Zobrazeno 1 - 10
of 29
pro vyhledávání: '"M C Bourin"'
Publikováno v:
Journal of Biological Chemistry. 265:15424-15431
Previous studies on rabbit thrombomodulin (TM) re- vealed that certain anticoagulant activities expressed by TM depend on the presence of an acidic domain tentatively identified as a sulfated galactosaminogly- can (Bourin, M.-C., dhlin, A.-K., Lane,
Autor:
M C Bourin, Ulf Lindahl
Publikováno v:
Biochemical Journal. 270:419-425
Thrombomodulin (TM), a major anticoagulant protein at the vessel wall, serves as a potent cofactor for the activation of Protein C by thrombin. Previous work has indicated that (rabbit) TM is a proteoglycan that contains a single polysaccharide chain
Autor:
M.-C. Bourin, B. Crozatier, Fabiola León-Velarde, Jean-Paul Richalet, K. Mohammadi, R. Germack
Publikováno v:
Scopus-Elsevier
Norepinephrine (NE)-induced desensitization of the adrenergic receptor pathway may mimic the effects of hypoxia on cardiac adrenoceptors. The mechanisms involved in this desensitization were evaluated in male Wistar rats kept in a hypobaric chamber (
Autor:
K, Monory, M C, Bourin, M, Spetea, C, Tömböly, G, Tóth, H W, Matthes, B L, Kieffer, J, Hanoune, A, Borsodi
Publikováno v:
The European journal of neuroscience. 12(2)
The recently discovered endomorphin 1 (Tyr-Pro-Trp-Phe-NH2) and endomorphin 2 (Tyr-Pro-Phe-Phe-NH2) were investigated with respect to their direct receptor-binding properties, and to their ability to activate G proteins and to inhibit adenylyl cyclas
Lack of acidic fibroblast growth factor activation by heparan sulfate species from diabetic rat skin
Autor:
M C, Bourin
Publikováno v:
Glycoconjugate journal. 14(4)
The glucosaminoglycans isolated from the skin of control and streptozotocin-diabetic rats were fractionated on ion-exchange chromatography into a heparan sulfate (HS)-like and a heparin-like species. In addition, a low sulfated fraction was isolated
Autor:
M C Bourin, Ulf Lindahl
Publikováno v:
The Biochemical journal. 289
Autor:
M C, Bourin
Publikováno v:
Annales de biologie clinique. 49(4)
The endothelial cell surface receptor thrombomodulin (TM) displays various anticoagulant functions: it acts as a cofactor for the activation of protein C (PC) by thrombin, prevents the activation of fibrinogen, platelets and Factor V by thrombin. TM
Publikováno v:
The Journal of biological chemistry. 265(26)
Previous studies on rabbit thrombomodulin (TM) revealed that certain anticoagulant activities expressed by TM depend on the presence of an acidic domain tentatively identified as a sulfated galactosaminoglycan (Bourin, M.-C., Ohlin, A.-K., Lane, D.,
Autor:
M.-C. Bourin, M.-C. Boffa
Publikováno v:
Revue Francaise de Transfusion et Immuno-hématologie. 27:807-816
Publikováno v:
Journal of Biological Chemistry. 263:8044-8052
Rabbit thrombomodulin displays three distinct blood anticoagulant activities: it promotes the activation of protein C by thrombin (protein C activation cofactor activity); it promotes the inactivation of thrombin by thrombin (direct anticoagulant act