Roles of phospholipase C and Ca(2+)-ATPase in calcium responses of single, fibrinogen-bound platelets.

Heemskerk, Johan W. M.; Vis, Piet; Feijge, Marion A.H.; Hoyland, John S.; Mason, William T.; Sage, Stewart O.

doi:10.1016/s0021-9258(18)54158-2

Cited by 80 publications

(14 citation statements)

References 42 publications

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“…These findings suggest a mechanism by which high concentrations of intracellular IP 3 can cause cells to maintain an elevated level of [Ca 2ϩ ] i . Indeed, this may explain the occurrence of sustained [Ca 2ϩ ] i elevations at high agonist concentrations (Jacob et al, 1988;Wakui et al, 1989;Heemskerk et al, 1993) and when cells are dialyzed with high concentrations of the nonmetabolized IP 3 analogue inositol 1,4,5 trisphosphorothioate (Petersen et al, 1991). Our findings also suggest a possible mechanism for the regulation of the frequency of [Ca 2ϩ ] i oscillations in cells containing IP 3sensitive Ca 2ϩ stores.…”

Section: Discussionsupporting

confidence: 52%

“…The frequency and amplitude of [Ca 2 ϩ ] i oscillations are essential for initiating numerous cellular processes, including selective stimulation of gene expression (Dolmetsch et al, 1998;Li et al, 1998) and the activation of specific enzymes (De Koninck and Schulman, 1998). It has been observed that as the concentration of agonist is increased [Ca 2 ϩ ] i oscillations increase in frequency, eventually becoming a sustained [Ca 2 ϩ ] i elevation (Jacob et al, 1988;Wakui et al, 1989;Heemskerk et al, 1993). A similar phenomenon has also been seen when cells are dialyzed with increasing concentrations of the nonmetabolized IP 3 analogue, inositol 1,4,5 trisphosphorothioate (Petersen et al, 1991).…”

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confidence: 99%

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Dual Regulation of Calcium Mobilization by Inositol 1,4,5-Trisphosphate in a Living Cell

Tertyshnikova

Fein

2000

The Journal of General Physiology

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Changes in cytosolic free calcium ([Ca2+]i) often take the form of a sustained response or repetitive oscillations. The frequency and amplitude of [Ca2+]i oscillations are essential for the selective stimulation of gene expression and for enzyme activation. However, the mechanism that determines whether [Ca2+]i oscillates at a particular frequency or becomes a sustained response is poorly understood. We find that [Ca2+]i oscillations in rat megakaryocytes, as in other cells, results from a Ca2+-dependent inhibition of inositol 1,4,5-trisphosphate (IP3)–induced Ca2+ release. Moreover, we find that this inhibition becomes progressively less effective with higher IP3 concentrations. We suggest that disinhibition, by increasing IP3 concentration, of Ca2+-dependent inhibition is a common mechanism for the regulation of [Ca2+]i oscillations in cells containing IP3-sensitive Ca2+ stores.

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Section: Discussionsupporting

confidence: 52%

mentioning

confidence: 99%

Dual Regulation of Calcium Mobilization by Inositol 1,4,5-Trisphosphate in a Living Cell

Tertyshnikova

Fein

2000

The Journal of General Physiology

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“…Although the involvement of intracellular Ca# + pools in platelet Ca# + signalling is well established, much less is known about their identification and respective roles during cell life [1][2][3]. At least two types of intracellular Ca# + pool are described : inositol 1,4,5trisphosphate (IP $ )-sensitive Ca# + pools and IP $ -insensitive Ca# + pools [4][5][6][7][8]. A new rationale for these distinct roles of multiple Ca# + pools has come from evidence for a plurality of sarco\ endoplasmic reticulum Ca# + ATPases (SERCAs), which take up Ca# + into Ca# + pools.…”

Section: Introductionmentioning

confidence: 99%

Platelet sarco/endoplasmic reticulum Ca2+ATPase isoform 3b and Rap 1b: interrelation and regulation in physiopathology

