Pathways of VLC-PUFA biosynthesis

Pathways of VLC-PUFA biosynthesis. Schematic diagram of in vivo n3 VLC-PUFA biosynthetic pathway mediated by ELOVL4 and other ELO families [modified after Suh and Clandinin ()]. 18:3n3, 20:5n3, or 22:5n3 can be converted to VLC-PUFA through the consecutive enzymatic activities of desaturases and elongases. Although some elongases are specific for a single step, others are nonspecific or multifunctional and act at several steps (e.g., human ELOVL5 and murine ELOVL2) (). We propose that ELOVL4 is essential for elongation of saturated 26:0 to 28:0 and of 26:5n3 to 28:5n3. It is also possible that ELOVL4 is necessary for generating (C30–C38):5n3, because these FAs are formed only in ELOVL4-expressing cells. However, other ELOVL proteins may be responsible for elongations of some of these VLC-PUFA (C30–C38) by using products generated by the ELOVL4 elongase activity. The synthesis of 34:6n3 and 36:6n3 in our study suggests desaturase activity on their shorter chain precursors. However, the specific desaturase(s) involved is not known. Reprinted from Agbaga et al. () with permission from publishers.

Publication

Retinal very long-chain PUFAs: new insights from studies on ELOVL4 protein. (2010) Martin-Paul Agbaga, et al. J Lipid Res. 2010 Jul;51(7):1624-1642. Figure: F6. Homo sapiens

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