Specificity of the purified inositol (1,3,4,5) tetrakisphosphate‐binding protein from porcine platelets

Cullen, Peter J.; Chung, Sung‐Kee; Chang, Young‐Tae; Dawson, Alan P.; Irvine, Robin F.

doi:10.1016/0014-5793(94)01435-4

Cited by 32 publications

(13 citation statements)

References 9 publications

(38 reference statements)

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“…For the 104 kDa Ins(1,3,4,5)P 4 binding protein purified from porcine platelets a specificity different from that reported here was described [33]. The binding site on the 104 kDa protein was shown to be highly selective for D-Ins(1,3,4,5)P 4 and to recognize primarily the phosphates at C-1, C-3 and C-5, whereas a phosphate group at C-4 and C-6 had only little influence on binding.…”

Section: Discussioncontrasting

confidence: 78%

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Determination of Specificity of a High-Affinity Inositol 1,3,4,5-Tetrakisphosphate Binding Site at a 42 kDa Receptor Protein, p42IP4: Comparison of Affinities of All Inositoltris-, -Tetrakis-, and -Pentakisphosphate Regioisomers

Stricker

Chang

Chung

et al. 1996

Biochemical and Biophysical Research Communications

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Section: Discussioncontrasting

confidence: 78%

“…The binding site on the 104 kDa protein was shown to be highly selective for D-Ins(1,3,4,5)P 4 and to recognize primarily the phosphates at C-1, C-3 and C-5, whereas a phosphate group at C-4 and C-6 had only little influence on binding. A phosphate group at C-2 was not tolerated [33] as with the 42 kDa InsP 4 receptor from pig brain.…”

Section: Discussionmentioning

confidence: 93%

Determination of Specificity of a High-Affinity Inositol 1,3,4,5-Tetrakisphosphate Binding Site at a 42 kDa Receptor Protein, p42IP4: Comparison of Affinities of All Inositoltris-, -Tetrakis-, and -Pentakisphosphate Regioisomers

Stricker

Chang

Chung

et al. 1996

Biochemical and Biophysical Research Communications

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“…The predicted B max is 9.6 nmol\mg of protein assuming one ligand binding site per molecule. In all respects, including the pH dependence for ligand binding [34], the human platelet protein appears to be identical to the 104 kDa protein from pig platelet plasma membranes isolated by Cullen et al [7]. These platelet proteins differ from all other putative InsP % binding proteins, such as the two fractions from brain with a high specific affinity for InsP % , which contained polypeptides of 182 plus 123 kDa and 174 plus 84 kDa respectively [14].…”

Section: Discussionmentioning

confidence: 99%

Isolation of InsP4 and InsP6 binding proteins from human platelets: InsP4 promotes Ca2+ efflux from inside-out plasma membrane vesicles containing 104 kDa GAP1IP4BP protein

O'Rourke

Matthews

Feinstein

1996

Biochemical Journal

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A low-density membrane fraction from human platelets contained the plasma membrane marker glycoprotein Ib (GpIb) and selective binding sites for InsP4 and InsP6. It was separated from the bulk of InsP3-receptor-containing membranes, but was heterogeneous, probably also containing surface-connected canalicular system and some lighter elements of the internal dense tubule system. After loading with calcium oxalate and re-centrifugation on Percoll gradients, this mixed fraction was subfractionated into light membranes containing all of the GpIb, high-affinity InsP4 binding sites (KD = 18 nM) and phosphate-stimulated Ca2+ transport activity. InsP4 (EC50 0.6 microM), but not InsP3 or InsP6, released up to 35% of the accumulated Ca2+ from these vesicles, which were shown to be inside-out plasma membrane vesicles by a biotinylation labelling technique and selective removal of right-side-out plasma membrane vesicles with streptavidin-agarose. Most of the InsP4, and all of the InsP6, binding was present in the much denser calcium oxalate-loaded subfractions, which were free of GpIb. InsP6 binding activity was chromatographically purified as a 116 kDa protein (KD for InsP6 = 5.9 nM), with an amino acid content and two internal peptide sequences identical to those of 116 kDa vinculin. A 104 kDa InsP4 binding protein (KD for InsP4 = 12 nM), probably identical to GAP1IP4BP described by Cullen, Hsuan, Truong, Letcher, Jackson, Dawson and Irvine [(1995) Nature (London) 376, 527-530], was also isolated. This InsP4 receptor may mediate Ca2+ influx in platelets that occurs subsequent to receptor-stimulated production of InsP3 and unloading of internal Ca2+ stores.

