Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us Hematol. J. (2001); 2(6):371-7 High molecular mass kininogen inhibits cathepsin G-induced platelet activation by forming a complex with cathepsin G. Selim TE, Ghoneim HR, Abdel Ghaffar HA, Colman RW, Dela Cadena RA Hematology Unit, Clinical Pathology Department, Al-Mansoura Faculty of Medicine, Al-Mansoura, Egypt. Abstract: INTRODUCTION: Preliminary studies have shown that high molecular mass kininogen (HK) inhibits cathepsin G-induced platelet activation. However, the potential mechanism underlying this inhibitory effect remains to be elucidated. MATERIALS AND METHODS: Suspensions of washed and gel-filtered platelets were used in radioligand binding and aggregation studies. The amidolytic activity of cathepsin G was measured using specific chromogenic substrate. Western blot technique was utilised to explore the potential complex formation between cathepsin G and HK. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis was used to analyse the cleavage products of HK. RESULTS: At a concentration of 1 microM, HK completely blocked cathepsin G-induced platelet shape change and secretion of ATP. HK inhibited cathepsin G-induced platelet aggregation in a concentration-dependent manner with an IC(50) of 0.48 microM. Moreover, HK was found to inhibit binding of (125)I-cathepsin G to gel-filtered platelets. (125)I-cathepsin G forms a complex with HK. The complex formation did not affect the amidolytic activity of cathepsin G. HK was proteolysed upon interaction with cathepsin G. CONCLUSION: Our results show that high molecular mass kininogen down-regulates cathepsin G-induced platelet activation by forming a complex with cathepsin G and thus prevents binding of cathepsin G to platelets. These kininogen-cathepsin G interactions may be potential targets for pharmacological intervention. [PUBMED: 11920276] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.