Study on the mechanism of the annexin II-mediated co-assembly of t-PA and plasminogen / 华中科技大学学报(医学)(英德文版)
Journal of Huazhong University of Science and Technology (Medical Sciences)
; (6): 21-76, 2002.
Article
Dans En
| WPRIM
| ID: wpr-329142
Responsable en Bibliothèque :
WPRO
ABSTRACT
In order to further investigate the effect of annexin II (Ann-II) on tissue plasminogen activator (t-PA)-dependent plasminogen (PLG) activation and its interactive mechanism, recombinant native Ann-II bound t-PA, PLG and plasmin with high affinity was examined. The flow cytometric assay showed that the ann-II expression rate was higher in the human umbilical vein endothelial cell (HUVEC) (87.65%) than in the HL-60 cells as controls (35.79%). Two irrelevant proteins, bovine serum albumin (BSA) and equine IgG (EIG) had no effect on the production of plasmin. Ann-II-mediated enhancement of t-PA-dependent PLG activation was inhibited by epsilon-aminocaproic acid or by pretreatment of Ann-II with carboxypeptidase B with the inhibitive rate being 77.8% and 77.0%, respectively. It was revealed that the effect of Ann-II on PLG activation was specific for t-PA. Urokinase didn't bind to Ann-II, demonstrating the role of receptor-related lysine residues on activation of PLG, showing that the Ann-II-PLG interaction was dependent upon carboxyl-terminal lysine residues. These findings suggest that annexin II-mediated co-assembly of t-PA and PLG may promote plasmin generation and play a key role in modulating fibrinolysis on the endothelial surface.
Texte intégral:
1
Indice:
WPRIM
Sujet Principal:
Pharmacologie
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Plasminogène
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Veines ombilicales
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Protéines recombinantes
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Endothélium vasculaire
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Cellules cultivées
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Activateur tissulaire du plasminogène
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Annexine A2
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Biologie cellulaire
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Fibrinolyse
Limites du sujet:
Humans
langue:
En
Texte intégral:
Journal of Huazhong University of Science and Technology (Medical Sciences)
Année:
2002
Type:
Article