Regulation of phospholipase C in cardiac hypertrophy

Bibliography

• Opie LH: The Heart: Physiology, from Cell to Circulation. Lippincott-Raven, NY, USA (1998)
   Google Scholar
• Hefti MA, Harder BA, Eppenberger HM, Schaub MC: Signaling pathways in cardiac myocyte hypertrophy. J. Mol. Cell. Cardiol. 29(11), 2873–2892 (1997).
   Google Scholar
• Comprehensive review identifying the many different pathways, and their crosslinks, that are activated in response to different stimuli during the cardiomyocyte hypertrophic response.
   Google Scholar
• Jaffre F, Callebert J, Sarre A et al.: Involvement of the serotonin 5-HT2B receptor in cardiac hypertrophy linked to sympathetic stimulation: control of interleukin-6, interleukin-1², and tumor necrosis factor-± cytokine production by ventricular fibroblasts. Circulation 110(8), 969–974 (2004)
   Google Scholar
• Nishikawa K, Yoshida M, Kusuhara M et al.: Left ventricular hypertrophy in mice with a cardiac-specific overexpression of interleukin-1. Am. J. Physiol. Heart Circ. Physiol. 291(1), H176–H183 (2006)
   Google Scholar
• Schmidt BM, Schmieder RE: Cardiotrophin: its importance as a pathogenetic factor and as a measure of left ventricular hypertrophy. J. Hypertens. 23(12), 2151–2153 (2005)
   Google Scholar
• Ponten A, Li X, Thoren P et al.: Transgenic overexpression of platelet-derived growth factor-C in the mouse heart induces cardiac fibrosis, hypertrophy, and dilated cardiomyopathy. Am. J. Pathol. 163(2), 673–682 (2003)
   Google Scholar
• Cheng TH, Shih NL, Chen CH et al.: Role of mitogen-activated protein kinase pathway in reactive oxygen speciesmediated endothelin-1-induced ²-myosin heavy chain gene expression and cardiomyocyte hypertrophy. J. Biomed. Sci. 12(1), 123–133 (2005)
   Google Scholar
• Schnabel P, Mies F, Nohr T, Geisler M, Bohm M: Differential regulation of phospholipase C-² isozymes in cardiomyocyte hypertrophy. Biochem. Biophys. Res. Commun. 275(1), 1–6 (2000).
   Google Scholar
• First evidence of a reciprocal regulation of c-fos and PLC ²
   Google Scholar
• gene expression in neonatal rat cardiomyocytes in response to norephinephrine (NE).
   Google Scholar
• Ganguly PK, Lee SL, Beamish RE, Dhalla NS: Altered sympathetic and adrenoceptors during the development of cardiac hypertrophy. Am. Heart J. 118(3), 520–525 (1989)
   Google Scholar
• Ruzicka M, Leenen FH: Relevance of blockade of cardiac and circulatory angiotensin-converting enzyme for the prevention of volume overload-induced cardiac hypertrophy. Circulation 91(1), 16–19 (1995)
   Google Scholar
• Lear W, Ruzicka M, Leenen FH: ACE inhibitors and cardiac ACE mRNA in volume overload-induced cardiac hypertrophy. Am. J. Physiol. 273(2 Pt 2), H641–H646 (1997)
   Google Scholar
• Zhao W, Ahokas RA, Weber KT, Sun Y: ANG-II-induced cardiac molecular and cellular events: role of aldosterone. Am. J. Physiol. 291(1), H336-H343 (2006)
   Google Scholar
• Jesmin S, Zaedi S, Maeda S et al.: Endothelin antagonism suppresses plasma and cardiac endothelin-1 levels in SHRSPs at the typical hypertensive stage. Exp. Biol. Med. 231(6), 919–924 (2006)
   Google Scholar
• Cernacek P, Stewart DJ, Monge JC, Rouleau JL: The endothelin system and its role in acute myocardial infarction. Can. J. Physiol. Pharmacol. 81(6), 598–606 (2003)
   Google Scholar
• Chien KR, Knowlton KU, Zhu H, Chien S: Regulation of cardiac gene expression during myocardial growth and hypertrophy: molecular studies of an adaptive physiologic response. FASEB J. 5(15), 3037–3046 (1991)
   Google Scholar
