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Thrombin stimulates proliferation of cultured rat aortic smooth muscle cells by a proteolytically activated receptor.
- C. McNamara, I. Sarembock, L. Gimple, J. Fenton, S. Coughlin, G. Owens
- Biology, MedicineThe Journal of clinical investigation
It is demonstrated that alpha-thrombin stimulates SMC proliferation via the proteolytic activation of a receptor very similar or identical to that previously identified, and thrombin-induced proliferation was dependent on enzymatic activity.
Thrombin-induced expression of endothelial P-selectin and intercellular adhesion molecule-1: a mechanism for stabilizing neutrophil adhesion
- Y. Sugama, C. Tiruppathì, K. offakidevi, T. Andersen, J. Fenton, A. Malik
- Biology, MedicineThe Journal of cell biology
- 2 November 1992
Thrombin-induced endothelial adhesivity involves early- and late-phase responses, and the initial reversible PMN adhesion is mediated by rapid P-selectin expression via TRP-14 generation, which enables the interaction of ICAM-1 with the CD18 beta 2 integrin on PMN.
The structure of a complex of recombinant hirudin and human alpha-thrombin.
The crystallographic structure of a recombinant hirudin-thrombin complex has been solved at 2.3 angstrom (A) resolution and abundant interactions may account for the high affinity and specificity of hirUDin.
Thrombin induces IL-6 production in fibroblasts and epithelial cells. Evidence for the involvement of the seven-transmembrane domain (STD) receptor for alpha-thrombin.
- L. Sower, C. Froelich, D. Carney, J. Fenton, G. Klimpel
- Biology, MedicineJournal of immunology
- 15 July 1995
The results suggest that fibroblasts and epithelial cells may represent a significant source of IL-6 in the inflammatory response to tissue injury, and that cytokine production is an important biologic consequence of thrombin's interaction with its seven-transmembrane domain (STD) receptor.
Thrombin‐induced chemotaxis and aggregation of neutrophils
- R. Bizios, L. Lai, J. Fenton, A. Malik
- Biology, MedicineJournal of cellular physiology
- 1 September 1986
The results suggest that thrombin‐induced neutrophil chemotaxis and aggregation are mediated by different mechanisms, sinceChemotaxis is a catalytically independent response whereas aggregation is an active site independent response.
Thrombin promotes activation of matrix metalloproteinase-2 produced by cultured vascular smooth muscle cells.
- Z. Galis, R. Kranzhöfer, J. Fenton, P. Libby
- Biology, MedicineArteriosclerosis, thrombosis, and vascular…
- 1 March 1997
The results suggest that at sites of vascular injury, thrombin may activate locally produced MMP-2 and thereby facilitate cell migration and proliferation and promote plaque instability by increasing local matrix-degrading activity.
Isoproterenol reduces thrombin-induced pulmonary endothelial permeability in vitro.
- F. Minnear, M. Demichele, D. Moon, C. Rieder, J. Fenton
- Chemistry, MedicineThe American journal of physiology
- 1 November 1989
It is suggested that isoproterenol can reduce the thrombin-induced increase in endothelial permeability in vitro by directly maintaining actin filaments and the shape of endothelial cells.
Human thrombins. Production, evaluation, and properties of alpha-thrombin.
- J. Fenton, M. Fasco, A. B. Stackrow
- Medicine, ChemistryThe Journal of biological chemistry
- 10 June 1977
Human thrombin generated by Taipan snake venom activation was compared with that produced by rapid thromboplastin activation and both throm bins migrated at the same rate during electrophoresis in SDS; identical pairs of NH2-terminal residues were released in three consecutive Edman degradation cycles.
Monocyte chemotaxis: stimulation by specific exosite region in thrombin.
Findings indicate that the regions in thrombin responsible for monocyte chemotaxis are proximate to those involved in certain protein recognition interactions of alpha-thrombin but are distinct from the catalytic site and from certain exosites required for clotting.
Function of glycoprotein Ib alpha in platelet activation induced by alpha-thrombin.
- L. De Marco, M. Mazzucato, A. Masotti, J. Fenton, Z. Ruggeri
- Chemistry, MedicineThe Journal of biological chemistry
- 15 December 1991
There is a correlation between occupancy of the high affinity sites for alpha-thrombin on GP Ib alpha and platelet activation, secretion, and aggregation, suggesting that GP Ibalpha is part of an alpha- Thrombin receptor relevant for platelet function.