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J Biol Chem, Vol. 273, Issue 28, 17954-17961, July 10, 1998

Involvement of Retinoic Acid/Retinoid Receptors in the Regulation of Murine B-crystallin/Small Heat Shock Protein Gene Expression in the Lens

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 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.

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