The possible involvement of protein phosphatase 1 in thrombin‐induced Ca2+ influx of human platelets
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Summary
The results suggest that the anti‐platelet effects of phosphatase inhibitors are due to the inhibition of Ca2+ influx and that proteinosphatase 1 plays a key role in the regulation of receptor operated Ca2- channel of human platelets.
- Type
- article
- Published
- 1993-04-01
- Cited by
- 15
- References
- 19
- OpenAlex
- https://openalex.org/W1513288562
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:25569345
Keywords
Okadaic acid, Phosphatase, Thrombin, EGTA, Platelet
References
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- The lumi-aggregometer: a new instrument for simultaneous measurement of secretion and aggregation by platelets.
- Electrophysiological evidence that glycoprotein IIb-IIIa complex is involved in calcium channel activation on human platelet plasma membrane.
- Ligand inhibition of the platelet glycoprotein IIb-IIIa complex function as a calcium channel in liposomes.
- Inositol phosphates and Ca2+ entry: toward a proliferation or a simplification?
- Use of manganese to discriminate between calcium influx and mobilization from internal stores in stimulated human neutrophils.
- Platelets and parotid acinar cells have different mechanisms for agonist-stimulated divalent cation entry.
- Changes in the platelet membrane glycoprotein IIb.IIIa complex during platelet activation.
- Inhibitory effect of a marine-sponge toxin, okadaic acid, on protein phosphatases. Specificity and kinetics.
- Calcium-independent activation of contractile apparatus in smooth muscle by calyculin-A.
- A novel protein phosphatase inhibitor, tautomycin Effect on smooth muscle
- Absence of (-) [3H]desmethoxyverapamil binding sites on human platelets and lack of evidence for voltage-dependent calcium channels.
- Thrombin-induced activation of calcium transport pathways and their role in platelet functions.
- Thrombin and ionomycin can raise platelet cytosolic Ca2+ to micromolar levels by discharge of internal Ca2+ stores: studies using fura-2.
- Thrombin-induced effects are selectively inhibited following treatment of intact human platelets with okadaic acid.
- Agonists stimulate divalent cation channels in the plasma membrane of human platelets
- Calcium channels in thrombin-activated human platelet membrane
- Platelet glycoproteins IIb and IIIa as a calcium channel in liposomes.
- Role of the glycoprotein IIb-IIIa complex in plasma membrane Ca2+ transport: a comparison of results obtained with platelets and human erythroleukemia cells.
Cited by
- Protein Phosphatase Inhibitors Exert Specific and Nonspecific Effects on Calcium Influx in Thapsigargin-Treated human Neutrophils
- N-Acetylsphingosine (C-ceramide) Inhibited Neutrophil Superoxide Formation and Calcium Influx (*)
- Immunolocalization of protein phosphatase type 1 in Paramecium cells using antibodies against recombinant protein and peptides.
- Characterization of a potent platelet aggregation inducer from Cerastes cerastes (Egyptian sand viper) venom.
- The involvement of protein phosphatases in platelet activation.
- Protein kinase C inhibits the transplasma membrane influx of Ca2+ triggered by 4-aminopyridine in Jurkat T lymphocytes.
- Aggregation-dependent signaling in human platelets is sensitive to protein serine/threonine phosphatase inhibitors.
- Phosphatase inhibitors suppress Ca2+ influx induced by receptor-mediated intracellular Ca2+ store depletion in human platelets.
- C6-ceramide maintains elevated cytosolic calcium levels in activated platelets.
- Platelet talin is phosphorylated by calyculin A
- Inhibition of Protein Phosphatase 1 Stimulates Secretion of Alzheimer Amyloid Precursor Protein
- The Phosphatase Inhibitor Calyculin-A Impairs Clot Retraction, Platelet Activation, and Thrombin Generation
- Protein phosphatase 1 in tumorigenesis: Is it worth a closer look?
- Protein Phosphatases in Platelet Function
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- Okadaic acid and microcystin-LR directly inhibit the methylation of protein phosphatase 2A by its specific methyltransferase.
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- Photoaffinity labeling of protein phosphatase 2A, the receptor for a tumor promoter okadaic acid, by [27-3H]methyl 7-O-(4-azidobenzoyl)okadaate.
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