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24,25-Dihydroxyvitamin D3 binds to catalase
University of Skövde, School of Life Sciences.
Department of Nutrition and Food Sciences, Center for Integrated Biosystems, Utah State University, Logan, UT 84322, United States / Kansas City University of Medicine and Biosciences, 1750 Independence Ave., Kansas City, MO 64106-1453, United States.
Department of Nutrition and Food Sciences, Center for Integrated Biosystems, Utah State University, Logan, UT 84322, United States.
Department of Nutrition and Food Sciences, Center for Integrated Biosystems, Utah State University, Logan, UT 84322, United States / Department of Nutrition and Food Sciences, Utah State University, Logan, UT 84322-8700, United States.
2006 (English)In: Journal of Cellular Biochemistry, ISSN 0730-2312, E-ISSN 1097-4644, Vol. 97, no 6, 1259-1266 p.Article in journal (Refereed) Published
Abstract [en]

There is increasing evidence that the vitamin D metabolite, 24,25-dihydroxyvitamin D3 (24,25(OH)2D3) has endocrine actions. In the current work, we report that an endogenous binding protein for 24,25(OH)2D3 is catalase, based on sequence analysis of the isolated protein. An antibody (Ab 365) generated against equivalent protein recognized bovine catalase and a 64 kDa band in subcellular fractions of chick intestine. A commercially available anti-catalase antibody reduced specific [3H]24,25(OH)2D3 binding in subcellular fractions of chick intestine by greater than 65%, relative to the same fractions treated with an unrelated antibody (Ab 099). The same commercially available anti-catalase was able to block the inhibitory actions of 24,25(OH)2D3 on 32P uptake in isolated intestinal epithelial cell suspensions. We subsequently characterized binding of steroid to commercially available catalase, and found that between 0 and 5 nM of enzyme added to subcellular fraction P2 (20,000g, 10-min post-nuclear pellet) resulted in a linear increase in the amount of [3H]24,25(OH)2D3 specifically bound. Additional studies indicated that 25(OH)D3 was an effective competitor for binding, whereas 1,25(OH)2D3 only poorly displaced [3H]24,25(OH)2D3. Saturation analyses with added catalase yielded a physiologically relevant affinity constant (KD = 5.6 ± 2.7 nM) and a Bmax = 209 ± 34 fmols/mg protein, comparable to previous studies using purified basal lateral membranes or vesicular fractions. Moreover, in a study on subcellular fractions isolated from chickens of varying ages, we found that in females, both specific [3H]24,25(OH)2D3 binding and catalase activity increased from 7- to 58-week-old birds, whereas in males, elevated levels of both parameters were expressed in preparations of 7- and 58-week-old birds. The data suggest that signal transduction may occur through modulation of hydrogen peroxide production.

Place, publisher, year, edition, pages
John Wiley & Sons, 2006. Vol. 97, no 6, 1259-1266 p.
Identifiers
URN: urn:nbn:se:his:diva-1792DOI: 10.1002/jcb.20717ISI: 000236301500010PubMedID: 16552753Scopus ID: 2-s2.0-33645682675OAI: oai:DiVA.org:his-1792DiVA: diva2:32068
Available from: 2007-08-31 Created: 2007-08-31 Last updated: 2013-04-10Bibliographically approved

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