., Molecular and integrated biology of thin filament protein phosphorylation in heart muscle. Ann N Y Acad Sci 2004;1015:39–52.

Noguchi T, et al., Thin-filament-based modulation of contractile performance in human heart failure. Circulation 2004;110(8):982–987.

Gomes AV, Harada K, Potter JD. A mutation in the N-terminus of Troponin I that is associated with hypertrophic cardiomyopathy affects the Ca2+ sensitivity, phosphorylation kinetics and proteolytic susceptibility of troponin. Journal of Molecular and Cellular Cardiology, 2005, in press.

Bodor GS, et al., Troponin I phosphorylation in the normal and failing adult human heart. Circulation, 1997;96(5):1495–1500.

Wattanapermpool J, Guo X, Solaro RJ. The unique amino-terminal peptide of cardiac troponin I regulates myofibrillar activity only when it is phosphorylated. J Mol Cell Cardiol 1995;27(7):1383–1391.

Fujino N, et al., Cardiac troponin T Arg92Trp mutation and progression from hypertrophic to dilated cardiomyopathy. Clin Cardiol 2001;24(5):397–402.

Fujino N, et al., A novel mutation Lys273Glu in the cardiac troponin T gene shows high degree of penetrance and transition from hypertrophic to dilated cardiomyopathy. Am J Cardiol 2002;89(1):29–33.

Mogensen J, et al., Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy. J Am Coll Cardiol 2004;44(10):2033–2040.

Li D, et al., Novel cardiac troponin T mutation as a cause of familial dilated cardiomyopathy. Circulation 2001;104(18):2188–2193.

Stefanelli CB, et al., Novel troponin T mutation in familial dilated cardiomyopathy with gender-dependant severity. Mol Genet Metab 2004;83(1/2):188–196.

Morimoto S, Lu QW, Harada K, Takahashi-Yanaga F, Minakami R, Ohta M, Sasaguri T, Ohtsuki I. Ca2+-desensitizing effect of a deletion mutation deltaK210 in cardiac troponin T that causes familial dilated cardiomyopathy. PNAS 2002;99(2):913–918.

Murphy RT, et al., Novel mutation in cardiac troponin I in recessive idiopath ic dilated cardiomyopathy. Lancet 2004;363(9406):371–372.

Gregorio CC, et al., The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity. J Cell Biol 1998;143(4):1013–1027.

Sorimachi H, et al., Tissue-specific expression and alpha-actinin binding properties of the Z-disc titin: Implications for the nature of vertebrate Z-discs. J Mol Biol 1997;270(5):688–695.

Makarenko I, et al., Passive stiffness changes caused by upregulation of compliant titin isoforms in human dilated cardiomyopathy hearts. Circ Res 2004;95(7):708–716.

Zou P, et al., Solution scattering suggests cross-linking function of telethon in in the complex with titin. J Biol Chem 2003;278(4):2636–2644.

Itoh-Satoh M, et al., Titin mutations as the molecular basis for dilated cardiomyopathy. Biochem Biophys Res Commun 2002;291(2):385–393.

Granzier H, Labeit S. Cardiac titin: An adjustable multi-functional spring . J Physiol 2002;541(Pt 2):335–342.

Arber S, et al., MLP-deficient mice exhibit a disruption of cardiac cytoarchitectural organization, dilated cardiomyopathy, and heart failure. Cell 1997;88(3):393–403.

Knoll R, et al., The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell 2002;111(7):943–955.

Mohapatra B, et al., Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis. Mol Genet Metab 2003;80(1/2):207–215.

Hayashi T, et al., Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy. J Am Coll Cardiol, 2004;44(11):2192–2201.

Frey N, Richardson JA, Olson EN. Calsarcins, a novel family of sarcomeric calcineurin-binding proteins. Proc Natl Acad Sci USA, 2000;97(26):14632–14637.

Milner DJ, et al., Disruption of muscle architecture and myocardial degenerat ion in mice lacking desmin. J Cell Biol 1996;134(5):1255–1270.

Olson TM, et al., Metavinculin mutations alter actin interaction in dilated cardiomyopathy. Circulation 2002;105(4):431–437.

Epstein ND, Davis JS. Sensing stretch is fundamental. Cell 2003;112(2):147–150.

Wang W, et al., Intracellular action of matrix metall- oproteinase-2 accounts for acute myocardial ischemia and reperfusion injury. Circulation 2002;106(12):1543–1549.

Sariahmetogly M, Skrzypiec M, Leon H, Sawicka J, Holmes C, Berthiamume GS, Sawicki G, Schulz R. Phosphorylation status of matrix metalloproteinase-2 and potential role in myocardial ischemia-reperfusion injury. Circulation 2004;110(17):III–267.

Li YY, et al., Downregulation of matrix metalloproteinases and reduction in collagen damage in the failing human heart after support with left ventricular assist devices. Circulation 2001;104(10):1147–1152.

Spinale FG, et al., A matrix metalloproteinase induction/activation system exists in the human left ventricular myocardium and is upregulated in heart failure. Circulation 2000;102(16):1944–1949.

Gerull B, et al., Mutations of TTN, encoding the giant muscle filament titin, cause familial dilated cardiomyopathy. Nat Genet 2002;30(2):201–204.