© 1996 American Heart Association, Inc.
Articles |
Phospholamban: A Prominent Regulator of Myocardial Contractility
the Department of Pharmacology & Cell Biophysics, University of Cincinnati (Ohio) College of Medicine.
Correspondence to Dr Evangelia G. Kranias, Department of Pharmacology & Cell Biophysics, University of Cincinnati College of Medicine, 231 Bethesda Ave, Cincinnati, OH 45267-0576.
Key Words: phospholamban • sarcoplasmic reticulum • cardiac contractility
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Regulation of Cardiac Sarcoplasmic Reticulum Ca2+ Uptake by Phospholamban |
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 Top Regulation of Cardiac... Structural Characteristics of...Regulation of Basal Myocardial...The Role of Phospholamban...Regulation of Phospholamban...SummaryReferences |
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In the early 1970s, a discovery was reported by Arnold Katz (Tada et al1 ), who demonstrated that phosphorylation of isolated cardiac sarcoplasmic reticulum membranes occurred mainly on a low molecular weight protein. This phosphoprotein was named phospholamban, from the Greek root words meaning "to receive phosphate."1 Phospholamban is a small protein, comprising 52 amino acid residues, and it is present in cardiac, smooth, and slow-twitch skeletal muscles. However, its regulatory effects have been mainly studied in cardiac muscle. In vitro studies indicated that phospholamban can be phosphorylated at three distinct sites by various protein kinases: serine 10, by protein kinase C; serine 16, by cAMP- or cGMP-dependent protein kinase; and threonine 17, by Ca2+-calmodulin–dependent protein kinase.2 3 Each phosphorylation is associated with stimulation of the initial rates of cardiac sarcoplasmic reticulum Ca2+ uptake, which is mainly pronounced at low [Ca2+], resulting in an overall increase in the affinity of the Ca2+ pump for Ca2+.4 5 On the basis of these observations, it was initially hypothesized that phosphorylated phospholamban functions as a stimulator of the cardiac sarcoplasmic reticulum Ca2+-ATPase (SERCA2) enzyme. However, in the late 1980s, a significant breakthrough occurred demonstrating that dephosphorylated phospholamban is actually an inhibitor of cardiac sarcoplasmic reticulum Ca2+ transport for Ca2+ and that phosphorylation relieves this inhibitory effect, giving the appearance of phosphorylation-induced stimulation.6 This finding, together with the identification of a cardiac sarcoplasmic reticulum–associated protein phosphatase that can dephosphorylate phospholamban,7 has led to our current understanding of phospholamban as a reversible inhibitor of the cardiac sarcoplasmic reticulum Ca2+ ATPase activity.
Phospholamban is also phosphorylated in situ during ß-adrenergic stimulation. Studies in intact beating hearts or isolated cardiac myocytes have shown that both serine 16 and threonine 17 in phospholamban become phosphorylated during isoproterenol stimulation.8 9 Phosphorylation of phospholamban and the accompanied increases in the cardiac sarcoplasmic reticulum Ca2+ uptake rates were suggested to be at least partially responsible for the stimulatory effects of ß-agonists in the mammalian heart.
