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Titolo:
Acute phase protein alpha(1)-acid glycoprotein interacts with plasminogen activator inhibitor type 1 and stabilizes its inhibitory activity
Autore:
Boncela, J; Papiewska, I; Fijalkowska, I; Walkowiak, B; Cierniewski, CS;
Indirizzi:
Med Univ Lodz, Dept Biophys, PL-90131 Lodz, Poland Med Univ Lodz Lodz Poland PL-90131 , Dept Biophys, PL-90131 Lodz, Poland Polish Acad Sci, Ctr Microbiol & Virol, PL-93232 Lodz, Poland Polish Acad Sci Lodz Poland PL-93232 biol & Virol, PL-93232 Lodz, Poland Tech Univ Lodz, Dept Biophys, PL-90537 Lodz, Poland Tech Univ Lodz Lodz Poland PL-90537 Dept Biophys, PL-90537 Lodz, Poland
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 38, volume: 276, anno: 2001,
pagine: 35305 - 35311
SICI:
0021-9258(20010921)276:38<35305:APPAGI>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
VASCULAR SMOOTH-MUSCLE; HUMAN ALPHA-1-ACID GLYCOPROTEIN; HUMAN-PLASMA; STRUCTURAL REQUIREMENTS; COMPLEX-FORMATION; BINDING-SITE; VITRONECTIN; PAI-1; EXPRESSION; THROMBIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
60
Recensione:
Indirizzi per estratti:
Indirizzo: Cierniewski, CS Med Univ Lodz, Dept Biophys, 3 Lindleya St, PL-90131 Lodz,Poland Med Univ Lodz 3 Lindleya St Lodz Poland PL-90131 , Poland
Citazione:
J. Boncela et al., "Acute phase protein alpha(1)-acid glycoprotein interacts with plasminogen activator inhibitor type 1 and stabilizes its inhibitory activity", J BIOL CHEM, 276(38), 2001, pp. 35305-35311

Abstract

alpha (1)-Acid glycoprotein, one of the major acute phase proteins, was found to interact with plasminogen activator inhibitor type 1 (PAI-1) and to stabilize its inhibitory activity toward plasminogen activators. This conclusion is based on the following observations: (a) alpha (1)-acid glycoprotein was identified to bind PAI-1 by a yeast two-hybrid system. Three of 10 positive clones identified by this method to interact with PAI-1 contained almost the entire sequence of alpha (1)-acid glycoprotein; (b) this protein formed complexes with PAI-1 that could be immunoprecipitated from both the incubation mixtures and blood plasma by specific antibodies to either PAI-1or alpha (1)-acid glycoprotein. Such complexes could be also detected by asolid phase binding assay; and (c) the real-time bimolecular interactions monitored by surface plasmon resonance indicated that the complex of alpha (1)-acid glycoprotein with PAI-1 is less stable than that formed by vitronectin with PAI-1, but in both cases, the apparent KD values were in the range of strong interactions (4.51 + 1.33 and 0.58 + 0.07 nm, respectively). The on rate for binding of PAI-1 to ai-glycoprotein or vitronectin differed by 2-fold, indicating much faster complex formation by vitronectin than by alpha (1)-acid glycoprotein. On the other hand, dissociation of PAI-1 bound to vitronectin was much slower than that from the alpha (1)-acid glycoprotein, as indicated by 4-fold lower k(off) values. Furthermore, the PAI-1 activity toward urokinase-type plasminogen activator and tissue-type plasminogen activator was significantly prolonged in the presence of alpha (1)-acid glycoprotein. These observations suggest that the complex of PAI-1 with alpha (1)-acid glycoprotein can play a role as an alternative reservoir of the physiologically active form of the inhibitor, particularly during inflammation or other acute phase reactions.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/04/20 alle ore 22:25:51