• Lamers JM, De Jonge HW, Panagia V, van Heugten HA: Receptor-mediated signalling pathways acting through hydrolysis of membrane phospholipids in cardiomyocytes. Cardioscience 4(3), 121–131 (1993)
   Google Scholar
• Post SR, Hammond HK, Insel PA: ²-adrenergic receptors and receptor signaling in heart failure. Annu. Rev. Pharmacol. Toxicol. 39, 343–360 (1999)
   Google Scholar
• Izumo S, Aoki H: Calcineurin – the missing link in cardiac hypertrophy. Nat. Med. 4(6), 661–662 (1998)
   Google Scholar
• Tappia PS, Singal T, Dent MR, Asemu G, Mangat R, Dhalla NS: Phospholipidmediated signaling in diseased myocardium. Future Lipidol. 1, 701–717 (2006)
   Google Scholar
• Tappia PS, Dent MR, Dhalla NS: Oxidative stress and redox regulation of phospholipase D in myocardial disease. Free Radic. Biol. Med. 41, 349–361 (2006)
   Google Scholar
• Tappia PS: Phospholipid-mediated signaling systems as novel targets for treatment of heart disease. Can. J. Physiol. Pharmacol. 85, 25–41 (2007)
   Google Scholar
• Rhee SG: Regulation of phosphoinositidespecific phospholipase C. Annu. Rev. Biochem. 70, 281–312 (2001).
   Google Scholar
• Comprehensive review identifying the mechanisms involved in the regulation of the phosphoinositide-specific PLC isozymes in different cell types.
   Google Scholar
• Singal T, Dhalla NS, Tappia PS: Phospholipase C may be involved in norepinephrine-induced cardiac hypertrophy. Biochem. Biophys. Res. Commun. 320(3), 1015–1019 (2004)
   Google Scholar
• Singal T, Dhalla NS, Tappia PS: Norepinephrine-induced changes in gene expression of phospholipase C in cardiomyocytes. J. Mol. Cell. Cardiol. 41(1), 126–137 (2006).
   Google Scholar
• First evidence showing that PLC activities regulate their own isozyme gene expression in adult rat cardiomyocytes in response to NE, which might represent a cycle of events that perpetuates or amplifies the hypertrophic response to NE.
   Google Scholar
• Tappia PS, Padua RR, Panagia V, Kardami E: Fibroblast growth factor-2 stimulates phospholipase C ² in adult cardiomyocytes. Biochem. Cell Biol. 77(6), 569–575 (1999)
   Google Scholar
• Guo Y, Rebecchi M, Scariata S: Phospholipase C ²2 binds to and inhibits phospholipase C δ1, 280(2), 1438–1447 (2005)
   Google Scholar
• Fukami K: Structure, regulation, and function of phospholipase C isozymes. J. Biochem. 131(3), 293–299 (2002)
   Google Scholar
• James SR, Downes CP: Structural and mechanistic features of phospholipases C: effectors of inositol phospholipid-mediated signal transduction. Cell. Signal. (5), 329–236 (1997)
   Google Scholar
• Lopez I, Mak EC, Ding J, Hamm HE, Lomasney JW: A novel bifunctional phospholipase C that is regulated by G±12 and stimulates the Ras/mitogen-activated protein kinase pathway. J. Biol. Chem. 276(4), 2758–2765 (2001)
   Google Scholar
• Heredia Mdel P, Delgado C, Pereira L et al.: Neuropeptide Y rapidly enhances [Ca2+]i transients and Ca2+ sparks in adult rat ventricular myocytes through Y1 receptor and PLC activation. J. Mol. Cell. Cardiol. 38(1), 205–212 (2005)
   Google Scholar
• Balogh J, Wihlborg AK, Isackson H et al.: Phospholipase C and cAMP-dependent positive inotropic effects of ATP in mouse cardiomyocytes via P2Y11-like receptors. J. Mol. Cell. Cardiol. 39(2), 223–230 (2005)
   Google Scholar
• Yin G, Yan C, Berk BC: Angiotensin II signaling pathways mediated by tyrosine kinases. Int. J. Biochem. Cell Biol. 35(6), 780–783 (2003)
   Google Scholar
• Kockskämper J, Zima AV, Roderick HL, Pieske B, Blatter LA, Bootman MD: Emerging roles of inositiol 1,4,5-trisphosphate signaling in cardiac myocytes. J. Mol. Cell. Cardiol. 45(2), 128–147 (2008).