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Structural Characteristics of Phospholamban |
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TopRegulation of Cardiac...Structural Characteristics of...Regulation of Basal Myocardial...The Role of Phospholamban...Regulation of Phospholamban...SummaryReferences |
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The structure of phospholamban is not presently known, but based on its amino acid sequence, several models have been proposed. It is generally accepted that there are two major domains: a hydrophilic domain (AA 1-30, indicating amino acid residues 1 to 30), which contains the three phosphorylation sites, and a hydrophobic domain (AA 31-52), which is anchored into the cardiac sarcoplasmic reticulum membrane. Part of the hydrophilic domain has been suggested to be in a helical configuration, and phosphorylation of phospholamban may unwind or disrupt this structural configuration.10 Evidence from several laboratories indicated the importance of the hydrophilic domain in mediating the regulatory effects of phospholamban on the cardiac sarcoplasmic reticulum Ca2+ pump.6 11 12 13 Actually, AA 2-18 in phospholamban have been suggested to interact with AA 336-412 and 467-762 in SERCA2 for functional modification.14
The hydrophobic domain of phospholamban has also been proposed to have a helical structure. There is presently no clear evidence that this domain interacts with the cardiac sarcoplasmic reticulum Ca2+ pump, although several studies have suggested that the hydrophobic portion of phospholamban is also important in mediating the regulatory effects.12 15 Cysteine residues in the 
-helical transmembrane domain provide for noncovalent interaction between monomeric forms and contribute to stabilization of a pentameric structure for phospholamban.16 Analysis of phospholamban pentamers indicated that pentamer formation was that of a left-handed coiled-coil helical bundle, with a cylindrical ion pore.17 Recent evidence demonstrated that a leucine zipper stabilizes the phospholamban pentameric association and forms a central ion pore,18 which may allow for Ca2+-selective ion transfer.19 However, it is not presently clear whether pentameric assembly is essential for functional regulation of the cardiac sarcoplasmic reticulum Ca2+ ATPase. Expression studies in cell free systems have indicated that the monomeric and pentameric forms of phospholamban are equally effective in mediating the regulatory effects on the Ca2+ pump.14
Another theory on phospholamban–Ca2+-ATPase interaction proposed a dimeric association of the Ca2+ pump proteins around a phospholamban pentamer.20 This model, based on time-resolved phosphorescence anisotropy, described a preferential interaction between the Ca2+-free pump and dephosphorylated phospholamban. Phospholamban phosphorylation destabilized the interaction and resulted in increased rotational mobility of the Ca2+-ATPase in the cardiac sarcoplasmic reticulum membrane.20
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Regulation of Basal Myocardial Contractility by Phospholamban |
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TopRegulation of Cardiac...Structural Characteristics of...Regulation of Basal Myocardial...The Role of Phospholamban...Regulation of Phospholamban...SummaryReferences |
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The role of phospholamban in the regulation of basal myocardial contractility has been recently elucidated through the development of a phospholamban-deficient mouse.21 These mice, created using gene-targeting methodology in murine embryonic stem cells, displayed hyperdynamic cardiac function, including increased systolic function, increased rates of left ventricular relaxation,21 and enhanced ventricular filling.22 Phospholamban-deficient hearts not only relaxed faster than wild-type hearts but also exhibited enhanced inotropic parameters, including increased rates of pressure development, which were assessed in work-performing preparations21 and in vivo, using echocardiographic analyses.22 These findings were substantiated by in vitro analyses of isolated ventricular cardiomyocytes from phospholamban-deficient hearts, which also exhibited enhancement of the rates of relengthening, shortening, and Ca2+ kinetics.23 The enhanced contractile parameters reflected subcellular alterations at the cardiac sarcoplasmic reticulum level. The affinity of the Ca2+ pump for Ca2+ was significantly increased, and this was associated with increased intraluminal cardiac sarcoplasmic reticulum Ca2+ content in the phospholamban-deficient hearts compared with wild-type hearts.21
The functional importance of phospholamban in the regulation of cardiac contractility has been further substantiated in studies of phospholamban heterozygous mice, which contain only one phospholamban-targeted allele.24 The hearts of these mice express 40% of the phospholamban levels present in wild-type mouse hearts, and this reduced phospholamban expression is associated with increases in the affinity of the cardiac sarcoplasmic reticulum Ca2+ transport system for Ca2+ and increases in contractile parameters. It is interesting to note that when the levels of phospholamban in the wild-type, phospholamban-heterozygous, and phospholamban-deficient hearts were plotted against the rates of contraction and relaxation for these hearts, there was a close linear correlation observed (Fig 1
), suggesting a prominent role for phospholamban in the regulation of the basal contractile parameters in the mammalian heart. Furthermore, since the levels of the cardiac sarcoplasmic reticulum Ca2+ ATPase were not affected in these genetically altered hearts,25 these data indicate that alterations in phospholamban levels, which may reflect alterations in the relative stoichiometry of phospholamban to the cardiac sarcoplasmic reticulum Ca2+ ATPase, are associated with parallel alterations in cardiac contractile parameters. However, the functional stoichiometry of phospholamban to the cardiac sarcoplasmic reticulum Ca2+ ATPase is not presently known. In vitro studies have reported values varying between 1:5 and 5:1 for phospholamban/SERCA2. In vivo studies using transgenic mice, which overexpress phospholamban specifically in the heart, suggested that the "functional stoichiometry" of phospholamban/SERCA2 is less than 1:1 in native cardiac sarcoplasmic reticulum membranes.26 The phospholamban protein levels in the hearts from these transgenic mice were twofold higher compared with wild-type hearts, and the increased phospholamban expression resulted in increased inhibition of the Ca2+-ATPase affinity for Ca2+, without any effects on the Vmax of this enzyme.26 Furthermore, when the relative levels of phospholamban to the cardiac sarcoplasmic reticulum Ca2+ ATPase were plotted against the EC50 values of the Ca2+-ATPase for Ca2+ in phospholamban overexpression, wild-type, phospholamban-heterozygous, and phospholamban-deficient hearts, there was a close linear correlation observed (Fig 2), indicating that the overexpressed phospholamban in the transgenic hearts was functionally coupled to the Ca2+-ATPase. The decreased affinity of the Ca2+-ATPase for Ca2+ in the phospholamban overexpression hearts was associated with decreases in the contractile parameters and depression of the Ca2+ transients in isolated cardiac myocytes compared with myocytes from wild-type hearts.26 Echocardiographic analyses of hearts from these transgenic mice demonstrated significantly suppressed fractional shortening and circumferential shortening compared with hearts from wild-type mice.26 Taken together, these studies in genetically altered mice indicate that phospholamban is a potent repressor of both contraction and relaxation parameters in the mammalian heart.
