Atrial Chamber-specific Expression of Sarcolipin Is Regulated during Development and Hypertrophic Remodeling

Minamisawa, Susumu; Wang, Yibin; Chen, Ju; Ishikawa, Yoshihiro; Chien, Kenneth R.; Matsuoka, Rumiko

doi:10.1074/jbc.m213132200

Cited by 107 publications

(136 citation statements)

References 24 publications

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“…On the other hand, SLN levels are predominant in the atria than the ventricle [14][15][16]25]. PLB is also expressed at low levels in slow-twitch skeletal muscles [27,28].…”

Section: Sln and Plb Are Differentially Expressed During Development mentioning

confidence: 99%

“…The expression of SERCA2a [3], PLB [29][30][31], and SLN mRNA [25] increase several fold during heart development, displaying coordinate regulation and indicates the increase in SR function during heart development. Thyroid hormone levels have been shown to modulate SR function by altering the expression of SERCA and its regulators.…”

Section: Sln and Plb Are Differentially Expressed During Development mentioning

confidence: 99%

“…Similarly, the expression of SLN is also altered under a variety of pathological conditions. SLN mRNA is down-regulated in atrial myocardium of patients with chronic atrial fibrillation [39] and hypertrophic remodeling of atria [25]. A recent study also showed that SLN mRNA was up-regulated ~50 fold in the hypertrophied ventricles of Nkx2-5 null mice [40].…”

Section: Sln and Plb Are Differentially Expressed During Development mentioning

confidence: 99%

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Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase

Bhupathy¹,

Babu²,

Periasamy³

2007

Journal of Molecular and Cellular Cardiology

119

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The cardiac sarcoplasmic reticulum calcium ATPase (SERCA2a) plays a critical role in maintaining the intracellular calcium homeostasis during cardiac contraction and relaxation. It has been well documented over the years that altered expression and activity of SERCA2a can lead to systolic and diastolic dysfunction. The activity of SERCA2a is regulated by two structurally similar proteins, phospholamban (PLB) and sarcolipin (SLN). Although, the relevance of PLB has been extensively studied over the years, the role SLN in cardiac physiology is an emerging field of study. This review focuses on the advances in the understanding of the regulation of SERCA2a by SLN and PLB. In particular, it highlights the similarities and differences between the two proteins and their roles in cardiac patho-physiology.

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“…On the other hand, SLN levels are predominant in the atria than the ventricle [14][15][16]25]. PLB is also expressed at low levels in slow-twitch skeletal muscles [27,28].…”

Section: Sln and Plb Are Differentially Expressed During Development mentioning

confidence: 99%

Section: Sln and Plb Are Differentially Expressed During Development mentioning

confidence: 99%

Section: Sln and Plb Are Differentially Expressed During Development mentioning

confidence: 99%

See 1 more Smart Citation

Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase

Bhupathy¹,

Babu²,

Periasamy³

2007

Journal of Molecular and Cellular Cardiology

119

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“…Our goals in this study were twofold: to determine whether NF-SLN and PLN fit into the same regulatory site in SERCA1a and to understand the structural basis for the superinhibition that results from coexpression of NF-SLN and PLN with SERCA1a or SERCA2a (8). This superinhibition is of potential physiological significance, because SLN and PLN are coexpressed in the heart (4,13,28).…”

Section: Models For the Interaction Of Sln With Serca1a In The Presenmentioning

confidence: 99%

Sarcolipin regulates sarco(endo)plasmic reticulum Ca ²⁺ -ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban

Asahi

Sugita

Kurzydlowski

et al. 2003

Proc. Natl. Acad. Sci. U.S.A.

