Solubilization, purification, and characterization of an inositol trisphosphate receptor.

Supattapone, Surachai; Worley, PF; Baraban, Jay M.; Snyder, Solomon H.

doi:10.1016/s0021-9258(19)57336-7

Cited by 617 publications

(86 citation statements)

References 21 publications

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“…Additionally, the subcellular distribution of the three isoforms is celltype dependent [64]. IP3R1 has a broad tissue distribution but is especially abundant in the cerebellum, where it was initially purified and characterized [65]. It is also expressed in vascular smooth muscle cells, thyroid, uterus, and lymphocytes [20,66,67].…”

Section: Ip3rsmentioning

confidence: 99%

Essential Roles of Intracellular Calcium Release Channels in Muscle, Brain, Metabolism, and Aging

Santulli

Marks

2015

CMP

184

165

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Calcium (Ca(2+)) release from intracellular stores controls numerous cellular processes, including cardiac and skeletal muscle contraction, synaptic transmission and metabolism. The ryanodine receptors (RyRs: RyR1, RyR2, RyR3) and inositol 1,4,5-trisphosphate receptors (IP3Rs: IP3R1, IP3R2, IP3R3) are the major Ca(2+) release channels (CRCs) on the endo/sarcoplasmic reticulum (ER/SR). RyRs and IP3Rs comprise macromolecular signaling complexes that include modulatory proteins which regulate channel activity in response to extracellular signals resulting in intracellular Ca(2+) release. Here we focus on the roles of CRCs in heart, skeletal muscle, brain, metabolism, and aging.

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Section: Ip3rsmentioning

confidence: 99%

Essential Roles of Intracellular Calcium Release Channels in Muscle, Brain, Metabolism, and Aging

Santulli

Marks

2015

CMP

184

165

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“…InsP3 binding in cerebellum was increased at alkaline pH, blocked by heparin (50% inhibition at 0.25-0.5 #M), and potently inhibited by Ca2+ (50 % inhibition at 0.3 /SM) through the mediation of a Ca2+-binding protein termed calmedin (Danoff et al, 1988). By using its affinity for heparin, an InsP.-binding protein was purified from rat cerebellum by affinity chromatography (Supattapone et al, 1988b). This InsP,-binding protein (Mr 260000) displayed most of the characteristics observed in cerebellar membranes, supporting the view that it is the physiological receptor.…”

Section: Introductionmentioning

confidence: 99%

The inositol 1,4,5-trisphosphate receptor binding sites of platelet membranes. pH-dependency, inhibition by polymeric sulphates, and the possible presence of arginine at the binding site

O'Rourke

Feinstein

1990

Biochemical Journal

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The present study was initiated to characterize the inositol 1,4,5-trisphosphate (InsP3)-binding site in human platelets that is involved in Ca2+ release. InsP3 binding to platelet membranes was measured in two ways; (1) by displacement of labelled InsP3 with unlabelled InsP3, as in previous studies, and (2) directly, using only radioactive InsP3 as ligand, over the concentration range 0.25-100 nM. At physiological pH (7.1) the binding data were best fitted by a model for a single saturable binding site, with KD = 11.8 nM and Bmax. = 1.4 pmol/mg of protein. At alkaline pH values (8.3 and 9.4) binding was best fitted by a two-site model, the second site being of higher affinity (KD = 0.75-1.2 nM) but lower concentration (Bmax. = 0.195-0.6 pmol/mg of protein). All binding of InsP3 was blocked by polymeric sulphates (heparin, dextran sulphate, polyvinyl sulphate) regardless of pH. The specific arginine-modifying reagent p-hydroxyphenylglyoxal irreversibly blocked InsP3 binding, suggesting the presence of arginine at the recognition site for InsP3 binding. NN'-dicyclohexylcarbodi-imide (DCCD) and 1-ethyl-3-(3-dimethylaminopropyl)carbodi-imide (ECCD), which are carboxy-group-specific reagents, blocked Ca2+ release, but not InsP3 binding, indicating the existence of another site that regulates Ca2+ release apart from the active centre for InsP3.

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“…The IP 3 R has been purified from rat cerebellum (Supattapone et al, 1988) and localized primarily to the endoplasmic reticulum (ER; Mignery et al, 1989;Ross et al, 1989) though nuclear, plasma membrane and neurotransmitter vesicle localizations have also been described (Khan et al, 1992;Furuichi et al, 1994;Furuichi and Mikoshiba, 1995;Petersen, 1996). Molecular cloning reveals three different isoforms encoded by different genes, IP 3 R1, 2, and 3 (Furuichi et al, 1989;Mignery et al, 1989;Sudhof et al, 1991;Ross et al, 1992;Blondel et al, 1993;Maranto, 1994;De Smedt et al, 1997).…”

mentioning

confidence: 99%

Differential cellular expression of isoforms of inositol 1,4,5-triphosphate receptors in neurons and glia in brain

Sharp

Nucifora

Blondel³

et al. 1999

J. Comp. Neurol.

186

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Inositol 1,4,5-trisphosphate receptors (IP 3 R) are mediators of second messenger-induced intracellular calcium release. Three isoforms are known to be expressed in brain, but their regional distributions and cellular localizations are little known. In order to better understand the roles of IP 3 receptor isoforms in brain function, a first step is to define their distributions. We have used affinity-purified antibodies directed against peptides unique to each isoform to determine their sites of expression in rat brain. Type 1 IP 3 R (IP 3 R1) is dramatically enriched in Purkinje neurons in cerebellum and neurons in other regions, consistent with previous studies. By contrast, IP 3 R2 is only detected in glia, whereas IP 3 R3 is predominantly neuronal, with little detected in glia. IP 3 R3 is enriched in neuropil, especially in neuronal terminals (which often contain large dense core vesicles) in limbic and basal forebrain regions including olfactory tubercle, central nucleus of the amygdala, and bed nucleus of the stria terminalis. In addition, IP 3 R1 and IP 3 R3 have clearly distinct time courses of expression in developing brains. These data suggest separate roles for inositol 1,4,5trisphosphate receptor isoforms in development, and for glial and neuronal function. The IP 3 R3 may be involved in regulation of neurotransmitter or neuropeptide release in terminals within specific nuclei of the basal forebrain and limbic system.

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Solubilization, purification, and characterization of an inositol trisphosphate receptor.

Cited by 617 publications

References 21 publications

Essential Roles of Intracellular Calcium Release Channels in Muscle, Brain, Metabolism, and Aging

Essential Roles of Intracellular Calcium Release Channels in Muscle, Brain, Metabolism, and Aging

The inositol 1,4,5-trisphosphate receptor binding sites of platelet membranes. pH-dependency, inhibition by polymeric sulphates, and the possible presence of arginine at the binding site

Differential cellular expression of isoforms of inositol 1,4,5-triphosphate receptors in neurons and glia in brain

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