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) or the time to half-relaxation of developed pressure (RT50, 
) are given for PLB-knockout (KO), PLB-heterozygous (HET), and wild-type (WT) hearts. The close linear correlation between the PLB/Ca2+-ATPase ratio and the time parameters of contraction and relaxation are depicted by regression lines.
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The Role of Phospholamban in Myocardial ß-Adrenergic Responsiveness |
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TopRegulation of Cardiac...Structural Characteristics of...Regulation of Basal Myocardial...The Role of Phospholamban...Regulation of Phospholamban...SummaryReferences |
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Studies in isolated beating hearts and cardiac myocytes have demonstrated that catecholamine administration results in phosphorylation of phospholamban in cardiac sarcoplasmic reticulum, phospholemman in sarcolemmal membranes, and troponin I and C protein in myofibrils. However, the rates of phosphorylation/dephosphorylation reactions on phospholamban appear to be faster than those of the other phosphoproteins, and phospholamban has been suggested to be a prominent mediator of the ß-adrenergic responses in the mammalian heart. Phosphorylation of phospholamban, in response to increases in cAMP levels during ß-agonist administration, is accompanied by increases in the activity of the cardiac sarcoplasmic reticulum Ca2+ transport system and increased rates of cardiac relaxation.27 28 29 The increased rates of Ca2+ uptake lead to increased cardiac sarcoplasmic reticulum Ca2+ sequestration levels, which are available for subsequent contractions, leading to increased contractile force. However, phospholamban is not only phosphorylated by cAMP-dependent protein kinase on serine 16 but also by Ca2+-calmodulin protein kinase on threonine 17,8 9 and the relative contribution of each phosphorylation in the inotropic and lusitropic effects of ß-agonists is not presently known.
The functional role of phospholamban in the ß-adrenergic signaling pathway has been recently elucidated using the phospholamban-deficient mouse. In vitro studies in isolated myocytes and cardiac preparations from these mice indicated significant attenuation of the inotropic and lusitropic effects of isoproterenol compared with wild-type preparations.21 23 Furthermore, in vivo studies using echocardiographic analyses of phospholamban-ablated hearts demonstrated that the ß-adrenergic stimulatory effects were also attenuated in the intact animal.22 Thus, although phospholamban is not the only protein involved in the transduction of cardiac ß-adrenergic signaling, the experimental evidence to date indicates that it is a major one. The function of phospholamban during catecholamine stimulation of the heart suggests a role for this protein as an internal "brake mechanism," which allows for rapid myocardial reaction, such that when adrenaline is released upon a "fight or flight" situation, the phospholamban "brake" is alleviated, allowing for rapid increases in cardiac contraction and relaxation.
