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Volume 16, Number 19,
Issue of October 1, 1996
pp. 6119-6124
Copyright ©1996 Society for Neuroscience
Lipocalin-Type Prostaglandin D Synthase ( -Trace) Is Located in
Pigment Epithelial Cells of Rat Retina and Accumulates within
Interphotoreceptor Matrix
Received May 10, 1996; revised July 9, 1996; accepted July 17, 1996.
Carsten T. Beuckmann1,
William C. Gordon2,
Yoshihide Kanaoka1,
Naomi Eguchi3,
Victor L. Marcheselli2,
Dimitry Y. Gerashchenko1,
Yoshihiro Urade1,
Osamu Hayaishi1, and
Nicolas G. Bazan2
1 Department of Molecular Behavioral Biology, Osaka
Bioscience Institute, Suita Osaka 565, Japan, 2 Louisiana
State University Medical Center, Neuroscience Center and Department of
Ophthalmology, New Orleans, Louisiana 70112, and
3 Precursory Research for Embryonic Science and Technology,
Research Development Corporation of Japan, Suita Osaka 565, Japan
Glutathione-independent prostaglandin D synthase, identical to
 -trace, (a major CSF protein), is localized in the CNS. This enzyme,
lipocalin-type prostaglandin D synthase, is a member of the lipocalin
family of secretory proteins that transport small lipophilic
substances. This enzyme's activity in adult rat retina was enriched
sixfold in retinal pigment epithelium (RPE) and even more in
interphotoreceptor matrix (IPM), all higher than brain. Western blots
with anti-lipocalin-type prostaglandin D synthase showed three distinct
immunoreactive bands. In the retinal cytosolic fraction, only one band
was observed (Mr 25,000); in IPM, the larger
component occurred (Mr 26,000). The RPE
membrane-bound fraction showed two bands (Mr
20,000 and 23,000), indicating synthesis, and the cytosolic fraction
contained two bands (Mr 23,000 and 26,000),
indicating modification for release into IPM. At least two
glycosylation sites occurred on the prostaglandin D synthase moiety,
explaining the three immunoreactive bands in Western blots.
Immunohistochemistry with polyclonal antibodies against this
lipocalin-type enzyme showed intense localization in RPE, but less in
photoreceptor outer and inner segments. In situ
hybridization showed mRNA specifically expressed in RPE. Thus,
lipocalin-type prostaglandin D synthase is predominantly expressed in
RPE and actively accumulated in IPM. This may demonstrate gene sharing
because, while catalyzing prostaglandin D2 synthesis, it
may perform an additional, unrelated role in IPM. This enzyme is
secreted from the RPE into IPM from which it is then taken up by
photoreceptors. However, the nature of its ligand(s) is not known; they
may be retinoids and/or docosahexanoic acid.
Key words:
immunohistochemistry;
interphotoreceptor matrix;
lipocalin-type prostaglandin D synthase;
prostaglandin D2;
retina;
retinal pigment epithelium
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