The relationship between vitamin D-stimulated calcium transport and intestinal calcium-binding protein in the chicken

Spencer, Rosemary; Charman, M.; Wilson, Peter W.F.; Lawson, David

doi:10.1042/bj1700093

Cited by 160 publications

(32 citation statements)

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“…The protein synthesis theory of 1,25(OH)2D3 function has been questioned recently (9,10,12) (10,13,14). However, this lack oftemporal correspondence has never been observed in this laboratory when truly vitamin Ddeficient chicks were used (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The primary effect of D3 was considered to be a modification of membrane phospholipids and thereby an increase in the permeability of the brush border membrane to Ca2+, with subsequent steps in the absorption ofcalcium somewhat secondary to this event (11,12). In this vein, Spencer et al (13), Bikle et al (10), and Thomasset et aL (14) reported that the administration of a single dose of 1,25(OH)2D3 to vitamin D-deficient animals stimulates calcium absorption prior to the induction of the synthesis of calciumbinding protein (CaBP), a protein product ofthe genomic action of the 1,25(OH)2D3. However, this lack of temporal correlation between CaBP synthesis and 1,25(OH)2D3-stimulated calcium absorption is contrary to our experience, as documented in this report.…”

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confidence: 99%

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Evidence for multiple effects of vitamin D3 on calcium absorption: response of rachitic chicks, with or without partial vitamin D3 repletion, to 1,25-dihydroxyvitamin D3.

Wasserman¹,

Brindak²,

Meyer³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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Determination of the Effect of 1,25(OH)2D3 on Calcium Absorption. Series 1. These experiments were designed to determine the temporal relationship between the stimulation of calcium absorption by 1,25(OH)2D3 and the appearance of CaBP. In one experiment, the chicks were injected intracardially with 1 Ag of 1,25(0H)2D3 in propylene glycol at time 0, and the degree ofduodenal absorption of 47Ca and the presence of CaBP in the mucosal tissue were determined 1, 2, 4, or 8 hr later. The absorption period was 30 min. In the second experiment, the protocol was the same except that the chicks received 300 ng of 1,25(0H)2D3 and the absorption period was 15 min.Series 2. Vitamin D3 [2 international units (IU) per day for 6 days] was administered orally to rachitic chicks before further treatment. In the first experiment, the partially repleted chicks were injected intracardially with 1,25(OH)2D3 or vehicle (propylene glycol) and the same protocol as for the rachitic chicks (see Series 1) was followed. In the second experiment, the rachitic chicks were divided into two groups: one group was partially repleted with vitamin D3 (2 IU/day) for 6 days and the other group received vehicle only. The chicks were further divided into two subgroups and injected intracardially with 300 ng of 1,25(0H)2D3 in propylene glycol or with vehicle, and the absorption of 47Ca and the appearance of CaBP were determined 1 or 2 hr later.Calcium Absorption Procedure. Calcium absorption was determined by the in situ ligated-loop procedure, with 47Ca as tracer, as described (17). The absorption period was 15 or 30 min. Residual 47Ca in the excised loop was measured with a Beckman Gamma-300 gamma counter with the discriminator set to exclude contributions from the 47Sc daughter. Absorption was calculated as 100 minus the percentage of 47Ca remaining in the segment. After measurement of radioactivity, the same segment was further analyzed for its CaBP content.As part of the last experiment of series 2, the net accumulation of 47Ca by the intestinal tissue was determined by re- 7939The publication costs ofthis article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

Evidence for multiple effects of vitamin D3 on calcium absorption: response of rachitic chicks, with or without partial vitamin D3 repletion, to 1,25-dihydroxyvitamin D3.

Wasserman¹,

Brindak²,

Meyer³

et al. 1982

Proc. Natl. Acad. Sci. U.S.A.

