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A novel retinoid binding property of human annexin A6
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Vitamin A (all‐trans retinol) and all‐trans retinoid acid (ATRA) interacted with human annexin A6 (AnxA6) as evidenced by AnxA6‐induced blue shift of retinoid absorption maxima, by AnxA6‐Trp fluorescence quenching and by a fluorescence resonance energy transfer from a Trp residue of AnxA6 to retinol. In addition, both retinoids stimulated the calcium‐dependent binding of AnxA6 to liposomes, accompanied by oligomerization of AnxA6. Up to our knowledge, it is a first report supporting the hypothesis of a direct implication of AnxA6 in vitamin A‐dependent tissue mineralization.
Title: A novel retinoid binding property of human annexin A6
Description:
Vitamin A (all‐trans retinol) and all‐trans retinoid acid (ATRA) interacted with human annexin A6 (AnxA6) as evidenced by AnxA6‐induced blue shift of retinoid absorption maxima, by AnxA6‐Trp fluorescence quenching and by a fluorescence resonance energy transfer from a Trp residue of AnxA6 to retinol.
In addition, both retinoids stimulated the calcium‐dependent binding of AnxA6 to liposomes, accompanied by oligomerization of AnxA6.
Up to our knowledge, it is a first report supporting the hypothesis of a direct implication of AnxA6 in vitamin A‐dependent tissue mineralization.
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