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  • 2000-2004  (1)
  • 1995-1999  (1)
  • thrombin  (2)
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  • 1
    Digitale Medien
    Digitale Medien
    Activation of rat mast cells upon stimulation of protease-activated receptor (PAR-1) (2000)
    Springer
    Bulletin of experimental biology and medicine 129 (2000), S. 314-317 
    Details
    ISSN: 1573-8221
    Schlagwort(e): mast cells ; proteolytically cleaved receptor ; thrombin ; β-hexosaminidase ; heparin
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Abstract In vivo experiments on the model of wound healing showed that thrombin and thrombin receptor agonist TRAP-6 stimulated heparin secretion by mast cells in rat subcutaneous fat: the saturation of mast cells with heparin decreased, while degranulation and granulolysis increased.In vitro studies showed that TRAP-6 caused a dose-dependent release of β-hexosaminidase from peritoneal mast cells. TRAP-6 also induced heparin release from these cells and inhibition of amidase activity of thrombin. Heparin released from mast cells had low anticoagulant activity. These data suggest that activation of mast cells with thrombin is mediated by PAR-1.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02439253
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Synthetic analog of the thymosinα1 fragment 24–28 alters the coagulating and aggregating activities of α-thrombin (1995)
    Springer
    Bulletin of experimental biology and medicine 120 (1995), S. 671-674 
    Details
    ISSN: 1573-8221
    Schlagwort(e): thrombin ; thymosin ; platelets ; blood coagulation
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Abstract A pentapeptide (EEAEN), which is the 24–28 fragment of the COOH-terminal sequence in the thymosinα1 molecule highly homologous with the 54–58 region of hirudin (with the complementary anion-binding exosite in the thrombin molecule), was synthesized by a solid-phase method. Preincubation of α-thrombin with EEAEN in concentrations of 0.1 pM to 1 nM reduced its clotting activity while preincubation of this enzyme with EEAEN in concentrations of 0.01 to 1 nM reduced its platelet-aggregating activity. The reaction of EEAEN with thrombin is shown to be similar to the reaction of the entire thymosinα1 molecule. It is concluded that the COOH-terminal thymosinα1 peptide EEAEN may be the reactive site responsible for the antithrombin activity of thymosinα1.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF02444656
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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    Artikel (Nationallizenzen)
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