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Regulation of Phospholamban Expression |
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TopRegulation of Cardiac...Structural Characteristics of...Regulation of Basal Myocardial...The Role of Phospholamban...Regulation of Phospholamban...SummaryReferences |
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Phospholamban is the product of a single gene, and it has been cloned from several species including the pig, chicken, mouse, and human. There is >96% homology between coding regions of the phospholamban gene among these species, and there have been no isoforms of phospholamban detected to date.30 The phospholamban gene has been mapped to human chromosome 6.31 Studies in the mouse have demonstrated that with regard to the circulatory system, phospholamban is differentially expressed, ranging from high levels of expression in ventricular muscle, to intermediate levels in atrial and pulmonary myocardial muscles, and to low but functionally significant levels of expression in aortic smooth muscle. Differential levels of phospholamban expression in ventricular and atrial compartments appeared to correlate with differences in the contractile parameters of these muscles.32
Phospholamban expression has also been shown to be regulated during development and aging. Increases in phospholamban expression over the course of cardiac development have been observed in the mouse, chicken, rat, and rabbit.31 32 33 34 Furthermore, decrements in phospholamban phosphorylation in the aging rat heart have been suggested to be associated with diminished contractile responses of these hearts to catecholamine stimulation.33
Myocardial phospholamban expression has also been shown to be regulated by the thyroid status in both the rat and the rabbit.34 35 During hypothyroidism, phospholamban mRNA levels were not changed in rabbit atrium and ventricle, whereas phospholamban protein levels were found to increase in rat hearts. These elevated levels of phospholamban in the rat heart were associated with decreased rates of cardiac sarcoplasmic reticulum Ca2+ uptake, consistent with increased inhibition of the cardiac sarcoplasmic reticulum Ca2+ pump, and decreased contractility.34 Opposite regulatory effects were observed for phospholamban expression during hyperthyroidism.34 35 Hyperthyroidism was associated with decreased levels of phospholamban mRNA in rabbit atria and ventricles and decreased levels of phospholamban protein in rat hearts. The decreases in phospholamban levels were reflected by increased rates of cardiac sarcoplasmic reticulum Ca2+ uptake, consistent with disinhibition of the Ca2+ pump and enhancement of contractile parameters.
Recent investigations of alterations in gene expression, which occur during heart failure, indicated that alterations in the relative ratio of phospholamban to the SR Ca2+ ATPase may be a hallmark of this disease.36 37 38 However, there is some discrepancy within the literature as to how phospholamban expression is altered during myocardial failure. Some studies conducted in failing human hearts have demonstrated reductions in phospholamban mRNA37 or phospholamban protein,36 37 38 whereas other studies observed no apparent alterations in phospholamban levels of failing human hearts.39 40 41 42 Although there continues to be controversy with regard to phospholamban alterations during cardiac failure, it is clear that intracellular alterations, which are associated with repression of cardiac contractility, are suggestive of a role of phospholamban in the etiology of the disease.
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Summary |
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TopRegulation of Cardiac...Structural Characteristics of...Regulation of Basal Myocardial...The Role of Phospholamban...Regulation of Phospholamban...SummaryReferences |
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Our understanding of the role of phospholamban in cardiac physiology has evolved over the past two decades to the point where this protein is now understood to be a critical repressor of myocardial contractility. Phospholamban, through its inhibitory effects on the affinity of the cardiac sarcoplasmic reticulum Ca2+ pump for Ca2+, represses both the rates of relaxation and contraction in the mammalian heart. These inhibitory effects can be relieved through (1) phospholamban phosphorylation, (2) downregulation of phospholamban gene expression, and (3) disruption of the phospholamban–Ca2+-ATPase interaction. Thus, genetic approaches and pharmacological interventions, designed to relieve the phospholamban inhibitory action on the cardiac sarcoplasmic reticulum Ca2+ pump and myocardial relaxation, may prove valuable in reversing the effects of several diseases in the mammalian heart. Such interventions could be designed to inhibit the phospholamban phosphatase, stabilize the phosphorylated state of phospholamban, interrupt the phospholamban-Ca2+-ATPase interaction, decrease phospholamban transcription, or disrupt phospholamban mRNA stability. Development of such therapeutic strategies to target phospholamban will be an important future goal for the clinical improvement of contractility in the failing heart.
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Acknowledgments |
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This study was supported by National Institutes of Health grants HL-26057, HL-52318, HL-22619 (Dr Kranias), and HL-08901 (Dr Koss).
Received July 29, 1996; accepted September 25, 1996.
