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J Biol Chem, Vol. 273, Issue 28, 17954-17961, July 10, 1998
From the Laboratory of Molecular and Developmental Biology, NEI,
National Institutes of Health, Bethesda, Maryland 20892-2730
Crystallins are a diverse group of abundant
soluble proteins that are responsible for the refractive properties of
the transparent eye lens. We showed previously that Pax-6 can activate
the
Involvement of Retinoic Acid/Retinoid Receptors in the Regulation
of Murine
B-crystallin/Small Heat Shock Protein Gene Expression in
the Lens
B-crystallin/small heat shock protein promoter via the
lens-specific regulatory regions LSR1 (
147/118) and LSR2
(78/46). Here we demonstrate that retinoic acid can induce the
accumulation of B-crystallin in N/N1003A lens cells and that
retinoic acid receptor heterodimers (retinoic acid receptor/retinoid X
receptor; RAR/RXR) can transactivate LSR1 and LSR2 in cotransfection
experiments. DNase I footprinting experiments demonstrated that
purified RAR/RXR heterodimers will occupy sequences resembling retinoic
acid response elements within LSR1 and LSR2. Electrophoretic mobility
shift assays using antibodies indicated that LSR1 and LSR2 can interact
with endogenous RAR/RXR complexes in extracts of cultured lens cells.
Pax-6 and RAR/RXR together had an additive effect on the activation of
B-promoter in the transfected lens cells. Thus, the
B-crystallin gene is activated by Pax-6 and retinoic acid receptors,
making these transcription factors examples of proteins that have
critical roles in early development as well as in the expression
of proteins characterizing terminal differentiation.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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