143

151

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S arco(endo)plasmic reticulum Ca 2ϩ -ATPases (SERCAs) are 110-kDa membrane proteins that catalyze the ATPdependent transport of Ca 2ϩ from the cytosol to the lumen of the sarco(endo)plasmic reticulum (1). SERCAs expressed in muscle are regulated by two members of a gene family: phospholamban (PLN) (2, 3) and sarcolipin (SLN) (4-6).PLN is a 52-aa membrane protein that interacts with SERCA molecules to lower their apparent affinity for Ca 2ϩ and inhibit their activity at low, but not at high, Ca 2ϩ concentrations (2, 7). SLN is a 31-aa membrane protein that resembles PLN in these essential inhibitory features (5, 8). The two proteins have similar transmembrane sequences (4, 9) but differ at their C termini, where PLN ends with the sequence Met-Leu-Leu-52 (10), whereas SLN ends with the more hydrophilic sequence, ArgSer-Tyr-Gln-Tyr-31. They also differ at their N termini: phosphorylation of PLN in a well conserved 30-aa cytosolic domain disrupts inhibitory interactions, accounting, in part, for the inotropic response of the heart to adrenergic stimulation (2, 7). The poorly conserved cytosolic sequence of SLN is 7 aa long and is not phosphorylated under normal conditions. A number of physiological studies have demonstrated that PLN is a key regulator of the kinetics of cardiac muscle function (11,12). PLN expression is largely restricted to cardiac, slow-twitch, and smooth muscle, whereas SLN is highly expressed in fasttwitch and, to a lesser extent, in cardiac muscle (4, 13). Nevertheless, both PLN and SLN can inhibit both SERCA1a and SERCA2a with similar characteristics (14). Although PLN exists in both pentameric and monomeric forms, it is generally accepted that the monomer is the inhibitory species (15, 16). When NF-SLN and PLN are coexpressed with SERCA, superinhibition of SERCA activity is observed (5, 8).Sites of interaction between SERCA and PLN have been identified in both cytosolic and transmembrane domains of SERCA and PLN by using cross-linking and mutagenesis (15,(17)(18)(19)(20)(21)(22). Modeling from high-resolution crystal and NMR structures has identified additional amino acids that interact between PLN domain Ia and the cytosolic domains of SERCA1a and between PLN domains Ib and II and transmembrane helices M2, M4, M6, and M9 in SERCA1a (10,23).In this study, we investigated interaction sites between NF-SLN and SERCA1a, showing that they overlap in important ways with the transmembrane sites of PLN͞SERC1a interaction. We also investigated sites involved in the superinhibition that results when PLN and SLN are coexpressed with SERCA1a or SERCA2a (8). Structural models were developed for the binary SLN͞SERCA1a and ternary PLN͞SLN͞SERCA1a complexes. Materials and MethodsMaterials. Enzymes for DNA manipulation were obtained from New England Biolabs and Pharmacia. G-Sepharose and a chemiluminescence kit for measurement of coimmunoprecipitation of interacting proteins were purchased from Pierce. FLAG antibody, M2, was purchased from Sigma; the anti-PLN antibody, 1D11, was a gift from Robert Johnson (Me...

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“…The expression of mouse sarcolipin mRNA, however, was most abundant in the atria and was undetectable in the ventricles, indicating an atrial chamber-specific expression pattern in the heart (Minamisawa et al, 2003b). Atrial chamber-specific expression of sarcolipin mRNA was increased during development and was down-regulated in the atria of hypertrophic heart.…”

Section: Introductionmentioning

confidence: 92%

Calcium cycling proteins in heart failure, cardiomyopathy and arrhythmias

Minamisawa

Sato²,

Cho³

2004

Exp Mol Med

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A bstractA grow in g b ody o f evidence, includ ing stud ies using genetically engineered m ouse m odels, has show n that C a 2+ cycling and C a 2+ -dependent sign alin g p ath w ays p lay a p ivo tal ro le in card iac hypertrophy and heart failure. In addition, recent stu d ies id en tified th at m u tatio n s o f th e g en es encodin g sarco plasm ic reticu lum (S R ) p rotein s cau se h um an card iom yopathies an d leth al ventricu lar arrhyth m ias. The reg ulatio n of C a 2+ hom eostasis via the SR proteins m ay have potential therapeutic value for heart diseases such as cardiom yopathy, heart failure and arrhythm ias.

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Atrial Chamber-specific Expression of Sarcolipin Is Regulated during Development and Hypertrophic Remodeling

Cited by 107 publications

References 24 publications

Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase

Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase

Sarcolipin regulates sarco(endo)plasmic reticulum Ca ²⁺ -ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban

Calcium cycling proteins in heart failure, cardiomyopathy and arrhythmias

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Atrial Chamber-specific Expression of Sarcolipin Is Regulated during Development and Hypertrophic Remodeling

Cited by 107 publications

References 24 publications

Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase

Sarcolipin and phospholamban as regulators of cardiac sarcoplasmic reticulum Ca2+ ATPase

Sarcolipin regulates sarco(endo)plasmic reticulum Ca 2+ -ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban

Calcium cycling proteins in heart failure, cardiomyopathy and arrhythmias

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Sarcolipin regulates sarco(endo)plasmic reticulum Ca ²⁺ -ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban