2000
DOI: 10.1006/bbrc.2000.3397
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Characterization of 25-Hydroxyvitamin D Binding Protein from Intestinal Cells

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Cited by 15 publications
(8 citation statements)
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References 24 publications
(18 reference statements)
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“…On the contrary, high expression of IDBP may be a compensatory mechanism to enhance vitamin D action in the face of a functional vitamin D de ciency. The notion of a reciprocal relation between 1,25-dihydroxyvitamin D action and cellular IDBP concentration would be consistent with the observations of Teegarden et al 11 on the role of 1,25-dihydroxyvitamin D on 25-hydroxyvitamin D-binding capacity. These investigators found that the level of a 68-kDa cytosolic vitamin D-binding protein was decreased by 1,25-dihydroxyvitamin D treatment in Caco-2 cells, a human intestinal cell line.…”
supporting
confidence: 90%
“…On the contrary, high expression of IDBP may be a compensatory mechanism to enhance vitamin D action in the face of a functional vitamin D de ciency. The notion of a reciprocal relation between 1,25-dihydroxyvitamin D action and cellular IDBP concentration would be consistent with the observations of Teegarden et al 11 on the role of 1,25-dihydroxyvitamin D on 25-hydroxyvitamin D-binding capacity. These investigators found that the level of a 68-kDa cytosolic vitamin D-binding protein was decreased by 1,25-dihydroxyvitamin D treatment in Caco-2 cells, a human intestinal cell line.…”
supporting
confidence: 90%
“…Besides, the efflux of D 3 from the cell compartment to the apical medium, which represents the intestinal lumen, was significantly more important than that of 25(OH)D 3 and 1α(OH)D 3 . This result may be explained by the presence of a cytosolic vitamin D binding protein (cDBP) [ 25 ], which would display a higher affinity for hydroxylated forms than for D 3 , similarly to plasma DBP [ 26 ].…”
Section: Discussionmentioning
confidence: 99%
“…25OHD is transported in the blood by a well-characterized vitamin D-binding protein, which has a higher affinity for 25OHD than for 1,25(OH) 2 D and native vitamin D, and which is present in large excess of the normal blood contents of its ligands [54]. A specific vitamin D-binding protein has been demonstrated in the cytosol from rat and human intestinal cells, which binds 25OHD with at least 1,000-fold greater affinity than 1,25(OH) 2 D, and thus may be involved in the absorption of 25OHD, or the calcium absorptive actions of 25OHD [55,56]. Yet another intracellular vitamin D-binding protein, which preferently binds 25OHD (3-fold greater affinity than for 1,25(OH) 2 D) has been characterized in New World monkeys [57].…”
Section: Bioavailability Homeostasis and Transportmentioning
confidence: 99%