Expression and functional analysis of the cellular retinoic acid binding protein from silkworm pupae (Bombyx mori).
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.
Wang
Xue-Jian
XJ
Institute of Biochemistry, College of Life Sciences, Zhejiang Sci-Tech University, Hangzhou 310018, China.
Chen
Jian
J
Lv
Zheng-Bing
ZB
Nie
Zuo-Ming
ZM
Wang
Dan
D
Shen
Hong-Dan
HD
Wang
Xue-Dong
XD
Wu
Xiang-Fu
XF
Zhang
Yao-Zhou
YZ
D000818:Animals; D012831:Bombyx; D002460:Cell Line; D049109:Cell Proliferation / Q000187:drug effects; D003001:Cloning, Molecular; D004351:Drug Resistance; D005786:Gene Expression Regulation; D011679:Pupa; D018168:Receptors, Retinoic Acid / Q000235:genetics / Q000502:physiology*; D014212:Tretinoin / Q000494:pharmacology*
D018168:Receptors, Retinoic Acid; C082927:retinoic acid binding protein I, cellular; D014212:Tretinoin