The correlation between 13-hydroxyoctadecadienoate dehydrogenase (13-HODE dehydrogenase) and intestinal cell differention

https://doi.org/10.1016/0090-6980(93)90075-IGet rights and content

Abstract

The enzyme 13-hydroxyoctadecadienoate dehydrogenase (13-HODE dehydrogenase) catalyzes the NAD+-dependent oxidation of 13-hydroxyoctadecadienoic acid to 13-oxooctadecadienoic acid. In that the oxygenation of linoleic acid is increasingly being shown to be involved in the regulation of cellular function, this enzyme is poised to play a key role in the expression of the biological activity of these compounds. We have measured the activity of 13-HODE dehydrogenase in rat intestinal cells at various stages of differentiation. The specific activity of 13-HODE dehydrogenase shows a strong positive correlation with the degree of differentiation of intestinal mucosal cells from both the small and large intestines. In the small intestine the gradient of activity parallels that of alkaline phosphatase, while in the colon the incorporation of 3H-deoxythymidine and 13-HODE dehydrogenase are inversely related. Since the expression of 13-HODE dehydrogenase is most likely not associated with the nutritive function of the intestinal tract, these data raise the possibility the enzyme plays a role in the process of cellular differentiation.

References (19)

There are more references available in the full text version of this article.

Cited by (36)

  • 13-Oxo-ODE is an endogenous ligand for PPARγ in human colonic epithelial cells

    2007, Biochemical Pharmacology
    Citation Excerpt :

    Subsequent dehydrogenation of 13-HODE by the NAD+-dependent 13-HODE dehydrogenase results in the formation of the 2,4-dienone 13-oxooctadecadienoic acid (13-Oxo-ODE) [42,43] (Fig. 1). 13-HODE dehydrogenase has been discovered by Bull and co-workers [42,44–47]. The highest levels of 13-HODE dehydrogenase activity were observed in the colon and liver relative to other tissues [44,47,48].

View all citing articles on Scopus
View full text