scholarly journals The Type I Inositol 1,4,5-Trisphosphate Receptor Interacts with Protein 4.1N to Mediate Neurite Formation through Intracellular Ca2+ Waves

Neurosignals ◽  
2011 ◽  
Vol 19 (2) ◽  
pp. 75-85 ◽  
Author(s):  
Michael J. Fiedler ◽  
Michael H. Nathanson
Keyword(s):  
Type I ◽  
Inositol 1,4,5 Trisphosphate ◽  
Neurite Formation ◽  
Intracellular Ca ◽  
Trisphosphate Receptor

Effect of halothane on intracellular calcium oscillations in porcine tracheal smooth muscle cells

1999 ◽  
Vol 276 (1) ◽  
pp. L81-L89 ◽  
Author(s):  
Christina M. Pabelick ◽  
Y. S. Prakash ◽  
Mathur S. Kannan ◽  
Keith A. Jones ◽  
David O. Warner ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Cells ◽  
Ryanodine Receptor ◽  
Muscle Cells ◽  
Calcium Oscillations ◽  
Tracheal Smooth Muscle ◽  
Permeabilized Cells ◽  
Inositol 1,4,5 Trisphosphate ◽  
Intracellular Ca ◽  
Trisphosphate Receptor

The effect of halothane on intracellular Ca2+ concentration ([Ca2+]i) regulation in porcine tracheal smooth muscle cells was examined with real-time confocal microscopy. Both 1 and 2 minimum alveolar concentration (MAC) halothane increased basal [Ca2+]iwhen Ca2+ influx and efflux were blocked, suggesting increased sarcoplasmic reticulum (SR) Ca2+ leak and/or decreased reuptake. In β-escin-permeabilized cells, heparin inhibition of inositol 1,4,5-trisphosphate-receptor channels blunted the halothane-induced increase in [Ca2+]i. Both 1 and 2 MAC halothane decreased the frequency and amplitude of ACh-induced [Ca2+]ioscillations (which represent SR Ca2+ release through ryanodine-receptor channels), abolishing oscillations in ∼20% of tracheal smooth muscle cells at 2 MAC. When Ca2+ influx and efflux were blocked, halothane increased the baseline and decreased the frequency and amplitude of [Ca2+]ioscillations, inhibiting oscillations in ∼70% of cells at 2 MAC. The fall time of [Ca2+]ioscillations and the rate of fall of the [Ca2+]iresponse to caffeine were both increased by halothane. These results suggest that halothane abolishes agonist-induced [Ca2+]ioscillations by 1) depleting SR Ca2+ via increased Ca2+ leak through inositol 1,4,5-trisphosphate-receptor channels, 2) decreasing Ca2+ release through ryanodine-receptor channels, and 3) inhibiting reuptake.

scholarly journals Polycystin 2 Interacts with Type I Inositol 1,4,5-Trisphosphate Receptor to Modulate Intracellular Ca2+Signaling

2005 ◽  
Vol 280 (50) ◽  
pp. 41298-41306 ◽  
Author(s):  
Yun Li ◽  
Jerry M. Wright ◽  
Feng Qian ◽  
Gregory G. Germino ◽  
William B. Guggino
Keyword(s):  
Type I ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

Molecular basis for calcium signaling in hepatic stellate cells

2007 ◽  
Vol 292 (4) ◽  
pp. G975-G982 ◽  
Author(s):  
Emma A. Kruglov ◽  
Paulo R. A. V. Correa ◽  
Gaurav Arora ◽  
Jin Yu ◽  
Michael H. Nathanson ◽  
...  
Keyword(s):  
Liver Fibrosis ◽  
Hepatic Stellate Cells ◽  
Stellate Cells ◽  
P2y Receptors ◽  
Type I ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor ◽  
Healthy Liver ◽  
Organ Fibrosis ◽  
Injured Liver

