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Journal of Lipid Research, Vol 37, 1947-1952, Copyright © 1996 by Lipid Research, Inc.
NL Mata, JR Mata and AT Tsin
Various properties of retinyl ester hydrolysis in the liver and the retinal
pigment epithelium (RPE) have been studied, yet the relationship between
the retinyl ester hydrolase (REH) activities in these tissues of the same
species is not known. In the present study, REH activities in bovine liver
and RPE microsomes were compared to explore potential biochemical
relationships of retinyl ester metabolism in these tissues. Rates of
[3H]all-trans retinyl palmitate hydrolysis by liver and RPE were comparable
(i.e., Vmaxapp approximately 300 pmol/min per mg; K(m)app approximately 30
microM), while hydrolysis of [3H]11-cis retinyl palmitate by RPE was
significantly higher (Vmaxapp = 1,667 pmol/min per mg). When equimolar
amounts (10 microM) of either [14C]triolein or unlabeled 11-cis retinyl
palmitate were added to [3H]all-trans REH assays, all-trans REH activities
in liver and RPE demonstrated similar time-dependent inhibition profiles.
In contrast, hydrolysis of [3H]11-cis retinyl palmitate by RPE was
relatively unaffected by addition of either [14C]triolein or unlabeled
all-trans retinyl palmitate. Additionally, modification of the microsomal
proteins with N-ethylmaleimide produced profound, dose-dependent
alterations in K(m)app values for all-trans retinyl ester hydrolysis,
whereas K(m)app for 11-cis REH in the RPE was not significantly altered.
These results have elucidated common biochemical features of all-trans
retinyl ester hydrolysis in liver and RPE. In contrast, hydrolysis of
11-cis retinyl ester in RPE is characterized by a distinctive substrate
preference and unique biochemical properties.
ARTICLES
Comparison of retinyl ester hydrolase activities in bovine liver and retinal pigment epithelium
Division of Life Sciences, University of Texas at San Antonio 78249- 0662, USA.
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