   Google Scholar
• Comprehensive review providing information on the possible functional roles of inositiol 1,4,5-trisphosphate (IP3) in the heart.
   Google Scholar
• Vasilevski O, Grubb DR, Filtz TM et al.: Ins(1,4,5)P3 regulates phospholipase C ²1 expression in cardiomyocytes. J. Mol. Cell. Cardiol. 45(5), 679–684 (2008).
   Google Scholar
• Demonstrates that PLC-derived IP3 can regulate the expression of PLC ²1 in neonatal rat cardiomycytes and provides new evidence for a functional role for IP3, and adding novel evidence for the involvement of PLC activities in the regulation of own isozyme gene expression.
   Google Scholar
• Wu X, Zhang T, Bossuyt J et al.: Local InsP3-dependent perinuclear Ca2+ signaling in cardic myocyte excitation-transcription coupling. J. Clin. Invest. 116(3), 675–682 (2006)
   Google Scholar
• Bers DM: Cardiac excitation–contraction coupling. Nature 415, 198–205 (2002)
   Google Scholar
• Mackenzie L, Bootman MD, Laine M et al.: The role of inositol 1,4,5-trisphosphate receptors in Ca2+ signaling and the generation of arrhythmias in rat atrial myocytes. J. Physiol. 555, 395–409 (2004)
   Google Scholar
• Zima AV, Blatter LA: Inositol 1,4,5-trisphosphate-dependent Ca2+ signaling in cat atrial excitation– contarction coupling and arrhythmias. J. Physiol. 555, 607–615 (2004)
   Google Scholar
• Newton AC, Johnson JE: Protein kinase C: a paradigm for regulation of protein function by two membrane-targeting modules. Biochim. Biophys. Acta 1376(2), 155–172 (1998)
   Google Scholar
• Malhotra A, Kang BP, Opawumi D, Belizaire W, Meggs LG: Molecular biology of protein kinase C signaling in cardiac myocytes. Mol. Cell. Biochem. 225(1), 97–107 (2001)
   Google Scholar
• Kamp TJ, Hell JW: Regulation of cardiac l-type calcium channels by protein kinase A and protein kinase C. Circ. Res. 87(12), 1095–1102 (2000)
   Google Scholar
• Churchill E, Budas G, Vallentin A, Koyanagi T, Mochly-Rosen D: PKC isozymes in chronic cardiac disease: possible therapeutic targets? Annu. Rev. Pharmacol. Toxicol. 48, 569–599 (2008).
   Google Scholar
• Focuses on the roles of specific PKC isozymes in atherosclerosis, fibrosis and cardiac hypertrophy, and examines the principles of pharmacology as they pertain to regulators of signaling cascades associated with these conditions.
   Google Scholar
• Dorn GW 2nd, Force T: Protein kinase cascades in the regulation of cardiac hypertrophy. J. Clin. Invest. 115, 527–537 (2005).
   Google Scholar
• Review of the developments in the area of PKC-mediated signal transduction and highlighting the utility of animal models that are helping to identify molecular targets of cardiac hypertrophy.
