## Abstract The desilked silkworm pupae (Bombyx mori L.) collected from Kollegala, Malavalli and Ramanagaram belt of Karnataka State (South India) were extracted with petroleum ether (60–80°C). The neutral lipids fraction was isolated and saponified. Saponifiable fraction was analysed for fatly aci
Expression and functional analysis of the cellular retinoic acid binding protein from silkworm pupae (Bombyx mori)
✍ Scribed by Xue-Jian Wang; Jian Chen; Zheng-Bing Lv; Zuo-Ming Nie; Dan Wang; Hong-Dan Shen; Xue-Dong Wang; Xiang-Fu Wu; Yao-Zhou Zhang
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 300 KB
- Volume
- 102
- Category
- Article
- ISSN
- 0730-2312
No coin nor oath required. For personal study only.
✦ Synopsis
Abstract
Cellular retinoic acid binding protein (CRABP) is a member of intracellular lipid‐binding protein (iLBP), and closely associated with retinoic acid (RA) activity. We have cloned the CRABP gene from silkworm pupae and studied the interaction between Bombyx mori CRABP (BmCRABP) and all‐trans retinoic acid (atRA). The MTT assay data indicated that when BmCRABP is overexpressed in Bm5 cells, the cells dramatically resisted to atRA‐induced growth inhibition. Conversely, the cells were sensitive to atRA treatment upon knocking down the BmCRABP expression. Subcellular localization revealed that BmCRABP is a cytoplasm protein, even when treated with atRA, the CRABP still remained in the cytoplasm. These data demonstrated that the function of BmCRABP have an effect on the physiological function of atRA. J. Cell. Biochem. 102: 970–979, 2007. © 2007 Wiley‐Liss, Inc.
📜 SIMILAR VOLUMES
A cDNA clone encoding a small GTP binding protein (BRho) was isolated from an embryonic cDNA library of Bombyx mori that encoded a polypeptide with 202 amino acids sharing 60-80% similarity with the Rho1 family of GTP binding proteins. The effector site and one of the guanine nucleotide binding site