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Titolo:
Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: Implications for platelet secretion
Autore:
Reed, GL; Houng, AK; Fitzgerald, ML;
Indirizzi:
Harvard Univ, Sch Publ Hlth, Cardiovasc Biol Lab, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 ardiovasc Biol Lab, Boston, MA 02115 USA Massachusetts Gen Hosp, Cardiac Unit, Boston, MA 02114 USA Massachusetts Gen Hosp Boston MA USA 02114 iac Unit, Boston, MA 02114 USA
Titolo Testata:
BLOOD
fascicolo: 8, volume: 93, anno: 1999,
pagine: 2617 - 2626
SICI:
0006-4971(19990415)93:8<2617:HPCSPA>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
GRANULE MEMBRANE-PROTEIN; SYNAPTIC VESICLE DOCKING; PLASMA-MEMBRANE; BINDING PROTEIN; KINASE-C; PHORBOL ESTERS; YEAST SEC1; CELL-LINE; IDENTIFICATION; RADIOIMMUNOASSAY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Reed, GL Harvardon,iv, Sch Publ Hlth, Cardiovasc Biol Lab, 677 HungtingtonAve, Bost Harvard Univ 677 Hungtington Ave Boston MA USA 02115 on Ave, Bost
Citazione:
G.L. Reed et al., "Human platelets contain SNARE proteins and a Sec1p homologue that interacts with syntaxin 4 and is phosphorylated after thrombin activation: Implications for platelet secretion", BLOOD, 93(8), 1999, pp. 2617-2626

Abstract

In response to thrombin and other extracellular activators, platelets secrete molecules from large intracellular vesicles (granules) to initiate thrombosis. Little is known about the molecular machinery responsible for vesicle docking and secretion in platelets and the linkage of that machinery to cell activation. We found that platelet membranes contain a full complementof interacting proteins-VAMP, SNAP-25, and syntaxin 4-that are necessary for vesicle docking and fusion with the plasma membrane. Platelets also contain an uncharacterized homologue of the Sec1p family that appears to regulate vesicle docking through its binding with a cognate syntaxin. This platelet Sec1 protein (PSP) bound to syntaxin 4 and thereby excluded the binding of SNAP-25 with syntaxin 4, an interaction critical to vesicle docking. As predicted by its sequence, PSP was detected predominantly in the platelet cytosol and was phosphorylated in vitro by protein kinase C (PKC), a secretion-linked kinase, incorporating 0.87 +/- 0.11 mol of PO4 per mole of protein. PSP was also specifically phosphorylated in permeabilized platelets after cellular stimulation by phorbol esters or thrombin and this phosphorylation was blocked by the PKC inhibitor Ro-31-8220. Phosphorylation by PKC in vitro inhibited PSP from binding to syntaxin 4. Taken together, these studies indicate that platelets, like neurons and other cells capable of regulated secretion, contain a unique complement of interacting vesicle docking proteins and PSP, a putative regulator of vesicle docking. The PKC-dependent phosphorylation of PSP in activated platelets and its inhibitory effects on syntaxin 4 binding provide a novel functional link that may be important incoupling the processes of cell activation, intracellular signaling, and secretion. (C) 1999 by The American Society of Hematology.

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Documento generato il 06/06/20 alle ore 00:39:31