   Google Scholar
• Sabri A, Steinberg SF: Protein kinase C isoform-selective signals that lead to cardiac hypertrophy and the progression of heart failure. Mol. Cell. Biochem. 251, 97–101 (2003)
   Google Scholar
• Rebecchi MJ, Pentyala SN: Structure, function, and control of phosphoinositidespecific phospholipase C. Physiol. Rev. 80(4), 1291–1335 (2000)
   Google Scholar
• Song C, Hu CD, Masago M et al.: Regulation of a novel human phospholipase C, PLC5, through membrane targeting by Ras. J. Biol. Chem. 276(4), 2752–2757 (2001)
   Google Scholar
• Saunders CM, Larman MG, Parrington J et al.: PLC ζ: a sperm-specific trigger of Ca2+ oscillations in eggs and embryo development. Development 129(15), 3533–3544 (2002)
   Google Scholar
• Wing MR, Bourdon DM, Harden TK: PLC-5: a shared effector protein in Ras-, Rho-, and G±²³-mediated signaling. Mol. Interv. 3(5), 273–280 (2003)
   Google Scholar
• Hwang JI, Oh YS, Shin KJ, Kim H, Ryu SH, Suh PG: Molecular cloning and characterization of a novel phospholipase C, PLC-·. Biochem. J. 389(Pt 1), 181–186 (2005)
   Google Scholar
• Tappia PS, Liu S-Y, Shatadal S, Takeda N, Dhalla NS, Panagia V: Changes in sarcolemmal PLC isoenzymes in postinfarct congestive heart failure: partial correction by imidapril. Am. J. Physiol. 277(1 Pt 2), H40–H49 (1999)
   Google Scholar
• Wolf RA: Association of phospholipase C-´ with a highly enriched preparation of canine sarcolemma. Am. J. Physiol. 263(5 Pt 1), C1021–C1028 (1992).
   Google Scholar
• First study to show that PLC ´
   Google Scholar
• the predominant PLC isozyme associated with the cardiac sarcolemma membrane.
   Google Scholar
• Wang H, Oestreich EA, Maekawa N et al.: Phospholipase C 5 modulates ²-adrenergic receptor-dependent cardiac contraction and inhibits cardiac hypertrophy. Circ. Res. 97(12), 1305–1313 (2005).
   Google Scholar
• Knockout model implicating PLC 5
   Google Scholar
• cardiac hypertrophy.
   Google Scholar
• Asemu G, Dhalla NS, Tappia PS: Inhibition of PLC improves postischemic recovery in isolated rat heart. Am. J. Physiol. 287, H2598-H2605 (2004)
   Google Scholar
• Kawaguchi H, Sano H, Iizuka K et al.: Phosphatidylinositol metabolism in hypertrophic rat heart. Circ. Res. 72(5), 966–972 (1993)
   Google Scholar
• Shoki M, Kawaguchi H, Okamoto H et al.: Phosphatidylinositol and inositolphosphatide metabolism in hypertrophied rat heart. Jpn Circ. J. 56(2), 142–147 (1992)
   Google Scholar
• Sakata Y: Tissue factors contributing to cardiac hypertrophy in cardiomyopathic hamsters (BIO14.6): involvement of transforming growth factor-² 1 and tissue renin–angiotensin system in the progression of cardiac hypertrophy. Hokkaido. Igaku. Zasshi. 68(1), 18–28 (1993)
   Google Scholar
• Dent MR, Dhalla NS, Tappia PS: Phospholipase C gene expression, protein content and activities in cardiac hypertrophy and heart failure due to volume overload. Am. J. Physiol. 282, H719–H727 (2004)
   Google Scholar
• Dent MR, Aroutiounova N, Dhalla NS, Tappia PS: Losartan attenuates phospholipase C isozyme gene expression in hypertrophied hearts due to volume overload. J. Cell. Mol. Med. 10, 470–479 (2006)
   Google Scholar
• Katan M: Families of phosphoinositidespecific phospholipase C: structure and function. Biochim. Biophys. Acta. 1436(1–2), 5–17 (1998)
   Google Scholar
• Jalili T, Takeishi Y, Song G, Ball NA, Howles G, Walsh RA: PKC translocation without changes in G±q and PLC-² protein abundance in cardiac hypertrophy and failure. Am. J. Physiol. 277, H2298–H2304 (1999)
   Google Scholar
• Giles TD, Sander GE, Thomas MG, Quiroz AC: ±-adrenergic mechanisms in the pathophysiology of left ventricular heart failure – an ana lysis of their role in systolic and diastolic dysfunction. J. Mol. Cell. Cardiol. 18, 33–43 (1986)
   Google Scholar
• Prasad K, O’Neil CL, Bharadwaj B: Effect of prolonged prazosin treatment on hemodynamic and biochemical changes in the dog heart due to chronic pressure overload. Jpn. Heart J. 25, 461–476 (1984)
   Google Scholar
• Motz W, Klepzig M, Strauer BE: Regression of cardiac hypertrophy: experimental and clinical results. J. Cardiovasc. Pharmacol. 10, S148–S152 (1987)
   Google Scholar
• Zakynthinos E, Pierrutsakos CH, Daniil Z, Papadogiannis D: Losartan controlled blood pressure and reduced left ventricular hypertrophy but did not alter arrhythmias in hypertensive men with preserved systolic function. Angiology 56, 439–449 (2005)
   Google Scholar
• Kanno Y, Kaneko K, Kaneko M et al.: Angiotensin receptor antagonist regresses left ventricular hypertrophy associated with diabetic nephropathy in dialysis patients. J. Cardiovasc. Pharmacol. 43, 380–386 (2004)
   Google Scholar
• Ruzicka M, Yuan B, Leenen FH: Effects of enalapril versus losartan on regression of volume overload-induced cardiac hypertrophy in rats. Circulation 90, 484–491 (1994)
   Google Scholar
• Rothermund L, Vetter R, Dieterich M et al.: Endothelin-A receptor blockade prevents left ventricular hypertrophy and dysfunction in salt-sensitive experimental hypertension. Circulation 106, 2305–2308 (2002)
   Google Scholar
• Yamamoto K, Masuyama T, Sakata Y, Nishikawa N, Mano T, Hori M: Prevention of diastolic heart failure by endothelin type A receptor antagonist through inhibition of ventricular structural remodeling in hypertensive heart. J. Hypertens. 20, 753–761 (2002)
   Google Scholar
• Lund AK, Goens MB, Nunez BA, Walker MK: Characterizing the role of endothelin-1 in the progression of cardiac hypertrophy in aryl hydrocardbon receptor (AhR) null mice. Toxicol. Appl. Pharmacol. 212, 127–135 (2006)
   Google Scholar
• Bai H, Wu LL, Xing DQ, Liu J, Zhao YL: Angiotensin II induced upregulation of G±q/11, phospholipase C ²3 and extracellular signal-regulated kinase 1/2 via angiotensin II type 1 receptor. Chin. Med. J. 117, 88–93 (2004)
   Google Scholar
• Lamers JM, Eskildsen-Helmond YE, Resink AM et al.: Endothelin-1-induced phospho- lipase C-² and D and protein kinase C isoenzyme in signaling leading to hypertrophy in rat cardiomyocytes. J. Cardiovasc. Pharmacol. 26(Suppl. 3), S100–S103 (1995)
   Google Scholar
• Nagata S: Apoptosis by death factor. Cell 88, 355–365 (1997)
   Google Scholar
• Badorff C, Ruetten H, Mueller S et al.: Fas receptor signaling inhibits glycogen synthase kinase 3² and induces cardiac hypertrophy following pressure overload. J. Clin. Invest. 109, 373–381 (2002).
   Google Scholar
• Identifies Fas-receptor activation, a classical death signal causing apoptosis via activation of the caspase cascade, as a novel pathway mediating cardiomyocyte hypertrophy in vitro and in vivo.
   Google Scholar
• Barac YD, Zeevi-Levin N, Yaniv G et al.: The 1,4,5-inositol trisphosphate pathway is a key component in Fas-mediated hypertrophy in neonatal rat ventricular myocytes. Cardiovasc. Res. 68, 75–86 (2005)
   Google Scholar
• Ruwhof C, van Wamel JT, Noordzij LA, Aydin S, Harper JC, van der Laarse A: Mechanical stress stimulates phospholipase C activity and intracellular calcium ion levels in neonatal cardiomyocytes. Cell Calcium 29, 73–83 (2001)
   Google Scholar
• D’Angelo DD, Sakata Y, Lorenz JN et al.: Transgenic G±q overexpression induces cardiac contractile failure in mice. Proc. Natl Acad. Sci. USA 94, 8121–8126 (1997).
   Google Scholar
• First study to construct transgenic mice that overexpressed wild-type G±
   Google Scholar
• in the heart. It was demonstrated that G±
   Google Scholar
• overexpression results in a biochemical and physiologic phenotype resembling both the compensated and decompensated phases of human cardiac hypertrophy.
   Google Scholar
• Sakata Y, Hoit BD, Liggett SB, Walsh RA, Dorn GW 2nd: Decompensation of pressure-overload hypertrophy in G±q-overexpressing mice. Circulation 97, 1488–1495 (1998)
   Google Scholar
• Adams JW, Sakata Y, Davis MG et al.: Enhanced G±q signaling: a common pathway mediates cardiac hypertrophy and apoptotic heart failure. Proc. Natl Acad. Sci. USA 95(17), 10140–10145 (1998).
   Google Scholar
• These authors suggest a mechanism in which moderate levels of Gq signaling stimulate cardiac hypertrophy whereas high-level Gq activation results in cardiomyocyte apoptosis. The identification of a single biochemical stimulus regulating cardiomyocyte growth and death provides a potential mechanism for the progression of compensated hypertrophy to decompensated heart failure.
   Google Scholar
• Sussman MA, Welch S, Walker A et al.: Altered focal adhesion regulation correlates with cardiomyopathy in mice expressing constitutively active rac1. J. Clin. Invest. 105, 875–886 (2000)
   Google Scholar
• Paradis P, Dali-Youcef N, Paradis FW, Thibault G, Nemer M: Overexpression of angiotensin II type I receptor in cardiomyocytes induces cardiac hypertrophy and remodeling. Proc. Natl Acad. Sci. USA 97, 931–936 (2000)
   Google Scholar
• Mende U, Kagen A, Cohen A, Aramburu J, Schoen FJ, Neer EJ: Transient cardiac expression of constitutively active G±q leads to hypertrophy and dilated cardiomyopathy by calcineurin-dependent and independent pathways. Proc. Natl. Acad. Sci. USA 95(23), 13893–13898 (1998)
   Google Scholar
• Mende U, Kagen A, Meister M, Neer EJ: Signal transduction in atria and ventricles of mice with transient cardiac expression of activated G protein ±q. Circ. Res. 85(11), 1085–1091 (1999)
   Google Scholar
• Mende U, Semsarian C, Martins DC et al.: Dilated cardiomyopathy in two transgenic mouse lines expressing activated G protein ±q: lack of correlation between phospholipase C activation and the phenotype. J. Mol. Cell. Cardiol. 33, 1477–1491 (2001).
   Google Scholar
• Independent line in the same genetic background (±q*44h) with lower expression of HA ±q* protein that ultimately results in dilated cardiomyopathy, but with no correlation between PLC activation and development of dilated cardiomyopathy in response to HA ±q* expression, suggesting a role for additional pathways and/or mechanisms.
   Google Scholar
• Hollinger S, Hepler JR: Cellular regulation of RGS proteins: modulators and integrators of G protein signaling. Pharmacol. Rev. 54(3), 527–559 (2002)
   Google Scholar
• Anger T, Zhang W, Mende U: Differential contribution of GTPase activation and effector antagonism to the inhibitory effect of RGS proteins on Gq-mediated signaling in vivo. J. Biol. Chem. 279(6), 3906–3915 (2004)
   Google Scholar
• Zhang W, Anger T, Su J et al.: Selective loss of fine tuning of Gq/11 signaling by RGS2 protein exacerbates cardiomyocyte hypertrophy. J. Biol. Chem. 281(9), 5811–5820 (2006)
   Google Scholar
• Lin F, Owens WA, Chen S et al.: Targeted ±1B-adrenergic receptor overexpression induces enhanced cardiac contractility but not hypertrophy. Circ. Res. 89(4), 343–350 (2001)
   Google Scholar
• Milano CA, Dolber PC, Rockman HA et al.: Myocardial expression of a constitutively active ±1²-adrenergic receptor in transgenic mice induces cardiac hypertrophy. Proc. Natl Acad. Sci. USA 91, 10109–10113 (1994)
   Google Scholar
• Heemskerk JWM, Farndale RW, Sage SO: Effects of U73122 and U73343 on human platelet calcium signalling and protein tyrosine phosphorylation. Biochim. Biophys. Acta 1355, 81–88 (1997)
   Google Scholar
• Jin W, Lo TM, Loh HH, Thayer SA: U73122 inhibits phospholipase C-dependent calcium mobilization in neuronal cells. Brain Res. 642, 237–243 (1994)
   Google Scholar
• Mogami H, Mills CL, Gallagher DV: Phospholipase C inhibitor, U73122, releases intracellular Ca2+, potentiates Ins(1,4,5)P-3-mediated Ca2+ release and directly activates in channels in mouse pancreatic acinar cells. Biochem. J. 324, 645–651 (1997)
   Google Scholar
• Muto Y, Nagao T, Urushidani T: The putative phospholipase C inhibitor U73122 and its negative control, U73343, elicit unexpected effects on the rabbit parietal cell. J. Pharmacol. Exp. Therap. 282, 1379–1388 (1997)
   Google Scholar
• Berven LA, Barritt GJ: Evidence obtained using single hepatocytes for inhibition by the phospholipase C inhibitor U73122 of store-operated Ca2+ inflow. Biochem. Pharmacol. 49, 1373–1379 (1995)
   Google Scholar
• Arthur JF, Matkovich SJ, Mitchell CJ, Biden TJ, Woodcock EA: Evidence for selective coupling of ±1-adrenergic receptors to phospholipase C-²1 in rat neonatal cardiomyocytes. J. Biol. Chem. 276, 37341–37346 (2001)
   Google Scholar
• Grubb DR, Vasilevski O, Huynh H, Woodcock EA: The extreme C-terminal region of phospholipase C ²1 determines subcellular localization and function; the ‘²’ splice variant mediates ±1-adrenergic receptor responses in cardiomyocytes. FASEB J. 22(8), 2768–2774 (2008).
