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Expert Review of Proteomics Volume 10, 2013 - Issue 1
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Editorial

Troponin I alterations detected by multiple-reaction monitoring: how might this impact the study of heart failure?

Jonathan A Kirk Department of Medicine, Johns Hopkins University, Baltimore, MD 21218, USA
,
Pingbo Zhang Department of Medicine, Johns Hopkins University, Baltimore, MD 21218, USA
,
Anne M Murphy Department of Pediatrics, Johns Hopkins University, Baltimore, MD 21218, USA
&
Jennifer E Van Eyk Department of Medicine and Biological Chemistry, Johns Hopkins University, Baltimore, MD 21218, USA. [email protected]
Pages 5-8 | Published online: 09 Jan 2014

References

  • Zhang P, Kirk JA, Ji W et al. Multiple reaction monitoring to identify site-specific troponin I phosphorylated residues in the failing human heart. Circulation 126(15), 1828–1837 (2012).
  • Roger VL, Go AS, Lloyd-Jones DM et al.; American Heart Association Statistics Committee and Stroke Statistics Subcommittee. Heart disease and stroke statistics – 2012 update: a report from the American Heart Association. Circulation 125(1), e2–e220 (2012).
  • Stull JT, Brostrom CO, Krebs EG. Phosphorylation of the inhibitor component of troponin by phosphorylase kinase. J. Biol. Chem. 247(16), 5272–5274 (1972).
  • Solaro RJ, Moir AJ, Perry SV. Phosphorylation of troponin I and the inotropic effect of adrenaline in the perfused rabbit heart. Nature 262(5569), 615–617 (1976).
  • Moir AJ, Perry SV. The sites of phosphorylation of rabbit cardiac troponin I by adenosine 3´:5´-cyclic monophosphate-dependent protein kinase. Effect of interaction with troponin C. Biochem. J. 167(2), 333–343 (1977).
  • Kooij V, Saes M, Jaquet K et al. Effect of troponin I Ser23/24 phosphorylation on Ca2+-sensitivity in human myocardium depends on the phosphorylation background. J. Mol. Cell. Cardiol. 48(5), 954–963 (2010).
  • Varian KD, Biesiadecki BJ, Ziolo MT, Davis JP, Janssen PM. Staurosporine inhibits frequency-dependent myofilament desensitization in intact rabbit cardiac trabeculae. Biochem. Res. Int. 2012, 290971 (2012).
  • Charo DN, Ho M, Fajardo G et al. Endogenous regulation of cardiovascular function by apelin-APJ. Am. J. Physiol. Heart Circ. Physiol. 297(5), H1904–H1913 (2009).
  • Kirk JA, MacGowan GA, Evans C et al. Left ventricular and myocardial function in mice expressing constitutively pseudophosphorylated cardiac troponin I. Circ. Res. 105(12), 1232–1239 (2009).
  • Zabrouskov V, Ge Y, Schwartz J, Walker JW. Unraveling molecular complexity of phosphorylated human cardiac troponin I by top down electron capture dissociation/electron transfer dissociation mass spectrometry. Mol. Cell Proteomics 7(10), 1838–1849 (2008).
  • Sakthivel S, Finley NL, Rosevear PR et al. In vivo and in vitro analysis of cardiac troponin I phosphorylation. J. Biol. Chem. 280(1), 703–714 (2005).
  • Arteaga GM, Warren CM, Milutinovic S, Martin AF, Solaro RJ. Specific enhancement of sarcomeric response to Ca2+ protects murine myocardium against ischemia-reperfusion dysfunction. Am. J. Physiol. Heart Circ. Physiol. 289(5), H2183–H2192 (2005).
  • Wolska BM, Arteaga GM, Peña JR et al. Expression of slow skeletal troponin I in hearts of phospholamban knockout mice alters the relaxant effect of beta-adrenergic stimulation. Circ. Res. 90(8), 882–888 (2002).
  • Noland TA, 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. 264(34), 20778–20785 (1989).
  • Wang H, Grant JE, Doede CM, Sadayappan S, Robbins J, Walker JW. PKC-betaII sensitizes cardiac myofilaments to Ca2+ by phosphorylating troponin I on threonine-144. J. Mol. Cell. Cardiol. 41(5), 823–833 (2006).
  • Buscemi N, Foster DB, Neverova I, Van Eyk JE. p21-activated kinase increases the calcium sensitivity of rat triton-skinned cardiac muscle fiber bundles via a mechanism potentially involving novel phosphorylation of troponin I. Circ. Res. 91(6), 509–516 (2002).
  • Oliveira SM, Zhang YH, Solis RS et al. AMP-activated protein kinase phosphorylates cardiac troponin I and alters contractility of murine ventricular myocytes. Circ. Res. 110(9), 1192–1201 (2012).
  • Sheehan KA, Ke Y, Wolska BM, Solaro RJ. Expression of active p21-activated kinase-1 induces Ca2+ flux modification with altered regulatory protein phosphorylation in cardiac myocytes. Am. J. Physiol., Cell Physiol. 296(1), C47–C58 (2009).
  • Januzzi JL Jr, Filippatos G, Nieminen M, Gheorghiade M. Troponin elevation in patients with heart failure: on behalf of the third Universal Definition of Myocardial Infarction Global Task Force: Heart Failure Section. Eur. Heart J. 33(18), 2265–2271 (2012).
  • Mcdonough LR, Van Eyk JE. Prepare to meet your markers: making the most out of troponin I degradation. American Heart Association Monograph on Cardiac Biomarkers. Adams III J, Apple FS, Jaffe AS, Wu AHB (Eds). Furtura Press, NY, USA, 13–22 (2001).

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