Sarcomeric Protein Mutations in Dilated Cardiomyopathy
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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.
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.