Identification of the proteins required for fatty acid desaturation in zebrafish (Danio rerio)
- Authors
- Chen, Y.S., Luo, W.I., Lee, T.L., Yu, S.S., and Chang, C.Y.
- ID
- ZDB-PUB-131112-12
- Date
- 2013
- Source
- Biochemical and Biophysical Research Communications 440(4): 671-676 (Journal)
- Registered Authors
- Chang, Chi-Yao
- Keywords
- cytochrome b6 reductase, elongase, fatty acid desaturase, fluorescence resonance energy transfer, zebrafish
- MeSH Terms
-
- Animals
- Fatty Acid Desaturases/genetics
- Fatty Acid Desaturases/metabolism*
- Fatty Acids/metabolism*
- HeLa Cells
- Humans
- Linoleoyl-CoA Desaturase/genetics
- Linoleoyl-CoA Desaturase/metabolism*
- Zebrafish/metabolism*
- Zebrafish Proteins/metabolism*
- PubMed
- 24103751 Full text @ Biochem. Biophys. Res. Commun.
Zebrafish Δ-5/Δ-6 fatty acid desaturase (Z-FADS) catalyzes the cascade synthesis of long-chain polyunsaturated fatty acids (PUFAs), thereby playing a pivotal role in several biological processes. In the current study, we report that the Z-FADS protein exists in close proximity to certain cytochrome b5 reductases (CYB5R2 and 3) and elongases (ELOVL2, 4, 5 and 7) on the endoplasmic reticulum, as determined using fluorescence microscopy and fluorescence resonance energy transfer. HeLa cells co-transfected with zebrafish fads and elovl2, 4, and 5 produced docosahexaenoic acid (DHA), as detected by gas chromatography. In addition, immunofluorescence cytochemistry and Western blot data revealed that Z-FADS is present in the mitochondria of HeLa cells. Collectively, our results implicate that Z-FADS, the sole fatty acid desaturase ever been identified in zebrafish, can serve as a universal fatty acid desaturase during lipogenesis.