Specific Receptors for Inositol 1,4,5-Trisphosphate in Endocrine Target Tissues

Guillemette, Gaétan; Balla, Tamás; Báukal, Albert J.; Catt, Kevin J.

doi:10.1007/978-1-4684-5598-4_21

Cited by 69 publications

(102 citation statements)

References 27 publications

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“…Morever, the IPrinduced Ca 2+ release has been found to be suppressed by micromolar concentrations of Cd 2+ in permeabilized d-cells [15]. The effect of Cd 2+ might reflect its binding to IP3 and thereby changing the binding properties of the trisphosphate to its receptor [25]. We cannot exclude that heparin also exerts its effect by binding IP3, but it should be remembered that both the polysaccaride and the trisphosphate are negatively charged [26].…”

Section: Resultsmentioning

confidence: 92%

Heparin inhibits IP₃‐induced Ca²⁺ release in permeabilized pancreatic β‐cells

et al. 1988

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Heparin was found to inhibit the Ca 2+ release induced by inositoi 1,4,5-trisphosphate (IP3) in permeabilized pancreatic fit:ells obtained from obese hyperglycemic mice. The effect of heparin was dose-dependent and not due to inhibition of Ca 2+ uptake into the IP3-sensitive pool. The effect appeared specific for hepafin and was not reproduced by other polysaccharides such as chondroitin sulfates. Heparin might consequently be a useful tool when investigating the molecular mechanism whereby IP 3 mobilizes Ca 2+ .

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Section: Resultsmentioning

confidence: 92%

Heparin inhibits IP₃‐induced Ca²⁺ release in permeabilized pancreatic β‐cells

et al. 1988

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“…Recently, an InsP3 binding site has been detected by analysis of a series of deleted or truncated mouse cerebellar InsP3R mutant proteins expressed in NG108-15 cells and shown that deletion of the region including SI (amino acids 316-352) greatly reduced InsP3 binding ofthe receptor (33). It has been reported that the dissociation constant (Kd) of InsP3 is 1.7-10.4 nM in peripheral tissues (16,18,19), whereas it is 80-100 nM in the cerebellum of adult mouse or rat (12,13). Therefore, it is possible that the SI domain has an effect on the affinity of InsP3.…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies have demonstrated that the InsP3R is identical to the P4w protein (12), which has been identified as a protein highly enriched in the cerebellar Purkinje cells (15). InsP3R/P400, however, has been shown to be a glycoprotein that is present in a variety of tissues (11,(16)(17)(18)(19). However, little is known about the heterogeneity of the InsP3R molecules among these tissues or whether different forms of InsP3R underlie its various activities.…”

mentioning

confidence: 99%

The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are expressed in a tissue-specific and developmentally specific manner.

Nakagawa

Okano

Furuichi

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

218

163

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Additional subtypes of the inositol 1,4,5-trisphosphate (InsP3) receptor are expressed in a tissue-specific and developmentally specific manner. They differ from the InsP3 receptor structure previously reported in two small variably spliced segments. One segment (SI) is located within the InsP3 binding site, whereas another segment (SiU) is located near putative sites for phosphorylation and ATP binding to modulate InsP3 action on Ca2+ flux. Therefore, we speculate that selective use of InsP3 receptor subtypes permits a tissuespecific and developmentally specific expression of functionally distinct channels.

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“…The finding that a considerable percentage of the platelet Ins(1,4,5)P3 phosphatase is associated with the membranes could be relevant to platelet physiology. This is of particular interest in light of the finding that Ins(1,4,5)-P3-binding sites are enriched in a fraction that co-purified with the plasma membrane of hepatocytes [39]. This enzyme is then adjacent to the site at which Ins(1,4,5)-P3 is produced.…”

Section: Discussionmentioning

confidence: 99%

Subcellular localization of the enzymes that dephosphorylate myo-inositol polyphosphates in human platelets

Vedia

Nolan

Lapetina

1988

Biochemical Journal

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The phosphatase-induced hydrolysis of [3H]inositol 1,4-bisphosphate [Ins(1,4)P2)] and [3H]inositol 1,4,5-trisphosphate [Ins(1,4,5)P3] was studied in platelet subcellular fractions. The activity that hydrolyses Ins(1,4)P2 is cytosolic, whereas the activity that hydrolyses Ins(1,4,5)P3 is present in both particulate and cytosolic fractions. The cytosolic Ins(1,4)P2 phosphatase hydrolyses the 1-phosphate of Ins(1,4)P2, whereas the cytosolic and membrane-bound Ins(1,4,5)P3 phosphatases hydrolyse the 5-phosphate of Ins(1,4,5)P3. In the presence of ATP, it is possible to observe a cytosolic Ins(1,4,5)P3 3-kinase that phosphorylates Ins(1,4,5)P3 to inositol 1,3,4,5-tetrakisphosphate. Apparent Km values for the particulate and the cytosolic Ins(1,4,5)P3 phosphatases are 100 tM and 40,/M respectively. A large proportion of the membraneassociated Ins(1,4,5)P3 phosphatase can be extracted with 1 M-NaCl, and the Mr of this enzyme, as determined by hydrodynamic studies, is 49000, whereas that of the cytosolic enzyme is 59000. The Km values for the cytosolic Ins(1,4)P2 phosphatase is 40 ,UM; this enzyme has an Mr of49 000. The highest specific activity of the Ins(1,4,5)P3 phosphatase is present in a highly purified plasma-membrane fraction.

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Specific Receptors for Inositol 1,4,5-Trisphosphate in Endocrine Target Tissues

Cited by 69 publications

References 27 publications

Heparin inhibits IP₃‐induced Ca²⁺ release in permeabilized pancreatic β‐cells

Heparin inhibits IP₃‐induced Ca²⁺ release in permeabilized pancreatic β‐cells

The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are expressed in a tissue-specific and developmentally specific manner.

Subcellular localization of the enzymes that dephosphorylate myo-inositol polyphosphates in human platelets

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Specific Receptors for Inositol 1,4,5-Trisphosphate in Endocrine Target Tissues

Cited by 69 publications

References 27 publications

Heparin inhibits IP3‐induced Ca2+ release in permeabilized pancreatic β‐cells

Heparin inhibits IP3‐induced Ca2+ release in permeabilized pancreatic β‐cells

The subtypes of the mouse inositol 1,4,5-trisphosphate receptor are expressed in a tissue-specific and developmentally specific manner.

Subcellular localization of the enzymes that dephosphorylate myo-inositol polyphosphates in human platelets

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Heparin inhibits IP₃‐induced Ca²⁺ release in permeabilized pancreatic β‐cells

Heparin inhibits IP₃‐induced Ca²⁺ release in permeabilized pancreatic β‐cells