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Inhibition of Hepatic Stearoyl-CoA Desaturase Activity by Trans-10,cis-12 Conjugated Linoleic Acid and its Deratives
Biochimica et Biophysica Acta (2000)
  • Yeonhwa Park, University of Massachusetts - Amherst
  • M. W Pariza
  • M. E Cook
  • J. M Storkson
  • J. M Ntambi
  • J. Sih
Abstract
Conjugated linoleic acid (CLA) has been reported to decrease stearoyl-CoA desaturase (SCD) activity by decreasing mRNA expression. This investigation was designed to determine whether structurally related compounds of CLA have a direct inhibitory effect on SCD activity. Trans-10,cis-12 CLA had strong inhibitory activity on SCD while cis-9,trans-11, and trans-9,trans-11 isomers had no effect. Trans-10 octadecenoate was not inhibitory, whereas cis-12 octadecenate was inhibitory, but not as effective as trans-10,cis-12 CLA. Of the oxygenated derivatives, 9-peroxy-cis/trans-10, trans-12 octadecadienoate was a more effective inhibitor than trans-10,cis-12 CLA, whereas 9-hydroxy-trans-10, cis-12 octadecadienoate was less effective. Interestingly, cis-11 octadecadienoate and cis-12 octadecen-10-ynoate were slightly inhibitory. However, trans-9 and trans-11 octadecenoates, and trans-9,cis-12 octadecadienoate were all inactive under test condition, as were linoleate, oleate, and arachidonate. Derivatives of CLA acid modified to alcohol, amide or chloride were all inactive. A cis-12 double bond appears to be a key structural feature for inhibiting SCD activity, especially when coupled with a trans-10 double, whereas a cis-11 double bond is less effective.
Disciplines
Publication Date
2000
Citation Information
Yeonhwa Park, M. W Pariza, M. E Cook, J. M Storkson, et al.. "Inhibition of Hepatic Stearoyl-CoA Desaturase Activity by Trans-10,cis-12 Conjugated Linoleic Acid and its Deratives" Biochimica et Biophysica Acta Vol. 1486 (2000)
Available at: http://works.bepress.com/yeonhwa_park/43/