Lacabaratz

Corvazier

Kovàcs³

et al. 1998

Biochemical Journal

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Platelet Ca2+ signalling involves intracellular Ca2+ pools, whose content is controlled by sarco/endoplasmic reticulum Ca2+ATPases (SERCAs). Among these, a key role is played by the inositol trisphosphate-sensitive Ca2+ pool, associated with the SERCA 3b isoform. We have investigated the control of this Ca2+ pool through the cAMP-dependent phosphorylation of the GTP-binding protein, Rap (Ras-proximate) 1b. We first looked for this Ca2+ pool target of regulation by studying the expression of the different SERCA and Rap 1 proteins in human platelets and various cell lines, by Western blotting and reverse transcription-PCR. Since co-expression of Rap 1b and SERCA 3b was obtained, we looked for their protein-protein interaction as a function of the cAMP-dependent phosphorylation of Rap 1b. Co-immunoprecipitations of SERCA 3b and Rap 1b proteins were found in the absence of phosphorylation, induced by the catalytic subunit of the cAMP-dependent protein kinase (csPKA). In contrast, upon pre-treatment of platelet membranes with csPKA, the SERCA 3b dissociated from the Rap 1b protein, in agreement with a role of its phosphorylated state in their interaction. Finally, we looked for adaptation of this complex in a platelet pathological model of hypertension. We investigated the expression of both proteins, as well as the cAMP-dependent phosphorylation of Rap 1b and SERCA 3b activity in platelets from control normotensive Wistar-Kyoto rats and from spontaneously hypertensive rats (SHRs). A decrease in SERCA 3b activity was associated with a decrease in Rap 1b endogenous phosphorylation in SHR platelets, consistent with a functional role in the regulation of the SERCA 3b-associated Ca2+ pool.

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“…: ::::.:.:.:. Figure 4 Comparative Rapi protein phosphorylation, expression and effect of C. Sub. on Ca2+ uptake In platelet membranes isolated from a normal individual and a patient with severe heart failure Mixed platelet membrane fractions (100000 g pellet) were isolated from a normal individual and from a patient with severe congestive heart failure.…”

Section: Relationship Between Platelet Ca2+ Transport and Rapl Protein Phosphorylation Effect Of C Sub Dialysismentioning

confidence: 99%

“…Activation of platelets by different physiological stimuli induces transduction signalling processes resulting in an increase in cytosolic Ca2+ concentration. This occurs by two phenomena: Ca2+ influx from extracellular medium through calcium channels and release of Ca2+ ions from intracellular Ca2+ storage pools including an inositol 1,4,5trisphosphate (InsP3)-sensitive Ca2+ pool and/or an InsP3insensitive Ca2+ pool [1][2][3][4].…”

Section: Introductionmentioning

confidence: 99%

Relationship between Rap1 protein phosphorylation and regulation of Ca2+ transport in platelets: a new approach

Magnier

Corvazier

Aumont

et al. 1995

Biochemical Journal

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Although the interrelationship between the two messengers Ca2+ and cyclic AMP in platelet function is well documented, its mechanism of action still remains to be established. We investigated here the question of the regulation of platelet Ca(2+)-ATPases by cyclic AMP through the phosphorylation of the Rap1 protein using a pathological model. We first found experimental conditions where Ca(2+)-transport by platelet membrane vesicles appeared to be dependent on the phosphorylation of the Rap1 protein. Then, we studied platelets of patients with congestive heart failure for their expression of the potential 97 kDa Ca(2+)-ATPase target of regulation through the Rap1 protein as well as the phosphorylation of the Rap1 protein using the catalytic subunit of the cyclic AMP-dependent protein kinase (C. Sub.). In the first patients studied, we found no significant modification in the expression of the 97 kDa Ca(2+)-ATPase by Western blotting using the PL/IM 430 monoclonal antibody which specifically recognized this isoform. In contrast, the Rap1 protein was differentially phosphorylated when using 15 micrograms/ml of the C. Sub. These results allowed us to use these pathological platelets to study the relationship between the expression of Rap1 protein and the regulation of Ca2+ transport by selecting a patient with severe heart failure. We could show a decrease in the expression as well as in the phosphorylation of Rap1 protein and demonstrate a lower effect of C. Sub. on Ca2+ transport. Finally, by studying a further series of patients, we could confirm that the decrease in Rap1 protein expression in heart failure, whatever its extent, was variable, and could strictly correlate the expression of Rap1 protein with the stimulatory effect of C. Sub. on Ca2+ transport. Besides the evidence for regulation of the expression of the Rap1 protein in platelets from patients with heart failure, these findings constitute a new approach in favour of the regulation of platelet Ca2+ transport through the phosphorylation of the Rap1 protein.

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Roles of phospholipase C and Ca(2+)-ATPase in calcium responses of single, fibrinogen-bound platelets.

Cited by 80 publications

References 42 publications

Dual Regulation of Calcium Mobilization by Inositol 1,4,5-Trisphosphate in a Living Cell

Dual Regulation of Calcium Mobilization by Inositol 1,4,5-Trisphosphate in a Living Cell

Platelet sarco/endoplasmic reticulum Ca2+ATPase isoform 3b and Rap 1b: interrelation and regulation in physiopathology

Relationship between Rap1 protein phosphorylation and regulation of Ca2+ transport in platelets: a new approach

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