The influence of glycosylation on the catalytic and fibrinolytic properties of pro-Urokinase

C. Lenich, R. Pannell, J. Henkin, V. Gurewich*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


We previously found that human pro-UK expressed in Escherichia coli is more active in fibrinolysis than recombinant human pro-UK obtained from mammalian cell culture media. To determine whether this difference is related to the lack of glycosylation of the E. coli product, we compared the activity of E. coli-derived pro-UK [(-)pro-UK] with that of a glycosylated pro-UK [(+)pro-UK] and of a mutant of pro-UK missing the glycosylation site at Asn-302 [(-)(302)pro-UK]. The latter two pro-UKs were obtained by expression of the human gene in a mammalian cell. The nonglycosylated pro-UKs were activated by plasmin more efficiently (≃2-fold) and were more active in clot lysis (1.5-fold) than the (+)pro-UK. Similarly, the nonglycosylated two-chain derivatives (UKs) were more active against plasminogen and were more rapidly inactivated by plasma inhibitors than the (+)UK. These findings indicate that glycosylation at Asn-302 influences the activity of pro-UK/UK and could be the major factor responsible for the enhanced activity of E. coli-derived pro-UK.

Original languageEnglish (US)
Pages (from-to)539-544
Number of pages6
JournalThrombosis and Haemostasis
Issue number5
StatePublished - 1992

ASJC Scopus subject areas

  • Hematology


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