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.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Actin Cytoskeleton / physiology
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Blood Platelets / physiology*
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Blood Platelets / ultrastructure
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Blood Proteins / metabolism
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Calcium / blood
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Carrier Proteins / blood
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Cyclic AMP / pharmacology
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Cytoplasmic Granules / physiology
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Cytoskeleton / physiology
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Diglycerides / pharmacology
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Gelsolin
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Humans
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Inositol 1,4,5-Trisphosphate
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Inositol Phosphates / blood
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Lysophospholipids
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Microfilament Proteins*
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Microtubules / physiology
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Molecular Weight
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Myosins / blood
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Phosphatidic Acids / blood
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Phosphoproteins / blood*
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Phosphorylation
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Platelet Activating Factor / physiology
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Platelet Aggregation
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Protein Kinase C / blood
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Tetradecanoylphorbol Acetate / pharmacology
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Thromboxane A2 / blood
Substances
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Blood Proteins
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Carrier Proteins
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Diglycerides
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Gelsolin
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Inositol Phosphates
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Lysophospholipids
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Microfilament Proteins
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Phosphatidic Acids
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Phosphoproteins
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Platelet Activating Factor
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brevin
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platelet protein P47
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Thromboxane A2
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Inositol 1,4,5-Trisphosphate
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Cyclic AMP
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Protein Kinase C
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Myosins
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Tetradecanoylphorbol Acetate
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Calcium