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References |
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TopRegulation of Cardiac...Structural Characteristics of...Regulation of Basal Myocardial...The Role of Phospholamban...Regulation of Phospholamban...SummaryReferences |
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A. P. Babick, E. J. F. Cantor, J. T. Babick, N. Takeda, N. S. Dhalla, and T. Netticadan Cardiac contractile dysfunction in J2N-k cardiomyopathic hamsters is associated with impaired SR function and regulation Am J Physiol Cell Physiol, November 1, 2004; 287(5): C1202 - C1208. [Abstract] [Full Text] [PDF]
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A. Ahmed Myocardial beta-1 adrenoceptor down-regulation in aging and heart failure: implications for beta-blocker use in older adults with heart failure Eur J Heart Fail, December 1, 2003; 5(6): 709 - 715. [Abstract] [Full Text] [PDF]
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L. S. Maier, T. Zhang, L. Chen, J. DeSantiago, J. H. Brown, and D. M. Bers Transgenic CaMKII{delta}C Overexpression Uniquely Alters Cardiac Myocyte Ca2+ Handling: Reduced SR Ca2+ Load and Activated SR Ca2+ Release Circ. Res., May 2, 2003; 92(8): 904 - 911. [Abstract] [Full Text] [PDF]
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C. Toyoshima, M. Asahi, Y. Sugita, R. Khanna, T. Tsuda, and D. H. MacLennan Inaugural Article: Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase PNAS, January 21, 2003; 100(2): 467 - 472. [Abstract] [Full Text] [PDF]
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R. Shenoy, I. Klein, and K. Ojamaa Differential regulation of SR calcium transporters by thyroid hormone in rat atria and ventricles Am J Physiol Heart Circ Physiol, October 1, 2001; 281(4): H1690 - H1696. [Abstract] [Full Text] [PDF]
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K. Nobe, R. L Sutliff, E. G Kranias, and R. J Paul Phospholamban regulation of bladder contractility: evidence from gene-altered mouse models J. Physiol., September 15, 2001; 535(3): 867 - 878. [Abstract] [Full Text] [PDF]
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G. C. Wellman, L. F. Santana, A. D. Bonev, and M. T. Nelson Role of phospholamban in the modulation of arterial Ca2+ sparks and Ca2+-activated K+ channels by cAMP Am J Physiol Cell Physiol, September 1, 2001; 281(3): C1029 - C1037. [Abstract] [Full Text] [PDF]
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Y. Zhong, S. Ahmed, I. L. Grupp, and M. A. Matlib Altered SR protein expression associated with contractile dysfunction in diabetic rat hearts Am J Physiol Heart Circ Physiol, September 1, 2001; 281(3): H1137 - H1147. [Abstract] [Full Text] [PDF]
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P. Molenaar, S. Bartel, A. Cochrane, D. Vetter, H. Jalali, P. Pohlner, K. Burrell, P. Karczewski, E.-G. Krause, and A. Kaumann Both {beta}2- and {beta}1-Adrenergic Receptors Mediate Hastened Relaxation and Phosphorylation of Phospholamban and Troponin I in Ventricular Myocardium of Fallot Infants, Consistent With Selective Coupling of {beta}2-Adrenergic Receptors to Gs-Protein Circulation, October 10, 2000; 102(15): 1814 - 1821. [Abstract] [Full Text] [PDF]
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I. A. Hobai, J. C. Hancox, and A. J. Levi Inhibition by nickel of the L-type Ca channel in guinea pig ventricular myocytes and effect of internal cAMP Am J Physiol Heart Circ Physiol, August 1, 2000; 279(2): H692 - H701. [Abstract] [Full Text] [PDF]
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M. Asahi, E. McKenna, K. Kurzydlowski, M. Tada, and D. H. MacLennan Physical Interactions between Phospholamban and Sarco(endo)plasmic Reticulum Ca2+-ATPases Are Dissociated by Elevated Ca2+, but Not by Phospholamban Phosphorylation, Vanadate, or Thapsigargin, and Are Enhanced by ATP J. Biol. Chem., May 12, 2000; 275(20): 15034 - 15038. [Abstract] [Full Text] [PDF]
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R. J. Hajjar, F. del Monte, T. Matsui, and A. Rosenzweig Prospects for Gene Therapy for Heart Failure Circ. Res., March 31, 2000; 86(6): 616 - 621. [Abstract] [Full Text] [PDF]
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L. Li, J. Desantiago, G. Chu, E. G. Kranias, and D. M. Bers Phosphorylation of phospholamban and troponin I in beta -adrenergic-induced acceleration of cardiac relaxation Am J Physiol Heart Circ Physiol, March 1, 2000; 278(3): H769 - H779. [Abstract] [Full Text] [PDF]
