Zobrazeno 1 - 10
of 85
pro vyhledávání: '"Ingrid L. Grupp"'
Publikováno v:
Journal of Molecular and Cellular Cardiology. 37:913-919
We have previously reported that genetic reduction of the Na,K-ATPase alpha1 isoform (alpha1(+/-)) results in a hypocontractile cardiac phenotype. This observation was surprising and unexpected. In order to determine if calcium overload contributes t
Autor:
W. Jonathan Lederer, Keith W. Dilly, Kin M. Choi, Harvey S. Hahn, Silvia Guatimosim, Mohammed A. Matlib, Brian D. Hoit, Yan Zhong, Ingrid L. Grupp
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 283:H1398-H1408
The goal of the study was to determine whether defects in intracellular Ca2+ signaling contribute to cardiomyopathy in streptozotocin (STZ)-induced diabetic rats. Depression in cardiac systolic and diastolic function was traced from live diabetic rat
Autor:
R. Johnson, Mike Gerst, Evangelia G. Kranias, Peter James, Rajesh Dash, T. Tamura, A.M. Gerdes, Carola Tilgmann, D. Holder, Albrecht Schmidt, Jay Patrick Slack, Ingrid L. Grupp
Publikováno v:
Journal of Molecular and Cellular Cardiology. 33:1031-1040
J. P. Slack, I. L. Grupp, R. Dash, D. Holder, A. Schmidt, M. J. Gerst, T. Tamura, C. Tilgmann, P. F. James, R. Johnson, A. M. Gerdes and E. G. Kranias. The Enhanced Contractility of the Phospholamban-deficient Mouse Heart Persists with Aging. Journal
Publikováno v:
Journal of Biological Chemistry. 275:24722-24727
The sarcoplasmic reticulum calcium ATPase SERCA2b is an alternate isoform encoded by the SERCA2 gene. SERCA2b is expressed ubiquitously and has a higher Ca(2+) affinity compared with SERCA2a. We made transgenic mice that overexpress the rat SERCA2b c
Autor:
Christian C. Evans, Brian D. Hoit, Greg P. Boivin, R. John Solaro, Beata M. Wolska, David F. Wieczorek, Kathy Pieples, Prabhakar Rethinasamy, Ingrid L. Grupp, Mariappan Muthuchamy
Publikováno v:
Circulation Research. 85:47-56
Abstract —To investigate the functional consequences of a tropomyosin (TM) mutation associated with familial hypertrophic cardiomyopathy (FHC), we generated transgenic mice that express mutant α-TM in the adult heart. The missense mutation, which
Autor:
Ingrid L. Grupp, Heping Cheng, Hiroshi Yamaguchi, William Lewis, Gyula Varadi, Edward G. Lakatta, James N. Muth, Long-Sheng Song, Arnold M. Schwartz, Gabor Mikala
Publikováno v:
Journal of Biological Chemistry. 274:21503-21506
The L-type voltage-dependent calcium channel (L-VDCC) regulates calcium influx in cardiac myocytes. Activation of the beta-adrenergic receptor (betaAR) pathway causes phosphorylation of the L-VDCC and that in turn increases Ca(2+) influx. Targeted ex
Autor:
G. Roger Askew, Alison L. Woo, Ingrid L. Grupp, Jerry B. Lingrel, Richard A. Walsh, Gunter Grupp, Paul F. James, Michelle L. Croyle
Publikováno v:
Molecular Cell. 3:555-563
It is well accepted that inhibition of the Na,K-ATPase in the heart, through effects on the Na/Ca exchanger, raises the intracellular Ca2+ concentration and strengthens cardiac contraction. However, the contribution that individual isoforms make to t
Autor:
Muthu Periasamy, Ingrid L. Grupp, Evgeny Loukianov, Richard A. Walsh, Gunter Grupp, Jonathan Lytton, Tanya Loukianova, Darryl L. Kirkpatrick, Yong Ji, Debra L. Baker
Publikováno v:
Circulation Research. 83:889-897
Abstract —In this study, we investigated whether the fast-twitch skeletal muscle sarco(endo)plasmic reticulum Ca 2+ transport pump (SERCA1a) can functionally substitute the cardiac SERCA2a isoform and how its overexpression affects cardiac contract
Publikováno v:
Journal of Molecular and Cellular Cardiology. 30:1545-1557
Tropomyosin, a coiled-coil dimer, stabilizes actin filaments and is central to the control of calcium-regulated striated muscle contraction. Striated muscle-specific alpha-tropomyosin is the predominant isoform in cardiac muscle, with low levels of b
Publikováno v:
American Journal of Physiology-Cell Physiology. 273:C1-C6
Phospholamban (PLB) is expressed in slow-twitch skeletal, cardiac, and smooth muscles. Several studies have indicated that it is an important regulator of basal contractility and the stimulatory responses to isoproterenol in the mammalian heart. To d