Inhibition of phosphatidylinositol-4-phosphate kinase by its product phosphatidylinositol-4,5-bisphosphate

Rooijen, Lucio A.A. Van; Rossowska, M; Bazán, Nicolás G.

doi:10.1016/0006-291x(85)90584-4

Cited by 54 publications

(17 citation statements)

References 13 publications

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“…In conclusion, the present investigation raises com¬ pelling arguments for the occurrence of the indepen¬ dent regulation of PI-PLC and PI 4-kinase activity and strongly suggests that the formation of PIP2 in pancreatic mouse islets is not solely regulated by a PIP2 feedback inhibition of PIP kinase, which is relieved by activation of PI-PLC (13).…”

Section: Ip2 Ip3supporting

confidence: 50%

“…Concomitantly, there was an increased formation of inositol phosphates and a corresponding fall in PI. These observations are best explained by a primary activation of PI-PLC with a consequent fall in PIP2, removal of PIP2's inhibitory effect on the PIP kinase resulting in enhanced flux from PI -PIP -PIP2 and decreased PI levels in accordance with the proposed mechanism for continuing synthesis of PIP2 under these experimental conditions (13). CCh not only activated PI 4-kinase and the flux from PI to PIP and PIP2, but also stimulated PI-PLC in accordance with previous findings in pancreatic rat islets (26,30,31).…”

Section: Ip2 Ip3mentioning

confidence: 59%

“…The pool of the substrate PIP2 is very small compared with the amounts of inositol phosphates produced, and virtually nothing is known about how the synthesis of PIP2 from PI (that is the pathway PI -PIP -PIP2) is regulated in pancreatic islets. The product, PIP2, inhibits PIP kinase in certain tissues (13). When product inhibition is relieved by PI-PLC activa¬ tion the pool of PIP2 could automatically be replenished.…”

Section: Introductionmentioning

confidence: 99%

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Carbamoylcholine regulation of polyphosphoinositide synthesis and hydrolysis in cultured, dispersed, digitonin-permeabilized mouse pancreatic islet cells

Kardasz

Thams²,

Capito³

et al. 1997

European Journal of Endocrinology

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Continuing formation of inositol phosphates during stimulation of pancreatic beta-cells by hormones and neurotransmitters requires the continued synthesis of the polyphosphoinositides phosphatidylinositol 4-phosphate (PIP) and phosphatidylinositol 4,5 bisphosphate (PIP2) from phosphatidylinositol (PI). In the present study we have investigated how this pathway and the activity of phosphoinositide-specific phospholipase C (PI-PLC) are regulated by carbamoylcholine (CCh), Ca2+, the phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA), GTP gamma S and NaF in 44-h [3H]inositol-labelled, dispersed and digitonin-permeabilized mouse pancreatic islet cells. CCh stimulated not only PI-PLC (G-protein-mediated) but also, by an as yet unknown mechanism, significantly enhanced PI 4-kinase activity, estimated as the PIP:PI ratio, by 100%, and further increased the flux from PI to PIP and PIP2, GTP gamma S and NaF mimicked the effects of CCh on PI-PLC but had no effect on the levels of PIP and PIP2, TPA raised the PIP:PI ratio by 75%. In addition TPA counteracted the CCh stimulation of PI-PLC. There was no effect of 10(-6) mol/l Ca2+ on the levels of PIP and PIP2. Experiments with quinacrine and adenosine confirmed that PI-PLC and PI 4-kinase could be regulated independently of each other. In conclusion, these data point to differential regulation of polyphosphoinositide synthesis and breakdown.

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Section: Ip2 Ip3supporting

confidence: 50%

Section: Ip2 Ip3mentioning

confidence: 59%

Section: Introductionmentioning

confidence: 99%

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Carbamoylcholine regulation of polyphosphoinositide synthesis and hydrolysis in cultured, dispersed, digitonin-permeabilized mouse pancreatic islet cells

Kardasz

Thams²,

Capito³

et al. 1997

European Journal of Endocrinology

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“…Several groups have investigated the regulation of PtdInsP2 synthesis: product inhibition by PtdInsP2 has been reported in several tissues (Van Rooijen et al, 1985;Lundberg et al, 1986;Pike and Arndt, 1988), whilst PtdInsP2 production is stimulated when fibroblasts adhere to fibronectin (McNamee et al, 1993), suggesting that integrin-mediated signals may activate PIPkin activity. EGF stimulates PtdInsP2 synthesis in isolated A431 cell membranes (Payrastre et al, 1990) and PIPkin activity co-immunoprecipitates with the EGF receptor from B82L cells (Cochet et al, 1991), suggesting possible regulation by growth factors.…”

Section: Introductionmentioning

confidence: 99%

Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton.