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“…Thus overall, these observations seem to suggest that these various exogenous agents enhance the endogenous effect of Ins(1,3,4,5)P % rather than cause an entirely different and independent effect. The data presented above strongly suggests that the effects of Ins(1,3,4,5)P % on Ins(2,4,5)P $ -mediated Ca# + mobilization in permeabilized L1210 cells involve GAP1 IP%BP , which has been reported to be a putative Ins(1,3,4,5)P % receptor on the basis of its specificity for Ins(1,3,4,5)P % binding [14,15]. However, at present, we cannot be sure whether GAP1 IP%BP or GAP1 m (or both) modulates the endogenous Ins(1,3,4,5)P % effect, i.e.…”

mentioning

confidence: 99%

Modulation of Ins(2,4,5)P3-stimulated Ca2+ mobilization by Ins(1,3,4,5)P4: enhancement by activated G-proteins, and evidence for the involvement of a GAP1 protein, a putative Ins(1,3,4,5)P4 receptor

Loomis-Husselbee

Walker

Bottomley

et al. 1998

Biochemical Journal

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We have previously shown that addition of Ins(1,3,4,5)P4 to permeabilized L1210 cells increases the amount of Ca2+ mobilized by a submaximal concentration of Ins(2,4,5)P3, and we suggested that, in doing this, Ins(1,3,4,5)P4 is not working via an InsP3 receptor but indirectly via an InsP4 receptor [Loomis-Husselbee, Cullen, Dreikhausen, Irvine and Dawson (1996) Biochem. J. 314, 811-816]. Here we have investigated whether this effect might be mediated by GAP1(IP4BP), recently identified as a putative receptor for Ins(1,3, 4,5)P4. GAP1(IP4BP) is a protein that interacts with one or more monomeric G-proteins, so we sought evidence for involvement of monomeric G-proteins in the effects of Ins(1,3,4,5)P4 in permeabilized L1210 cells. Guanosine 5'-[gamma-thio]triphosphate (GTP[S]) enhanced the effect of Ins(1,3,4,5)P4 on Ins(2,4, 5)P3-stimulated Ca2+ mobilization, but had no effect on the action of Ins(2,4,5)P3 alone. A specific enhancement of only the action of Ins(1,3,4,5)P4 was also seen with GTP[S]-loaded R-Ras or Rap1a (two G-proteins known to interact with GAP1(IP4BP)), whereas H-Ras was inactive at similar concentrations. Guanosine 5'-[beta-thio]diphosphate (GDP[S]) did not alter the action of either Ins(2,4,5)P3 or Ins(1,3,4,5)P4. Finally, the addition of exogenous GAP1(IP4BP), purified from platelets, markedly enhanced the effect of Ins(1,3,4,5)P4, and again, the amount of Ca2+ mobilized by Ins(2,4,5)P3 alone was unaltered. We conclude that the increase in Ins(2,4,5)P3-stimulated Ca2+ mobilization by Ins(1,3,4, 5)P4 may be mediated by GAP1(IP4BP) or a closely related protein (such as GAP1(m)), and if so, the action of the GAP1 is not solely to regulate GTP loading of a G-protein, but rather it acts with a G-protein to cause its effect.

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Specificity of the purified inositol (1,3,4,5) tetrakisphosphate‐binding protein from porcine platelets

Cited by 32 publications

References 9 publications

Determination of Specificity of a High-Affinity Inositol 1,3,4,5-Tetrakisphosphate Binding Site at a 42 kDa Receptor Protein, p42IP4: Comparison of Affinities of All Inositoltris-, -Tetrakis-, and -Pentakisphosphate Regioisomers

Determination of Specificity of a High-Affinity Inositol 1,3,4,5-Tetrakisphosphate Binding Site at a 42 kDa Receptor Protein, p42IP4: Comparison of Affinities of All Inositoltris-, -Tetrakis-, and -Pentakisphosphate Regioisomers

Isolation of InsP4 and InsP6 binding proteins from human platelets: InsP4 promotes Ca2+ efflux from inside-out plasma membrane vesicles containing 104 kDa GAP1IP4BP protein

Modulation of Ins(2,4,5)P3-stimulated Ca2+ mobilization by Ins(1,3,4,5)P4: enhancement by activated G-proteins, and evidence for the involvement of a GAP1 protein, a putative Ins(1,3,4,5)P4 receptor

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