Endoplasmic reticulum stress response of Bombyx mori calreticulin
Autor(es): Goo, TW; Park, S; Jin, BR; Yun, EY; Kim, I; Nho, S; Kang, SW; Kwon, OY
Resumo: 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.
Palavras-Chave: Bombyx mori; BM5 cell; Calreticulin; Endoplasmic reticulum
Imprenta: Molecular Biology Reports, v. 32, n. 3, p. 133-139, 2005
Identificador do objeto digital: 10.1007/s11033-004-5908-7
Descritores: Aedes aegypti - DNA ; Aedes aegypti - Proteins
Data de publicação: 2005
