Endoplasmic reticulum stress response of Bombyx mori calreticulin.
We isolated a calreticulin cDNA from the silkworm, Bombyx mori. The cDNA encodes 398 amino acid residues of B. mori calreticulin, with an endoplasmic reticulum retentional HDEL motif at its C-terminus and a predicted molecular mass of 45,801 Da. The B. mori calreticulin shows high protein homology with calreticulin from G. mellonella (88%), A. aegypti (71%), D. melanogaster (69%) and H. sapiens (63%). The highest level of mRNA expression of B. mori calreticulin was exhibited in the fat body of this insect. Although expression of B. mori calreticulin was affected by disturbances in intracellular calcium levels, other ER stress conditions such as inhibition of intracellular protein transport, reduction of disulfide formation, glycosylation inhibition, heat shock and oxidative stress did not disrupt induction of B. mori calreticulin.
Goo
Tae Won
TW
Department of Sericulture and Entomology, National Institute of Agricultural Science and Technology, Suwon, 441-744, Korea.
Park
Soojung
S
Jin
Byung Rae
BR
Yun
Eun Young
EY
Kim
Iksoo
I
Nho
Si-Kab
SK
Kang
Seok-Woo
SW
Kwon
O-Yu
OY
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D012831:Bombyx / Q000235:genetics* / Q000378:metabolism; D037282:Calreticulin / Q000096:biosynthesis / Q000235:genetics*; D004721:Endoplasmic Reticulum / Q000187:drug effects / Q000502:physiology*; D019476:Insect Proteins / Q000096:biosynthesis / Q000235:genetics; D008969:Molecular Sequence Data; D010802:Phylogeny; D012333:RNA, Messenger / Q000378:metabolism; D016415:Sequence Alignment
D037282:Calreticulin; D019476:Insect Proteins; D012333:RNA, Messenger