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PAR-1-dependent pp60src activation is dependent on protein kinase C and increased [Ca2+]: evidence that pp60src does not regulate PAR-1-dependent Ca2+ entry in human platelets

  • M T Harper
  • , S O Sage

    Research output: Contribution to journalArticle (Academic Journal)peer-review

    22 Citations (Scopus)

    Abstract

    The role of the tyrosine kinase pp60src in PAR-1-dependent Ca2+ entry was investigated in human platelets. pp60src plays a role in thapsigargin (TG)-evoked store-operated Ca2+ entry (SOCE), which is thought to be a major component of thrombin-evoked Ca2+ entry.
    Original languageEnglish
    Pages (from-to)2695-703
    Number of pages9
    JournalJournal of Thrombosis and Haemostasis
    Volume4
    Issue number12
    DOIs
    Publication statusPublished - Dec 2006

    Keywords

    • Egtazic Acid
    • Calcium
    • Humans
    • Cytochalasin D
    • Cytoskeleton
    • Indoles
    • Blood Platelets
    • Peptide Fragments
    • Pyrimidines
    • Phosphorylation
    • Protein Kinase C
    • Time Factors
    • Calcium Signaling
    • Receptor, PAR-1
    • Carbazoles
    • Plasma Membrane Calcium-Transporting ATPases
    • Enzyme Activation
    • Enzyme Inhibitors
    • Proto-Oncogene Proteins pp60(c-src)
    • Thapsigargin
    • Phospholipid Ethers
    • Actins
    • Chelating Agents
    • Type C Phospholipases
    • Sarcoplasmic Reticulum Calcium-Transporting ATPases

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