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PubMed · 3010667

Platelet protein phosphorylation.

J M Gerrard·L L Friesen·J M McCrea·S J Israels·P Robinson
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Abstract

As can be seen from this review, protein phosphorylation appears involved in both positive and negative regulation of platelets. To date, good evidence has been presented for the involvement of protein phosphorylation in the regulation of granule centralization (i.e. myosin light chain phosphorylation). It is probable that protein phosphorylation may also be involved in granule labilization, pseudopod formation and ATP synthesis. Protein phosphorylation in association with platelet activation appears mediated through calcium flux, in the case of myosin light chain phosphorylation, and through diglyceride or other substances in the case of 47P phosphorylation. A summary scheme is shown in Figure 1.

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Actin CytoskeletonBlood PlateletsBlood ProteinsCalciumCarrier ProteinsCyclic AMPCytoplasmic GranulesCytoskeletonDiglyceridesGelsolinHumansInositol 1,4,5-TrisphosphateInositol PhosphatesLysophospholipidsMicrofilament ProteinsMicrotubulesMolecular WeightMyosinsPhosphatidic AcidsPhosphoproteinsPhosphorylationPlatelet Activating FactorPlatelet AggregationProtein Kinase CTetradecanoylphorbol AcetateThromboxane A2Journal ArticleResearch Support, Non-U.S. Gov'tReview

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J M Gerrard, L L Friesen, J M McCrea, S J Israels, P Robinson. 1985. Platelet protein phosphorylation.. https://doi.org/10.1007/978-1-4615-9442-0_17

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