نتایج جستجو برای: serca2a

تعداد نتایج: 624  

2017
Xiao Yu Xiao-Dong Zhao Rong-Qi Bao Jia-Yu Yu Guo-Xing Zhang Jing-Wei Chen

BACKGROUND To investigate the effects and involved mechanisms of the modified Yi Qi decoction (MYQ) in cardiac ischemia-reperfusion (IR) induced injury. METHODS Male Sprague-Dawley rats were subjected to a 30-min coronary arterial occlusion followed by reperfusion, low or high dose decoction of MYQ was administrated orally for 1 week or 1 month. RESULTS Both in 1 week and 1 month IR rat gro...

2002
YOSHIHIRO KIMURA MAKOTO INUI

Phospholamban (PLN) reversibly inhibits the Ca -ATPase of cardiac sarcoplasmic reticulum (SERCA2a) through a direct protein-protein interaction, playing a pivotal role in the regulation of intracellular Ca in heart muscle cells. The interaction between PLN and SERCA2a occurs at multiple sites within the cytoplasmic and membrane domains. Here, we have reconstituted the cytoplasmic protein-protei...

Journal: :American journal of physiology. Regulatory, integrative and comparative physiology 2010
Melissa M Thomas Chris Vigna Andrew C Betik A Russell Tupling Russell T Hepple

Aging skeletal muscle shows an increased time to peak force and relaxation and a decreased specific force, all of which could relate to changes in muscle Ca(2+) handling. The purpose of this study was to determine if Ca(2+)-handling protein content and function are decreased in senescent gastrocnemius muscle and if initiating a training program in late middle age (LMA, 29 mo old) could improve ...

Journal: :Circulation. Heart failure 2013
Antoine H Chaanine Ronald E Gordon Erik Kohlbrenner Ludovic Benard Dongtak Jeong Roger J Hajjar

BACKGROUND We have shown that BNIP3 expression is significantly increased in heart failure (HF). In this study, we tested the effects of BNIP3 manipulation in HF. METHODS AND RESULTS In a rat model of pressure overload HF, BNIP3 knockdown significantly decreased left ventricular (LV) volumes with significant improvement in LV diastolic and systolic function. There were significant decreases i...

Journal: :American journal of physiology. Heart and circulatory physiology 2007
Susumu Sakata Djamel Lebeche Naoya Sakata Yuri Sakata Elie R Chemaly Li Fan Liang Yoshiaki Takewa Dongtak Jeong Woo Jin Park Yoshiaki Kawase Roger J Hajjar

The aim of this study was to examine how global cardiac gene transfer of sarcoplasmic reticulum Ca(2+)-ATPase (SERCA2a) can influence left ventricular (LV) mechanical and energetic function, especially in terms of O(2) cost of LV contractility, in normal rats. Normal rats were randomized to receive an adenovirus carrying the SERCA2a (SERCA) or beta-galactosidase (beta-Gal) gene or saline by a c...

Journal: :American journal of physiology. Heart and circulatory physiology 1999
Yong Ji Evgeny Loukianov Tanya Loukianova Larry R Jones Muthu Periasamy

We recently generated a transgenic (TG) mouse model in which the fast-twitch skeletal muscle sarcoplasmic reticulum (SR) Ca2+-ATPase (SERCA1a) is overexpressed in the heart. Ectopic overexpression of SERCA1a results in remodeling of the cardiac SR containing 80% SERCA1a and 20% endogenous SERCA2a with an ∼2.5-fold increase in the total amount of SERCA protein (E. Loukianov et al. Circ. Res. 83:...

Journal: :Circulation 2002
Federica del Monte Sian E Harding G William Dec Judith K Gwathmey Roger J Hajjar

BACKGROUND Myocardial cells from failing human hearts are characterized by abnormal calcium handling, a negative force-frequency relationship, and decreased sarcoplasmic reticulum Ca2+ ATPase (SERCA2a) activity. In this study, we tested whether contractile function can be improved by decreasing the inhibitory effects of phospholamban on SERCA2a with adenoviral gene transfer of antisense phospho...

Journal: :Frontiers in bioscience : a journal and virtual library 2008
Leticia Vittone Cecilia Mundina-Weilenmann Alicia Mattiazzi

Sarcoplasmic reticulum (SR) Ca2+ ATPase (SERCA2a) transports Ca2+ into the SR, decreasing the cytosolic Ca2+ during relaxation and increasing the SR Ca2+ available for contraction. SERCA2a activity is regulated by phosphorylation of another SR protein: Phospholamban (PLN). Dephosphorylated PLN inhibits SERCA2a. Phosphorylation of PLN by either cAMP or cGMP-dependent protein kinase at Ser16 or t...

Journal: :American journal of physiology. Heart and circulatory physiology 2009
Jason R Waggoner Kenneth S Ginsburg Bryan Mitton Kobra Haghighi Jeffrey Robbins Donald M Bers Evangelia G Kranias

Phospholamban has been suggested to be a key regulator of cardiac sarcoplasmic reticulum (SR) Ca cycling and contractility and a potential therapeutic target in restoring the depressed Ca cycling in failing hearts. Our understanding of the function of phospholamban stems primarily from studies in genetically altered mouse models. To evaluate the significance of this protein in larger mammalian ...

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