   Google Scholar
• First study to show that the extreme C-terminal sequences of the PLC ²1 splice variants determine localization and function. PLC ²1a is localized in the cytoplasm, whereas PLC ²1b targets to the sarcolemma and is enriched in caveole. It was also demonstrated that responses initiated by ± 1-adrenoceptor (±1-AR) activation involves only PLC ²1b.
   Google Scholar
• Morris JB, Huynh H, Vasilevski O, Woodcock EA: ±1-adrenergic receptor signaling is localized to caveolae in neonatal rat cardiomyocytes. J. Mol. Cell. Cardiol. 41, 17–125 (2006).
   Google Scholar
• Examined the possibility that sarcolemmal phosphatidylinositol 4,5, bisphosphate (PIP2) exists in different pools and that only one of these provides the substrate for ±1-adrenergic receptor (AR) activated PLC. It was revealed that PIP2 in cardiomyocyte sarcolemma is compartmentalized and that ±1-AR signaling is localized to caveole.
   Google Scholar
• Barka T, van der Noen H, Shaw PA: Proto-oncogene fos (c-fos) expression in the heart. Oncogene 1, 439–443 (1987)
   Google Scholar
• Hannan RD, West AK: Adrenergic agents, but not triiodo-l-thyronine induce c-fos and c-myc expression in the rat heart. Basic Res. Cardiol. 86, 154–164 (1991)
   Google Scholar
• Iwaki K, Sukhatme VP, Shubeita HE, Chien KR: ±- and ²-adrenergic stimulation induces distinct patterns of immediate early gene expression in neonatal rat myocardial cells. fos/jun expression is associated with sarcomere assembly; Egr-1 induction is primarily an ±1-mediated response. J. Biol. Chem. 265, 13809–13817 (1990)
   Google Scholar
• Komuro I, Kaida T, Shibazaki Y et al.: Stretching cardiac myocytes stimulates protooncogene expression. J. Biol. Chem. 265, 3595–3598 (1990)
   Google Scholar
• Sadoshima J, Qiu Z, Morgan JP, Izumo S: Tyrosine kinase activation is an immediate and essential step in hypotonic cell swelling-induced ERK activation and c-fos gene expression in cardiac myocytes. EMBO J. 15(20), 5535–5546 (1996)
   Google Scholar
• Chiu R, Boyle WJ, Meek J, Smeal T, Hunter T, Karin M: The c-Fos protein interacts with c-Jun/AP-1 to stimulate transcription of AP-1 responsive genes. Cell 54, 541–552 (1988)
   Google Scholar
• Lijnen P, Petrov V: Antagonism of the rennin–angiotensin system, hypertrophy and gene expression in cardiac myocytes. Methods Find Exp. Clin. Pharmacol. 21(5), 363–374 (1999), 104 Omura T, Yoshiyama M, Yoshida K et al.: Dominant negative mutant of c-Jun inhibits cardiomyocyte hypertrophy induced by endothelin 1 and phenylephrine. Hypertension 39(1), 81–86 (2002)
   Google Scholar
• Dhalla NS, Xu Y-J, Sheu S-S, Tappia PS, Panagia V: Phosphatidic acid: a potential signal transducer for cardiac hypertrophy. J. Mol. Cell. Cardiol. 29, 2865–2871 (1997).
