Enhanced expression of recombinant human cyclooxygenase 1 from stably-transfected Drosophila melanogaster S2 cells by dimethyl sulfoxide is mediated by up-regulation of nitric oxide synthase and transcription factor Kr-h1

Biotechnol Lett. 2012 Jul;34(7):1243-50. doi: 10.1007/s10529-012-0911-x. Epub 2012 Mar 29.

Abstract

Recombinant human cyclooxygenase 1 (COX-1) was expressed from stably-transfected Drosophila melanogaster S2 (S2) cells. DMSO improved the expression of recombinant COX-1 by 180 %. DMSO increased the expression of nitric oxide synthase (NOS) at both the RNA and protein levels; NOS expression was closely correlated with the synthesis of recombinant COX-1 mRNA in stably-transfected S2 cells. DMSO also induced the gene encoding Kr-h1 which binds to the CACCC element of the metallothionein promoter to enhance the expression of recombinant COX-1. Therefore, DMSO improves the expression of recombinant COX-1 via NOS and/or the transcription factor Kr-h1.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Blotting, Western
  • Cell Line
  • Cyclooxygenase 1 / biosynthesis*
  • Cyclooxygenase 1 / genetics
  • Dimethyl Sulfoxide / metabolism*
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster
  • Gene Expression
  • Gene Expression Profiling
  • Gene Expression Regulation / drug effects*
  • Humans
  • Kruppel-Like Transcription Factors / metabolism*
  • Nitric Oxide Synthase / biosynthesis*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / genetics
  • Reverse Transcriptase Polymerase Chain Reaction
  • Transfection

Substances

  • Drosophila Proteins
  • Kr-h1 protein, Drosophila
  • Kruppel-Like Transcription Factors
  • Recombinant Proteins
  • Nitric Oxide Synthase
  • Cyclooxygenase 1
  • Dimethyl Sulfoxide