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Gene Review

PLN  -  phospholamban

Sus scrofa

 
 
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Disease relevance of PLN

 

High impact information on PLN

 

Chemical compound and disease context of PLN

 

Biological context of PLN

 

Anatomical context of PLN

 

Associations of PLN with chemical compounds

 

Other interactions of PLN

  • Phospholamban, a regulator of the SERCA2 Ca2(+)-transport ATPase in cardiac/slow-twitch skeletal/smooth muscle, could not be detected in Purkinje neurons [19].
  • We tested the hypothesis that activation of protein kinase C (PKC) isoforms in pressure-overload heart failure was prevented by angiotensin-converting enzyme (ACE) inhibition, resulting in normalization of cardiac sarcoplasmic reticulum (SR) Ca2+ ATPase (SERCA) 2a and phospholamban protein levels and improvement in intracellular Ca2+ handling [20].
  • Regional alterations in SR Ca(2+)-ATPase, phospholamban, and HSP-70 expression in chronic hibernating myocardium [21].
 

Analytical, diagnostic and therapeutic context of PLN

References

  1. Differential changes in cardiac phospholamban and sarcoplasmic reticular Ca(2+)-ATPase protein levels. Effects on Ca2+ transport and mechanics in compensated pressure-overload hypertrophy and congestive heart failure. Kiss, E., Ball, N.A., Kranias, E.G., Walsh, R.A. Circ. Res. (1995) [Pubmed]
  2. Increased activity of the sarcoplasmic reticular calcium pump in porcine stunned myocardium. Lamers, J.M., Duncker, D.J., Bezstarosti, K., McFalls, E.O., Sassen, L.M., Verdouw, P.D. Cardiovasc. Res. (1993) [Pubmed]
  3. Calcium transport and phospholamban in sarcoplasmic reticulum of ischemic myocardium. Schoutsen, B., Blom, J.J., Verdouw, P.D., Lamers, J.M. J. Mol. Cell. Cardiol. (1989) [Pubmed]
  4. Effects of adenosine receptor and muscarinic cholinergic receptor agonists on cardiac protein phosphorylation. Influence of pertussis toxin. Neumann, J., Bokník, P., Bodor, G.S., Jones, L.R., Schmitz, W., Scholz, H. J. Pharmacol. Exp. Ther. (1994) [Pubmed]
  5. Purification of porcine phospholamban expressed in Escherichia coli. Yao, Q., Bevan, J.L., Weaver, R.F., Bigelow, D.J. Protein Expr. Purif. (1996) [Pubmed]
  6. Effects of Levosimendan, a cardiotonic agent targeted to troponin C, on cardiac function and on phosphorylation and Ca2+ sensitivity of cardiac myofibrils and sarcoplasmic reticulum in guinea pig heart. Edes, I., Kiss, E., Kitada, Y., Powers, F.M., Papp, J.G., Kranias, E.G., Solaro, R.J. Circ. Res. (1995) [Pubmed]
  7. A1-adenosine receptor-mediated inhibition of isoproterenol-stimulated protein phosphorylation in ventricular myocytes. Evidence against a cAMP-dependent effect. Gupta, R.C., Neumann, J., Durant, P., Watanabe, A.M. Circ. Res. (1993) [Pubmed]
  8. Elevated levels of endogenous adenosine alter metabolism and enhance reduction in contractile function during low-flow ischemia: associated changes in expression of Ca(2+)-ATPase and phospholamban. Sommerschild, H.T., Lunde, P.K., Deindl, E., Jynge, P., Ilebekk, A., Kirkebøen, K.A. J. Mol. Cell. Cardiol. (1999) [Pubmed]
  9. Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to beta-adrenergic stimulation. Wegener, A.D., Simmerman, H.K., Lindemann, J.P., Jones, L.R. J. Biol. Chem. (1989) [Pubmed]
  10. Site-specific derivatives of wheat germ calmodulin. Interactions with troponin and sarcoplasmic reticulum. Strasburg, G.M., Hogan, M., Birmachu, W., Thomas, D.D., Louis, C.F. J. Biol. Chem. (1988) [Pubmed]
  11. Phospholamban remains associated with the Ca2+- and Mg2+-dependent ATPase following phosphorylation by cAMP-dependent protein kinase. Negash, S., Yao, Q., Sun, H., Li, J., Bigelow, D.J., Squier, T.C. Biochem. J. (2000) [Pubmed]
  12. In vitro cyclic AMP induced phosphorylation of phospholamban: an early marker of long-term recovery of function following reperfusion of ischaemic myocardium? van der Giessen, W.J., Verdouw, P.D., ten Cate, F.J., Essed, C.E., Rijsterborgh, H., Lamers, J.M. Cardiovasc. Res. (1988) [Pubmed]
  13. Upregulated and downregulated transcription of myocardial genes after pulmonary artery banding in pigs. Bauer, E.P., Kuki, S., Zimmermann, R., Schaper, W. Ann. Thorac. Surg. (1998) [Pubmed]
  14. Structure and dynamics of phospholamban in solution and in membrane bilayer: computer simulations. Houndonougbo, Y., Kuczera, K., Jas, G.S. Biochemistry (2005) [Pubmed]
  15. cDNA cloning and sequencing of phospholamban from pig stomach smooth muscle. Verboomen, H., Wuytack, F., Eggermont, J.A., De Jaegere, S., Missiaen, L., Raeymaekers, L., Casteels, R. Biochem. J. (1989) [Pubmed]
  16. Phospholamban and troponin I are substrates for protein kinase C in vitro but not in intact beating guinea pig hearts. Edes, I., Kranias, E.G. Circ. Res. (1990) [Pubmed]
  17. Inotropic responses to isoproterenol and phosphodiesterase inhibitors in intact guinea pig hearts: comparison of cyclic AMP levels and phosphorylation of sarcoplasmic reticulum and myofibrillar proteins. Rapundalo, S.T., Solaro, R.J., Kranias, E.G. Circ. Res. (1989) [Pubmed]
  18. Changes in phosphoinositide turnover in isolated guinea pig hearts stimulated with isoproterenol. Edes, I., Solaro, R.J., Kranias, E.G. Circ. Res. (1989) [Pubmed]
  19. A study of the organellar Ca2(+)-transport ATPase isozymes in pig cerebellar Purkinje neurons. Plessers, L., Eggermont, J.A., Wuytack, F., Casteels, R. J. Neurosci. (1991) [Pubmed]
  20. Effect of angiotensin-converting enzyme inhibition on protein kinase C and SR proteins in heart failure. Takeishi, Y., Bhagwat, A., Ball, N.A., Kirkpatrick, D.L., Periasamy, M., Walsh, R.A. Am. J. Physiol. (1999) [Pubmed]
  21. Regional alterations in SR Ca(2+)-ATPase, phospholamban, and HSP-70 expression in chronic hibernating myocardium. Fallavollita, J.A., Jacob, S., Young, R.F., Canty, J.M. Am. J. Physiol. (1999) [Pubmed]
  22. Expression of endoplasmic-reticulum Ca2(+)-pump isoforms and of phospholamban in pig smooth-muscle tissues. Eggermont, J.A., Wuytack, F., Verbist, J., Casteels, R. Biochem. J. (1990) [Pubmed]
  23. Enhanced gene expression of calcium regulatory proteins in stunned porcine myocardium. Frass, O., Sharma, H.S., Knöll, R., Duncker, D.J., McFalls, E.O., Verdouw, P.D., Schaper, W. Cardiovasc. Res. (1993) [Pubmed]
 
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