1996

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Thrombin‐stimulated aggregation of human platelets promotes an increase in the phosphatidylinositol 4‐phosphate (PtdIns 4‐P) 5‐kinase (PIPkin) activity in the cytoskeleton. This phenomenon is associated with translocation of PIPkin isoform C to the cytoskeleton and with an increase in the amount of phosphatidylinositol bisphosphate (PtdInsP2) bound to the cytoskeletal pellet. All three of these effects are prevented if the platelets are not stirred or if RGD‐containing peptides are present, demonstrating that they require integrin activation. All three are also abolished by pretreatment with okadaic acid, which also prevents the aggregation‐dependent translocation of pp60(c‐src) to the cytoskeleton. The results point to the existence of a cytoskeletally associated PtdInsP2 pool under the control of integrin‐mediated signals that act via PIPkin C and suggest that a common, okadaic acid‐sensitive mechanism may underlie the aggregation‐dependent translocation of certain signalling molecules to the platelet cytoskeleton.

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“…The mechanisms controlling the concentration of PtdIns(4,5)P2 are not known, but, because active PtdIns4P 5kinases and PtdIns(4,5)P2 5-phosphomonoesterases may continuously 'cycle' Ptdlns(4,5)P2, they could impinge on either its synthesis or degradation; hence an increase in net synthesis could be produced by an increase in the rate of PtdIns4P 5-kinase and/or a decrease in the rate of PtdIns(4,5)P2 5-phosphomonoesterase. Suggested mechanisms for direct regulation of PtdIns4P 5-kinase include product inhibition (Van Rooijen et al, 1985;Lundberg et al, 1986), G-proteins (Smith and Chang, 1989;Wieland, 1988, 1990b), tyrosine kinases (Gaudette and Holub, 1990;Payrastre et al, 1990) and translocation to the cytoskeleton or to receptors (Cochet et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

Monoclonal antibodies to phosphatidylinositol 4-phosphate 5-kinase: distribution and intracellular localization of the C isoform

Brooksbank¹,

Butcher

Irvine³

et al. 1993

Biochemical Journal

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We have raised a panel of monoclonal antibodies to PtdIns4P 5-kinase C purified from bovine brain [Divecha, Brooksbank and Irvine (1992) Biochem. J. 288, 637-642]. This panel includes antibodies which specifically recognize PtdIns4P 5-kinase C both in a native catalytically active condition, and/or when presented on Western blots. Some of the former antibodies will also inhibit PtdIns4P 5-kinase C activity. We have used the blotting antibodies to study the bovine tissue distribution of PtdIns4P 5-kinase C and its distribution in mammalian species. We have also studied its localization in Jurkat cells and found it to be predominantly bound to membranes, with only a minority localized to the cytoskeleton. Neither PtdIns4P 5-kinase activity nor PtdIns4P 5-kinase C, as detected by Western blotting, were increased in the cytoskeleton after stimulation of Jurkat cells with OKT3. These antibodies should prove to be extremely useful tools with which to study the regulation of PtdIns4P 5-kinase C.

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Inhibition of phosphatidylinositol-4-phosphate kinase by its product phosphatidylinositol-4,5-bisphosphate

Cited by 54 publications

References 13 publications

Carbamoylcholine regulation of polyphosphoinositide synthesis and hydrolysis in cultured, dispersed, digitonin-permeabilized mouse pancreatic islet cells

Carbamoylcholine regulation of polyphosphoinositide synthesis and hydrolysis in cultured, dispersed, digitonin-permeabilized mouse pancreatic islet cells

Aggregation-dependent, integrin-mediated increases in cytoskeletally associated PtdInsP2 (4,5) levels in human platelets are controlled by translocation of PtdIns 4-P 5-kinase C to the cytoskeleton.

Monoclonal antibodies to phosphatidylinositol 4-phosphate 5-kinase: distribution and intracellular localization of the C isoform

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