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Titolo:
HUMAN TRYPTASE FIBRINOGENOLYSIS IS OPTIMAL AT ACIDIC PH AND GENERATESANTICOAGULANT FRAGMENTS IN THE PRESENCE OF THE ANTI-TRYPTASE MONOCLONAL-ANTIBODY B12
Autore:
REN S; LAWSON AE; CARR M; BAUMGARTEN CM; SCHWARTZ LB;
Indirizzi:
VIRGINIA COMMONWEALTH UNIV,MED COLL VIRGINIA,DEPT INTERNAL MED,POB 980263 RICHMOND VA 23298 VIRGINIA COMMONWEALTH UNIV,MED COLL VIRGINIA,DEPT INTERNAL MED RICHMOND VA 23298 VIRGINIA COMMONWEALTH UNIV,MED COLL VIRGINIA,DEPT PHYSIOL RICHMOND VA23298
Titolo Testata:
The Journal of immunology
fascicolo: 7, volume: 159, anno: 1997,
pagine: 3540 - 3548
SICI:
0022-1767(1997)159:7<3540:HTFIOA>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAST-CELL TRYPTASE; HUMAN-LUNG TRYPTASE; COMPLEMENTARY-DNA; ACTIVE TETRAMER; PROTEASE; CHYMASE; ACTIVATION; MITOGEN; POTENT; SKIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
45
Recensione:
Indirizzi per estratti:
Citazione:
S. Ren et al., "HUMAN TRYPTASE FIBRINOGENOLYSIS IS OPTIMAL AT ACIDIC PH AND GENERATESANTICOAGULANT FRAGMENTS IN THE PRESENCE OF THE ANTI-TRYPTASE MONOCLONAL-ANTIBODY B12", The Journal of immunology, 159(7), 1997, pp. 3540-3548

Abstract

Human tryptase is uniquely regulated by its association with heparin anti resists inhibition by biological protease inhibitors, The effectsof pH and B12, an IgG anti-tryptase mAb, on cleavage of the syntheticsubstrate tosyl-Gly-Pro-Lys-p-nitroanilide and of the biological substrate fibrinogen by tryptase were examined. Tosyl-Gly-Pro-Lys-p-nitroanilide cleavage was optimal at neutral pH and was inhibited by the B12mAb at acidic and neutral pH values, At pH 7.5, inhibition was reversible and noncompetitive. In contrast, the optimal pH for tryptase to cleave fibrinogen was acidic. B12 dramatically enhanced the rate and extent that tryptase cleaved all three fibrinogen subunits at pH 6.0 to 6.5, but inhibited these activities at neutral pH. Major fibrinogen cleavage fragments generated at acidic pH by the B12:tryptase complex were identical with those made by plasmin. Thus, at acid pH, tryptase alone destroyed the ability of fibrinogen to clot, while the B12:tryptase complex increased the rate of fibrinogenolysis and also generated the anticoagulant, fragment D. The acidic pH optimum for tryptase fibrinogenolysis may direct this activity to tissue sites oi inflammation, Aputative biological equivalent to B12 would limit tryptase fibrinogenolytic activity at sites of neutral pH, such as blood, but would augment activity at acidic sites.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 05:15:08