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 journal › Article (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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