Endoplasmic Reticulum Stress Response of Bombyx mori Calreticulin

  • Goo, Tae-Won (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology) ;
  • Park, Soojung (Department of Anatomy, College of Medicine, Chungnam National University) ;
  • Jin, Byung-Rae (College of Natural Resources and Life Science, Dong-A University) ;
  • Yun, Eun-Young (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technolog) ;
  • Kim, Iksoo (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technolog) ;
  • Nho, Si-Kab (Department of Natural Fiber Science, College of Agricultura and Life Sciences, Kyungpook National University) ;
  • Kang, Seok-Woo (Department of Sericulture and Entomology, National Institute of Agricultural Science and Technolog) ;
  • Kwon, O-Yu (Department of Anatomy, College of Medicine, Chungnam National University)
  • Published : 2003.10.01

Abstract

To further understanding of the role of calreticulin in insects, we have isolated a cDNA of calreticulin from silkworm, Bombyx mori. The cDNA encodes a 398 amino acid residues of B. mori calreticulin with endoplasmic reticulum retentional HDEL motif at its C-terminus, and a predicted molecular mass of 45801 Da. The B. mori calreticulin shows high protein homology with those of G mellonella (88%), A. aegypti (71%) and H. sapiens (63%). (omitted)

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