title: PI3 kinase-dependent stimulation of platelet migration by stromal cell-derived factor 1 (SDF-1).
abstract: Platelets have been regarded as static cells that do not move once they adhere to a matrix. The present study explored, whether platelets are able to migrate. In contrast to the current opinion, we found that platelets were mobile, able to migrate over a surface, and transmigrate through a transwell membrane and endothelium toward a source of stromal cell-derived factor 1 (SDF-1). Platelet migration was stimulated by SDF-1, which led to the downstream activation and phosphorylation of Wiskott-Aldrich syndrome protein. SDF-1 signaling and subsequent platelet migration could be inhibited by CXCR4-receptor blocker AMD3100, pertussis toxin, inhibition of phosphoinositol 3-kinase (PI3 kinase) with LY294002 or wortmannin, and disruption of actin polymerization with cytochalasin B. The potential of platelets to migrate in an SDF-1-mediated fashion may redefine the role of platelets in the pathophysiology of vascular inflammation, subsequent atherosclerotic degeneration, and vascular regeneration.
authors.affiliation: Abteilung III, Kardiologie und Kreislauferkrankungen, Medizinische Klinik, Universitätsklinikum Tübingen, Otfried-Müller-Strasse 10, 72076, Tübingen, Germany.
authors.forename: Bjoern F
authors.initials: BF
authors.lastname: Kraemer
authors.forename: Oliver
authors.initials: O
authors.lastname: Borst
authors.forename: Eva-Maria
authors.initials: EM
authors.lastname: Gehring
authors.forename: Tanja
authors.initials: T
authors.lastname: Schoenberger
authors.forename: Benjamin
authors.initials: B
authors.lastname: Urban
authors.forename: Elena
authors.initials: E
authors.lastname: Ninci
authors.forename: Peter
authors.initials: P
authors.lastname: Seizer
authors.forename: Christine
authors.initials: C
authors.lastname: Schmidt
authors.forename: Boris
authors.initials: B
authors.lastname: Bigalke
authors.forename: Miriam
authors.initials: M
authors.lastname: Koch
authors.forename: Ivo
authors.initials: I
authors.lastname: Martinovic
authors.forename: Karin
authors.initials: K
authors.lastname: Daub
authors.forename: Tobias
authors.initials: T
authors.lastname: Merz
authors.forename: Laura
authors.initials: L
authors.lastname: Schwanitz
authors.forename: Konstantinos
authors.initials: K
authors.lastname: Stellos
authors.forename: Fabienne
authors.initials: F
authors.lastname: Fiesel
authors.forename: Martin
authors.initials: M
authors.lastname: Schaller
authors.forename: Florian
authors.initials: F
authors.lastname: Lang
authors.forename: Meinrad
authors.initials: M
authors.lastname: Gawaz
authors.forename: Stephan
authors.initials: S
authors.lastname: Lindemann
mesh_terms: D000818:Animals; D001792:Blood Platelets / Q000166:cytology* / Q000187:drug effects / Q000201:enzymology*; D001808:Blood Vessels / Q000187:drug effects / Q000473:pathology; D002465:Cell Movement / Q000187:drug effects*; D054377:Chemokine CXCL12 / Q000494:pharmacology*; D002633:Chemotaxis / Q000187:drug effects; D003094:Collagen / Q000494:pharmacology; D004727:Endothelium / Q000187:drug effects / Q000378:metabolism; D005340:Fibrinogen / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000378:metabolism; D006801:Humans; D007511:Ischemia / Q000473:pathology; D051379:Mice; D008810:Mice, Inbred C57BL; D019869:Phosphatidylinositol 3-Kinases / Q000378:metabolism*; D010766:Phosphorylation / Q000187:drug effects; D016062:Porosity / Q000187:drug effects; D019718:Receptors, CXCR4 / Q000378:metabolism; D051316:Wiskott-Aldrich Syndrome Protein / Q000378:metabolism
chemical_list: D054377:Chemokine CXCL12; D019718:Receptors, CXCR4; D051316:Wiskott-Aldrich Syndrome Protein; D005340:Fibrinogen; D003094:Collagen; D019869:Phosphatidylinositol 3-Kinases; D019204:GTP-Binding Proteins