Deglycosylation increases the fibrinolytic activity of a deletion mutant of tissue-type plasminogen activator.
Thromb Haemost
; 63(3): 464-71, 1990 Jun 28.
Article
in En
| MEDLINE
| ID: mdl-2119528
delta 2-89 t-PA is a deletion mutant lacking the finger (F) and epidermal growth factor (EGF) domains; thus, the fibrin interaction of this molecule must be mediated solely by the kringle region. In the present study, the influence of the oligosaccharide side-chains on the activity of delta 2-89 t-PA has been investigated. delta 2-89 t-PA was secreted in two forms, designated I and II, which presumably differ by the lack of one asparagine-linked oligosaccharide in the kringle 2 domain of form II. Forms I and II of delta 2-89 t-PA were purified; form II displayed higher fibrinolytic activity than form I. When form I was partially deglycosylated or treated to remove sialic acid, fibrinolytic activity was increased. Production of delta 2-89 t-PA in the presence of tunicamycin led to secretion of a glycan-free activator with higher activity. These findings suggest that certain oligosaccharide side-chains, particularly those containing sialic acid, can interfere with the interaction between the kringle region of t-PA and fibrin.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Tissue Plasminogen Activator
/
Fibrinolysis
Language:
En
Journal:
Thromb Haemost
Year:
1990
Document type:
Article