Enzyme association with PPARgamma: evidence of a new role for 15-lipoxygenase type 2 |
| |
Authors: | Flores Anthony M Li Lu McHugh Nora G Aneskievich Brian J |
| |
Institution: | Department of Pharmaceutical Sciences, 372 Fairfield Road, U-2092, University of Connecticut, Storrs, CT 06269, USA. |
| |
Abstract: | Fatty acids have historically important structural roles in contributing to epidermal barrier function and therefore cutaneous health. Their metabolism to bioactive compounds is often up-regulated in response to cutaneous toxins thus providing them with functional roles. Some metabolites of arachidonic acid, such as 15S-hydroxyeicosatetraenoic acid (HETE), also serve functional roles as direct ligands for peroxisome proliferator activated receptors (PPARs). 15S-HETE, produced by 15-lipoxygenase type 2 (15-LOX-2), is an endogenous ligand for PPARgamma. This report demonstrates epidermal keratinocyte expression of both 15-LOX-2 and PPARgamma and provides evidence for a relationship beyond that of ligand-producer and -user, namely in vivo association of the two proteins at the molecular level making the enzyme a candidate nuclear receptor coregulator. Such close physical approximation of the 15S-HETE-producing enzyme and PPARgamma could potentiate the receptor response to a short-lived ligand. 15-LOX-2 may exemplify a class of enzymatically active nuclear receptor coactivator proteins distinct from those previously described but sharing their ability to promote expression from nuclear receptor-regulated promoters. |
| |
Keywords: | AA arachidonic acid HETE hydroxyeicosatetraenoic acid LOX lipoxygenase NR nuclear receptor PPAR peroxisome proliferator activated receptor |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|