Determination of the rates of synthesis and degradation of vitamin D-dependent chick intestinal and renal calcium-binding proteins

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Abstract

Vitamin D3 and its biologically active metabolite 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] are shown to induce in the chick intestine and kidney the biosynthesis of a calcium binding protein (CaBP). In vitamin D3-replete chickens raised under adequate dietary calcium (Ca) and phosphorus (P) conditions, the steady-state level of intestinal CaBP (30–50 g/mg protein) is 5- to 20-fold greater than that of renal CaBP. Whereas dietary phosphorus restriction is known to elevate both intestinal and renal CaBP levels, dietary calcium restriction elevates only intestinal CaBP. The present study reports the rates of biosynthesis in vivo and in vitro, and of biodegradation in vivo, of both intestinal and renal CaBP after administration of vitamin D3 or 1,25(OH)2D3 to rachitic chicks. The apparent rate constant of degradation for intestinal CaBP was 0.024 h−1 (t12 = 29 h) and that for renal CaBP was 0.019 h−1 (t12 = 36 h) while total cellular soluble protein in the intestine and kidney had half-lives of 43 and 70 h, respectively. The time course of induction of the synthesis of CaBP was determined in intestine and kidney after administration of a physiological dose of 1,25(OH)2D3 to rachitic chicks. Intestinal CaBP synthesis was detectable by 3 hours, reached a maximal rate by 10 hours, and sharply decayed by 16–20 hours. The time course of induction of renal CaBP synthesis was very similar, although the rate of renal CaBP synthesis was readily detectable at the initial time of administration of 1,25(OH)2D3. The relative rates of synthesis of CaBP in the intestine and kidney under a variety of dietary Ca and P conditions in the vitamin D3-replete chick exactly paralleled the steady-state level of CaBP in these two tissues. These results are consistent with a model in which the steady-state levels of intestinal and renal CaBP are solely determined by their respective rates of biosynthesis; the CaBP biosynthetic capability, in turn, is regulated by the availability of 1,25(OH)2D3 to each target organ.

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    This is paper XXXI in a series entitled “Studies on the Mode of Action of Calciferol.” The previous paper in this series is Ref. (1). This work was supported by USPHS Grants AM-09012 (A. W. N.) and AM-23198 (H. L. H.), NSF Grant PCM76-24446 (H. L. H.), and Research Career Development Award (H. L. H.) AM-00412.

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    Present address: Department of Chemistry, Harvard University, Cambridge, Mass. 02138.

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