Effects of human mast cell tryptase on the kinetics of blood clotting

Thrombosis Research

Volumn 109, Issue 2-3, 2003, Pages 153-156

  Samoszuk, Michael ^a   Corwin, Mark ^a   Hazen, Stanley L ^b  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b LERNER RESEARCH INSTITUTE   (United States)

Author keywords

Heparin; Mast cell; Thromboelastography; Tryptase

Indexed keywords

HEPARIN; PLASMINOGEN ACTIVATOR; TRYPTASE;

ANTICOAGULATION; ARTICLE; BLEEDING; BLOOD CLOTTING; CORRELATION ANALYSIS; ENZYME ACTIVITY; HEMATOLOGIC DISEASE; HUMAN; KINETICS; MAST CELL; NORMAL HUMAN; PRIORITY JOURNAL;

EID: 0037464817     PISSN: 00493848     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0049-3848(03)00150-6     Document Type: Article

References (18)

1. Smith T.F., Welch T.R., Allen J.B., Sondheimer J.M. Cutaneous mastocytosis with bleeding: probable heparin effect. Cutis. 39:1987;241-244.
2. Kauhanen P., Kovanen P.T., Reunala T., Lassila R. Effects of skin mast cells on bleeding time and coagulation activation at the site of platelet plug formation. Thromb. Haemost. 79:1998;843-847.
3. Valent P., Baghestanian M., Bankl H.C., Sillaber C., Sperr W.R., Wojta J.et al. New aspects in thrombosis research: possible role of mast cells as profibrinolytic and antithrombotic cells. Thromb. Haemost. 87:2002;786-790.
4. Schwartz L.B. Tryptase, a mediator of human mast cells. J. Allergy Clin. Immunol. 86:1990;594-598.
5. Schwartz L.B., Bradford T.R. Regulation of tryptase from human lung mast cells by heparin. J. Biol. Chem. 261:1986;7372-7379.
6. Hallgren J., Spillman D., Pejler G. Structural requirements and mechanism for heparin-induced activation of a recombinant mouse mast cell tryptase, mouse mast cell protease-6. J. Biol. Chem. 276:2001;42774-42781.
7. Huang C., Wong G.W., Ghildyal N., Gurish M.F., Sali A., Matsumoto R.et al. The tryptase, mouse mast cell protease 7, exhibits anticoagulant activity in vivo and in vitro due to its ability to degrade fibrinogen in the presence of the diverse array of protease inhibitors in plasma. J. Biol. Chem. 272:1997;31885-31893.
8. Thomas V.A., Wheeless C.J., Stack M.S., Johnson D.A. Human mast cell tryptase fibrinogenolysis: kinetics, anticoagulation mechanism, and cell adhesion disruption. Biochemistry. 37:1998;2291-2298.
9. Cohen E., Caprini J., Zuckerman I., Vagher P., Robinosn B. Evaluation of three methods used to evaluate accelerated coagulability. Thromb. Res. 10:1977;587-604.
10. Caprini J.A., Zuckerman I., Cohen E., Vagher J.P., Lipp V. The identification of accelerated coagulability. Thromb. Res. 9:1976;167-180.
11. Caprini J.A., Arcelus J.I., Laubach M., Size G., Hoffman K.N., Coats R.W.et al. Postoperative hypercoagulability and deep-vein thrombosis after laparoscopic cholecystectomy. Surg. Endosc. 9:1995;304-309.
12. Schwartz L.B. Tryptase: a mast cell serine protease. Methods Enzymol. 244:1994;88-100.
13. Schwartz L.B., Bradford T.R., Littman B.H., Wintroub B.U. The fibrinogenolytic activity of purified tryptase from human lung mast cells. J. Immunol. 135:1985;2762-2767.
14. Hatanaka K., Minamiyama M., Tanaka K., Taguchi T., Tajima S., Kitamura Y.et al. High susceptibility to ADP-induced thrombus formation in mast cell-deficient W/Wv mice. Thromb. Res. 40:1985;453-464.
15. Kitamura Y., Taguchi T., Yokoyama M.et al. Higher susceptibility of mast-cell-deficient W/WV mutant mice to brain thromboembolism and mortality caused by intravenous injection of India ink. Am. J. Pathol. 122:1986;469-480.
16. Kauhanen P., Kovanen P.T., Reunala T., Lassila R. Effects of skin mast cells on bleeding time and coagulation activation at the site of platelet plug formation. Thromb. Haemost. 79:1998;843-847.
17. Cirino G., Cicala C., Bucci M., Sorrentino L., Ambrosini G., DeDominicis G.et al. Factor Xa as an interface between coagulation and inflammation. Molecular mimicry of factor Xa association with effector cell protease receptor-1 induces acute inflammation in vivo. J. Clin. Invest. 99:1997;2446-2451.
18. Dugina T.N., Kiseleva E.V., Chistov I.V., Umarova B.A., Strukova S.M. Receptors of the PAR family as a link between blood coagulation and inflammation. Biochemistry. 67:2002;65-84.