Expression of Bombyx mori 30Kc19 protein in Escherichia coli and its anti-apoptotic effect in Sf9 cell

Won Jong Rhee, Eun Hee Lee, Tai Hyun Park

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

The silkworm hemolymph has an anti-apoptotic activity in insect, mammalian, and human cell systems. The protein from silkworm hemolymph with the highest apoptosis inhibiting activity was found to be 30Kc19 protein, which was one of the '30K proteins'. In this study, 30Kc19 protein encoded by the 30Kc19 gene of the silkworm was expressed in Escherichia coli with (pET-22b(+)) and without (pET-3a) pelB leader sequence. 30Kc19 protein was over-expressed largely as a soluble form by pET-3a and both as soluble and insoluble forms by pET-22b(+). The medium was supplemented with each of the recombinant 30Kc19 proteins, and their presence was found to inhibit nuclear fragmentation and apoptotic body formation in actinomycin D-induced Sf9 cell apoptosis. Moreover, 30Kc19 protein repressed the activation of Sf-caspase-1. The 30Kc19 protein obtained from periplasm showed the most effective anti-apoptotic activity. This protein holds great potential for industrial and pharmaceutical applications since mass production and easy purification of this protein is possible.

Original languageEnglish
Pages (from-to)645-650
Number of pages6
JournalBiotechnology and Bioprocess Engineering
Volume14
Issue number5
DOIs
StatePublished - Oct 2009

Bibliographical note

Funding Information:
Acknowledgement This research was supported by WCU (World Class University) program through the Korea Science and Engineering Foundation funded by the Ministry of Education, Science and Technology (R32-2008-000-10213-0).

Keywords

  • 30Kc19 protein
  • Anti-apoptotic activity
  • Apoptosis
  • Caspase
  • Sikworm hemolymph

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