Thrombin stimulates the intracellular relocation of annexin V in human platelets.
Annexins are a family of proteins that have been implicated in a range of intracellular processes. In this paper we confirm the existence of annexin V in human platelets (0.02 +/- 0.005% of cell protein). We also demonstrate that 13.7 +/- 6.8% of intracellular annexin V becomes tightly associated with membranes in response to platelet activation by the physiological agonist thrombin and requires non-ionic detergent for solubilization. Thrombin stimulation also induces the association of annexin V (11.0 +/- 4.6% of the total) with the membrane in a manner which requires prolonged treatment with EGTA for its release from the membrane.
Department of Biochemistry and Molecular Biology, University of Leeds, UK.
P J
PJ
Trotter
M A
MA
Orchard
J H
JH
Walker
D017304:Annexin A5 / Q000378:metabolism*; D001792:Blood Platelets / Q000187:drug effects* / Q000378:metabolism; D004533:Egtazic Acid; D006801:Humans; D015539:Platelet Activation; D013347:Subcellular Fractions; D013917:Thrombin / Q000494:pharmacology*
D017304:Annexin A5; D004533:Egtazic Acid; D013917:Thrombin