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J Biol Chem, Vol. 273, Issue 11, 6341-6350, March 13, 1998
From the Expression of the trabecular meshwork inducible
glucocorticoid response (TIGR) gene progressively increases from barely
detectable levels to greater than 2% of total cellular mRNA over
10 days exposure of trabecular meshwork (TM) cells to dexamethasone.
Cycloheximide blocked most of the TIGR mRNA induction, suggesting a
requirement for ongoing protein synthesis. The genomic structure of
TIGR (~20 kilobases) consists of 3 exons, and a 5-kilobase promoter
region that contains 13 predicted hormone response elements, including several glucocorticoid regulatory elements, and other potentially important regulatory motifs. TIGR cDNA encodes an
olfactomedin-related glycoprotein of 504 amino acids with motifs for
N- and O-linked glycosylation,
glycosaminoglycan initiation, hyaluronic acid binding, and leucine
zippers. Recombinant TIGR (rTIGR) showed oligomerization and specific
binding to TM cells. Anti-rTIGR antibody detected multiple
translational/post-translational forms of TIGR produced by the cells
(including secreted 66 kDa/55 kDa glycoproteins/proteins in the media
and 55 kDa cellular proteins), whereas Northern blot showed a single
mRNA species. The findings suggest potential mechanisms by which
TIGR could obstruct the aqueous humor fluid flow and participate in the
pathogenesis of glaucoma.
Gene Structure and Properties of TIGR, an Olfactomedin-related
Glycoprotein Cloned from Glucocorticoid-induced Trabecular Meshwork
Cells
,,,,
Cellular Pharmacology Laboratories,
Department of Ophthalmology, School of Medicine, University of
California, San Francisco, California 94143-0730 and the ¶ Mayo
Clinic, Rochester, Minnesota 55905
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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