Progressive liver fibrosis (with the resultant cirrhosis) is the primary cause of chronic liver failure. Hepatic stellate cells (HSCs) are critically important mediators of liver fibrosis. In the healthy liver, HSCs are quiescent lipid-storing cells limited to the perisinusoidal endothelium. However, in the injured liver, HSCs undergo myofibroblastic transdifferentiation (activation), which is a critical step in the development of organ fibrosis. HSCs express P2Y receptors linking extracellular ATP to inositol (1,4,5)-trisphosphate-mediated cytosolic Ca2+ signals. Here, we report that HSCs express only the type I inositol (1,4,5)-trisphosphate receptor and that the receptor shifts into the nucleus and cell extensions upon activation. These cell extensions, furthermore, express sufficient machinery to enable local application of ATP to evoke highly localized Ca2+ signals that induce localized contractions. These autonomous units of subcellular signaling and response reveal a new level of subcellular organization, which, in turn, establishes a novel paradigm for the local control of fibrogenesis in the liver.

scholarly journals Defining the minimal structural requirements for partial agonism at the type I myo -inositol 1,4,5-trisphosphate receptor

FEBS Letters ◽  
1997 ◽  
Vol 402 (2-3) ◽  
pp. 241-245 ◽  
Author(s):  
Robert A. Wilcox ◽  
Abdul Fauq ◽  
Alan P. Kozikowski ◽  
Stefan R. Nahorski
Keyword(s):  
Type I ◽  
Partial Agonism ◽  
Structural Requirements ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

scholarly journals TRPC3 Regulates Agonist-stimulated Ca2+Mobilization by Mediating the Interaction between Type I Inositol 1,4,5-Trisphosphate Receptor, RACK1, and Orai1

2009 ◽  
Vol 285 (11) ◽  
pp. 8045-8053 ◽  
Author(s):  
Geoffrey E. Woodard ◽  
José J. López ◽  
Isaac Jardín ◽  
Ginés M. Salido ◽  
Juan A. Rosado
Keyword(s):  
Type I ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

scholarly journals Proteolysis of type I inositol 1,4,5-trisphosphate receptor in WB rat liver cells

2003 ◽  
Vol 375 (3) ◽  
pp. 603-611 ◽  
Author(s):  
M. Tariq KHAN ◽  
Suresh K. JOSEPH
Keyword(s):  
Angiotensin Ii ◽  
Rat Liver ◽  
Liver Cells ◽  
Peptide Sequence ◽  
Endoplasmic Reticulum Membrane ◽  
Type I ◽  
Lysosomal Protease ◽  
Inositol 1,4,5 Trisphosphate ◽  
Rat Liver Cells ◽  
Trisphosphate Receptor

A comparison of the basal degradation of type I InsP3Rs [d-myo-inositol 1,4,5-trisphosphate receptor], measured by pulse–chase analysis or by analysis of immunoreactive InsP3Rs after cycloheximide addition, indicated that the small pool of newly synthesized radioactive InsP3Rs degraded relatively rapidly compared with the large pool of mature InsP3Rs. An antibody (Ab) against a peptide sequence within the IL-3 (third intraluminal loop) of the receptor (IL-3 Ab) was used to identify protected proteolytic fragments that may accumulate in cells. The IL-3 Ab recognized a 56 kDa fragment in both WB rat liver cells and A7R5 smooth-muscle cells. Gel filtration experiments indicated that the 56 kDa fragment was monomeric and, based on reactivity to other Abs, was missing the cytosol-exposed N- and C-terminal segments of the receptor. The addition of the lysosomal protease inhibitor chloroquine resulted in the rapid disappearance of the 56 kDa band. This effect was mimicked by the cysteine protease inhibitors leupeptin, N-acetyl-l-leucyl-l-leucyl-l-methioninal and N-acetyl-leucyl-leucyl-norleucinal. Lactacystin and NH4Cl were less effective. A second fragment of 16 kDa containing the C-terminus accumulated only when the cells were treated with NH4Cl, and not with any of the other inhibitors tested. No N-terminal-reactive fragments were observed. We propose that mature InsP3R tetramers dissociate into monomers and that the 56 kDa fragment is a cleavage intermediate of the monomer representing the six transmembrane domains. Angiotensin-II-stimulated down-regulation of InsP3Rs in WB cells has been shown to involve the ubiquitin/proteasome pathway. Angiotensin-II treatment of WB cells neither resulted in the accumulation of any new fragments nor increased the levels of the 56 or 16 kDa fragments. We conclude that basal and agonist-stimulated degradations of InsP3Rs occur by different pathways. The agonist-mediated pathway involves the concerted removal and proteolysis of the entire receptor molecule from the endoplasmic reticulum membrane without the appearance of intermediate intraluminal fragments.

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