Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Grant G. Kelley"'
Autor:
Colin A. Leech, Grant G. Kelley, Michael W. Roe, Elvira Dzhura, Parisa Afshari, Frank Schwede, Xiangquan Li, George G. Holz, Hans-G. Genieser, Oleg G. Chepurny, Igor Dzhura
Publikováno v:
Islets. 1:260-265
Epac2 is a cAMP-regulated guanine nucleotide exchange factor (cAMP-GEF) that is proposed to mediate stimulatory actions of the second messenger cAMP on mouse islet insulin secretion. Here we have used methods of islet perifusion to demonstrate that t
Autor:
Frank Schwede, George G. Holz, Grant G. Kelley, Igor Dzhura, Michael J. Rindler, Elvira Dzhura, Xiangquan Li, Hans G. Genieser, Colin A. Leech, Oleg G. Chepurny
Publikováno v:
Journal of Biological Chemistry. 284:10728-10736
To ascertain the identities of cyclic nucleotide-binding proteins that mediate the insulin secretagogue action of cAMP, the possible contributions of the exchange protein directly activated by cAMP (Epac) and protein kinase A (PKA) were evaluated in
Autor:
Robert T. Dirksen, Sundeep Malik, Sanjeewa A. Goonasekera, Grant G. Kelley, Emily A. Oestreich, Burns C. Blaxall, Alan V. Smrcka
Publikováno v:
Journal of Biological Chemistry. 284:1514-1522
Recently, we identified a novel signaling pathway involving Epac, Rap, and phospholipase C (PLC)epsilon that plays a critical role in maximal beta-adrenergic receptor (betaAR) stimulation of Ca2+-induced Ca2+ release (CICR) in cardiac myocytes. Here
Publikováno v:
Journal of Biological Chemistry. 282:20104-20115
Inositol 1,4,5-trisphosphate (IP(3)) receptors are endoplasmic reticulum (ER) membrane calcium channels that, upon activation, become substrates for the ER-associated degradation (ERAD) pathway. Although it is clear that IP(3) receptors are polyubiqu
Autor:
Alan V. Smrcka, Katherine A. Kaproth-Joslin, Huan Wang, Robert T. Dirksen, Emily A. Oestreich, Burns C. Blaxall, Sundeep Malik, Grant G. Kelley
Publikováno v:
Journal of Biological Chemistry. 282:5488-5495
Recently we demonstrated that PLC(epsilon) plays an important role in beta-adrenergic receptor (betaAR) stimulation of Ca(2+)-induced Ca(2+) release (CICR) in cardiac myocytes. Here we have reported for the first time that a pathway downstream of bet
Autor:
Tom D. Bunney, Grant G. Kelley, Puneet Garg, Christian Becker, Alper Soylu, Dontscho Kerjaschki, Thomas Gudermann, Alexander Dietrich, Roxana Cleper, Jinhong Liu, Alexey N. Tsygin, Lina Basel-Vanagaite, Andreas Kispert, Caroline S. Sorli, Rannar Airik, Martin Pohl, Friedhelm Hildebrandt, Bettina E. Mucha, Matilda Katan, Martin Griebel, Alan V. Smrcka, Meera Goyal, Aysin Bakkaloglu, Katrin Hasselbacher, Bernward Hinkes, Rasheed Gbadegesin, John F. O'Toole, Rüdiger Waldherr, Massimo Attanasio, Roger C. Wiggins, Sudha Mudumana, Bryan L. Wharram, Christopher N. Vlangos, Edgar A. Otto, Asher D. Schachter, Lawrence B. Holzman, Fatih Ozaltin, Bethan E. Hoskins, Gudrun Nürnberg, Iain A. Drummond, Hassan Chaib, Dominik Seelow, Peter Nürnberg, Rakesh Verma, Shazia Ashraf, Dominik N. Müller, Hans Christian Hennies
Publikováno v:
Nature Genetics. 38:1397-1405
Nephrotic syndrome, a malfunction of the kidney glomerular filter, leads to proteinuria, edema and, in steroid-resistant nephrotic syndrome, end-stage kidney disease. Using positional cloning, we identified mutations in the phospholipase C epsilon ge
Autor:
Grant G. Kelley, Robert T. Dirksen, Burns C. Blaxall, Karen L. Vikstrom, Naoya Maekawa, Emily A. Oestreich, Alan V. Smrcka, Tara A. Bullard, Huan Wang
Publikováno v:
Circulation Research. 97:1305-1313
Phospholipase C (PLC) ε is a recently identified enzyme regulated by a wide range of molecules including Ras family small GTPases, Rho A, Gα 12/13 , and Gβγ with primary sites of expression in the heart and lung. In a screen for human signal tran
Publikováno v:
Biochemical Journal. 378:129-139
PLCepsilon (phospholipase Cepsilon) is a novel PLC that has a CDC25 guanine nucleotide exchange factor domain and two RA (Ras-association) domains of which the second (RA2) is critical for Ras activation of the enzyme. In the present studies, we exam
Publikováno v:
Molecular and Cellular Endocrinology. 177:107-115
The mechanism by which glucose and other fuels stimulate phosphoinositide-specific phospholipase C (PLC) in pancreatic islet beta cells is not known. Previous studies have suggested that glucose may couple to PLC beta 1 and PLC delta 1. To determine
Publikováno v:
The EMBO Journal. 20:743-754
Three classes of mammalian phosphoinositide-specific phospholipase C (PLC) have been characterized, PLCβ, PLCγ and PLCδ, that are differentially regulated by heterotrimeric G-proteins, tyrosine kinases and calcium. Here we describe a fourth class,