Secretion of Active Urokinase-type Plasminogen Activator from the Yeast Yarrowia lipolytica

  • Ryu, Ho-Myoung (Department of Microbiology, Chungnam National University) ;
  • Kang, Woo-Kyu (Department of Microbiology, Chungnam National University) ;
  • Kang, Hyun-Ah (Korea Research Institute of Bioscience and Biotechnology) ;
  • Kim, Jeong-Yoon (Department of Microbiology, Chungnam National University)
  • Published : 2003.04.01

Abstract

In order to study the secretion of the human urokinase-type plasminogen activator, u-PA, from the yeast yarrowia lipolytica, three kinds of integrative expression vector were constructed. These vectors differed only in their secretion control legions, pre-, pre-dip-(dipeptide Stretch) or pre-dip-pro sequences of the alkaline extracellular protease, which were joined inflame to the human u-PA cDNA. The recombinant Y. lipolytica Strains, transformed with the expression vectors, secreted the hyperglycosylated u-PA. A fibrin plate assay of the culture supernatants showed that the hyperglycosylated u-PA proteins could catalyze fibrinolysis, and that the pre-dip sequence was the most efficient secretory signal for the secretion of the u-PA from Y. lipolyica. This result suggests that Y. lipolytica can be developed as a potential host for the production of recombinant human u-PA.

Keywords

References

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