Expression and functional analysis of the cellular retinoic acid binding protein from silkworm pupae (Bombyx mori).
J Cell Biochem
; 102(4): 970-9, 2007 Nov 01.
Article
en En
| MEDLINE
| ID: mdl-17486602
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.
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Base de datos:
MEDLINE
Asunto principal:
Tretinoina
/
Resistencia a Medicamentos
/
Receptores de Ácido Retinoico
Límite:
Animals
Idioma:
En
Revista:
J Cell Biochem
Año:
2007
Tipo del documento:
Article
País de afiliación:
China