누에 배양세포로부터 분리한 Protein Disulfide Isomerase 유전자의 발현 특성

Molecular Characterization of a Bombyx mori Protein Disulfide Isomerase(bPDI)

  • 구태원 (농촌진흥청 농업과학기술원) ;
  • 윤은영 (농촌진흥청 농업과학기술원) ;
  • 황재삼 (농촌진흥청 농업과학기술원) ;
  • 강석우 (농촌진흥청 농업과학기술원) ;
  • 권오유 (충남대학교 의과대학)
  • 발행 : 2001.10.01

초록

Many secreted proteins have disulfide bonds that are important for their structure and function. Protein disulfide isomerase (PDI, EC 5.3.1.4.), an enzyme that catalyzes the formation and rearrangement of thiol/disulfide exchange reactions, is a resident of the endoplasmic reticulum (ER). The subcellular localization and its function as catalyst of disulfide bond formation in the biosynthesis of secretory and cell membrane proteins suggest that PDI plays a key role in the secretory pathway. We have isolated a cDNA encoding protein disulfide isomerase from Bombyx mori(bPDI). It has been characterized under ER stress conditions (dominantly induced by calcium ionophore A23187, tunicamycin and DTT), which is known to cause an accumulation of unfolded proteins in the ER. Furthermore, It has also been examined for tissue distribution(pronounced at the fat body), hormonal regulation (juvenile hormone, insulin and juvenile +transferrin; however, it is not effected by transferrin alone), and the effect of exogenous bacteria (peak at 16 h after infection) on the bPDI mRNA expression. The results suggest that bPDI is a member of the ER stress protein group, and it may play an important role in exogenous bacterial infection in fat body, and that homones regulate its expression.

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