   Google Scholar
• Comprehensive review identifying the hypertrophic signal-transducing pathways that are activated in response to phosphatidic acid.
   Google Scholar
• Small K, Feng JF, Lorenz J et al.: Cardiac specific overexpression of transglutaminase II (Gh) results in a unique hypertrophy phenotype independent of phospholipase C activation. J. Biol. Chem. 23, 21291–21296 (1999).
   Google Scholar
• Demonstrates that overexpression of Gh (TGII) results in hypertrophy independent of activation of PLC. Evidence for TGII acting as a G-protein-like transducer of receptor signaling to PLC in the heart is not supported by these studies.
   Google Scholar
• Eskildsen-Helmond YE, Bezstarosti K, Dekkers DH, van Heugten HA, Lamers JM: Cross-talk between receptor-mediated phospholipase C-² and D via protein kinase C as intracellular signal possibly leading to hypertrophy in serum-free cultured cardiomyocytes. J. Mol. Cell. Cardiol. 29, 2545–2559 (1997)
   Google Scholar
• Peivandi AA, Huhn A, Lehr HA et al.: Upregulation of phospholipase D expression and activation in ventricular pressureoverload hypertrophy. J. Pharmacol. Sci. 98, 244–254 (2005)
   Google Scholar
• Tappia PS, Yu CH, Di Nardo P, Pasricha AK, Dhalla NS, Panagia V: Depressed responsiveness of phospholipase C isoenzymes to phosphatidic acid in congestive heart failure. J. Mol. Cell. Cardiol. 33, 431–440 (2001)
   Google Scholar
• Henry RA, Boyce SY, Kurz T, Wolf RA: Stimulation and binding of myocardial phospholipase C by phosphatidic acid. Am. J. Physiol. 269, C349–C358 (1995).
   Google Scholar
• First study to show that phosphatidic acid can bind onto and stimulate specific PLC isozymes in the heart and identifies a novel regulatory mechanism of PLC activities.
   Google Scholar
• Tappia PS, Maddaford TG, Hurtado C, Panagia V, Pierce GN: Depressed phosphatidic acid-induced contractile activity of failing cardiomyocytes. Biochem. Biophys. Res. Commun. 300, 457–463 (2003)
   Google Scholar
• Pagano RE, Longmiur KJ: Phosphorylation, transbilayer movement and facilitated intracellular transport of diacylglycerol are involved in the uptake of a fluorescent analogue of phosphatidic acid by cultured fibroblasts. J. Biol. Chem. 260, 1909–1916 (1995)
   Google Scholar
• Murthy SN, Chung PH, Lin L, Lomasney JW: Activation of phospholipase C5 by free fatty acids and cross talk with phospholipase D and phospholipase A2. Biochemistry 45, 10987–10997 (2006)
   Google Scholar
• Liu SY, Tappia PS, Dai J, Williams SA, Panagia V: Phospholipase A2-mediated activation of phospholipase D in rat heart sarcolemma. J. Mol. Cell. Cardiol. 30, 1203–1214 (1998)
   Google Scholar
• Strauer BE, Bayer F, Brecht HM, Motz W: The influence of sympathetic nervous activity on regression of cardiac hypertrophy. J. Hypertens. 3, S39–S44 (1985)
   Google Scholar
• Prasad K, O’Neil CL, Bharadwaj B: Effect of prolonged prazosin treatment on hemodynamic and biochemical changes in the dog heart due to chronic pressure overload. Jpn Heart J. 25, 461–476 (1984)
   Google Scholar
• Strauer BE: Progression and regression of heart hypertrophy in arterial hypertension: pathophysiology and clinical aspects. Z. Kardiol. 74, 171–178 (1995)
   Google Scholar
• Strauer BE: Regression of myocardial and coronary vascular hypertrophy in hypertensive heart disease. J. Cardiovasc. Pharmacol. 12, S45–S54 (1988).
   Google Scholar