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C. W. Balke and Y. Wang Distinguishing Mechanisms From Markers of Cardiac Contractile Dysfunction : More Than 1 Way to Skin the Cat of Heart Failure Circulation, February 22, 2000; 101(7): 738 - 739. [Full Text] [PDF]
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M. I. Miyamoto, F. del Monte, U. Schmidt, T. S. DiSalvo, Z. B. Kang, T. Matsui, J. L. Guerrero, J. K. Gwathmey, A. Rosenzweig, and R. J. Hajjar Adenoviral gene transfer of SERCA2a improves left-ventricular function in aortic-banded rats in transition to heart failure PNAS, January 18, 2000; 97(2): 793 - 798. [Abstract] [Full Text] [PDF]
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M.A. McIntosh, S.M. Cobbe, and G.L. Smith Heterogeneous changes in action potential and intracellular Ca2+ in left ventricular myocyte sub-types from rabbits with heart failure Cardiovasc Res, January 14, 2000; 45(2): 397 - 409. [Abstract] [Full Text] [PDF]
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W. F. Bluhm, E. G. Kranias, W. H. Dillmann, and M. Meyer Phospholamban: a major determinant of the cardiac force-frequency relationship Am J Physiol Heart Circ Physiol, January 1, 2000; 278(1): H249 - H255. [Abstract] [Full Text] [PDF]
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R.-P. Xiao, H. Cheng, Y.-Y. Zhou, M. Kuschel, and E. G. Lakatta Recent Advances in Cardiac {beta}2-Adrenergic Signal Transduction Circ. Res., November 26, 1999; 85(11): 1092 - 1100. [Abstract] [Full Text] [PDF]
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M. Asahi, Y. Kimura, K. Kurzydlowski, M. Tada, and D. H. MacLennan Transmembrane Helix M6 in Sarco(endo)plasmic Reticulum Ca2+-ATPase Forms a Functional Interaction Site with Phospholamban. EVIDENCE FOR PHYSICAL INTERACTIONS AT OTHER SITES J. Biol. Chem., November 12, 1999; 274(46): 32855 - 32862. [Abstract] [Full Text] [PDF]
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B. Huang, S. Wang, D. Qin, M. Boutjdir, and N. El-Sherif Diminished Basal Phosphorylation Level of Phospholamban in the Postinfarction Remodeled Rat Ventricle : Role of {beta}-Adrenergic Pathway, Gi Protein, Phosphodiesterase, and Phosphatases Circ. Res., October 29, 1999; 85(9): 848 - 855. [Abstract] [Full Text] [PDF]
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U. Schmidt, R. J. Hajjar, C. S. Kim, D. Lebeche, A. A. Doye, and J. K. Gwathmey Human heart failure: cAMP stimulation of SR Ca2+-ATPase activity and phosphorylation level of phospholamban Am J Physiol Heart Circ Physiol, August 1, 1999; 277(2): H474 - H480. [Abstract] [Full Text] [PDF]
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M. Kuschel, Y.-Y. Zhou, H. Cheng, S.-J. Zhang, Y. Chen, E. G. Lakatta, and R.-P. Xiao Gi Protein-mediated Functional Compartmentalization of Cardiac beta 2-Adrenergic Signaling J. Biol. Chem., July 30, 1999; 274(31): 22048 - 22052. [Abstract] [Full Text] [PDF]
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V. J. Kadambi, N. Ball, E. G. Kranias, R. A. Walsh, and B. D. Hoit Modulation of force-frequency relation by phospholamban in genetically engineered mice Am J Physiol Heart Circ Physiol, June 1, 1999; 276(6): H2245 - H2250. [Abstract] [Full Text] [PDF]
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K. H. Desai, E. Schauble, W. Luo, E. Kranias, and D. Bernstein Phospholamban deficiency does not compromise exercise capacity Am J Physiol Heart Circ Physiol, April 1, 1999; 276(4): H1172 - H1177. [Abstract] [Full Text] [PDF]
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E. Mirit, A. Palmon, Y. Hasin, and M. Horowitz Heat acclimation induces changes in cardiac mechanical performance: the role of thyroid hormone Am J Physiol Regulatory Integrative Comp Physiol, February 1, 1999; 276(2): R550 - R558. [Abstract] [Full Text] [PDF]
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A. Kaumann, S. Bartel, P. Molenaar, L. Sanders, K. Burrell, D. Vetter, P. Hempel, P. Karczewski, and E.-G. Krause Activation of ß2-Adrenergic Receptors Hastens Relaxation and Mediates Phosphorylation of Phospholamban, Troponin I, and C-Protein in Ventricular Myocardium From Patients With Terminal Heart Failure Circulation, January 12, 1999; 99(1): 65 - 72. [Abstract] [Full Text] [PDF]
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