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“…Previous studies using an in vitro translation assay [36] showed that mRNA coding for 28-kDa cholecalcin appears in the chick intestine 2 h after a single calcitriol dose administered to vitamin-Ddeficient birds. The relatively low yield of 28-kDa cholecalcin in the cell-free system compared with that of the 9-kDa protein [14,37] may account for the difference between the short delay for 9-kDa-cholecalcin mRNA stimulation and the later 28-kDa-cholecalcin mRNA induction. However, the changes in the concentrations of both 9-kDa cholecalcin and its mRNA were dissociated in the period immediately following hormonal induction (Fig.…”

Section: Discussionmentioning

confidence: 99%

Cholecalcin (a 9‐kDa cholecalciferol‐induced calcium‐binding protein) messenger RNA

Desplan

Thomasset

1985

European Journal of Biochemistry

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In view of the possible physiological importance of the 9-kDa cholecalcin (a 9000-Mr cholecalciferol-induced calcium-binding protein) in the intestinal transport of calcium in mammals, the gene expression of this protein has been analysed. Its regulation in the digestive tract of the growing rat by calcitriol (1,25-dihydroxycholecalciferol) was studied using a specific cloned [32P]cDNA to 9-kDa cholecalcin. Northern hybridisation studies show that the cDNA sequence hybridises to a single 500 -600-nucleotide species throughout the digestive tract and therefore demonstrate identical 9-kDa-cholecalcin mRNA processing in the whole of the intestine and caecum. The highest concentrations of cholecalcin mRNA occur in the duodenum, proximal jejunum and caecum. The observed differences in 9-kDa-cholecalcin mRNA levels correlate well with both the in vivo variations in cholecalcin itself and with the known intestinal sites of calcium absorption. The whole intestine is able to respond to exogenous calcitriol but the response of the distal intestine and caecum, as measured by the increase in cholecalcin mRNA and corresponding protein, was proportionally higher than in the duodenum. The rapid production of fully functional cholecalcin mRNA, which was detectable as early as 1 h after a single dose of calcitriol to vitamin-D-deficient rats, provides convincing evidence that calcitriol increases 9-kDa cholecalcin production by increasing cholecalcin gene expression at the transcriptional level.Cholecalcin, a cholecalciferol-induced calcium-binding protein which was first isolated from the chick intestine by Wasserman and Taylor [l], belongs to the large family of intracellular proteins which bind calcium with high affinity While the chick produces a single 28000-M, protein (28-kDa cholecalcin), the rat possesses both the 28-kDa cholecalcin, found mainly in the kidney and cerebellum, and a smaller, 9000-M, protein (9-kDa cholecalcin) which is characteristic of the duodenum [3]. The rat intestinal 9-kDa cholecalcin is concentrated in the cytoplasm of the absorptive cells of the duodenum [4] where it accounts for 2% of the soluble protein [3]. Although its exact molecular function remains unclear, mammalian 9-kDa cholecalcin is probably involved in the complex process of intestinal calcium absorption [5], which is under the control of (calcitriol) (1,25-dihydroxycholecalciferol), a calciotropic hormone required for the optimal absorption of calcium by the intestine. Its mechanism of action is apparently steroid-hormone-like. Evidence for this includes, in the rat, the localisation of calcitriol within the nuclei of the intestinal absorptive cells [6], the identification of a specific high-affinity receptor protein [7] and the calcitriol-dependent level of intestinal 9-kDa cholecalcin [3, 81. The synthesis of 9-kDa cholecalcin in a cellfree system from rat duodenal poly(A)-rich RNA has recently been described [9] and a complementary DNA has been synthesised and cloned in pBR322 [lo]. The resulting cloned cDNA (pC 109) hybridis...

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“…Ornithine decarboxylase (EC 4.1.1.17), spermidine N ' -acetyltransferase (EC 2.3.1.57), polyamine oxidase (EC 1.4.3.6). transport activity apparently preceded the synthesis of calbindin [20,25,261. The role of calbindin in the intestinal calcium transport mechanism is still a matter of controversy.…”

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Purification and characterization of spermidine N¹‐acetyltransferase from chick duodenum

Shinki

Suda

1989

European Journal of Biochemistry

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We have reported that spermidine N' -acetyltransferase has a larger role than ornithine decarboxylase in putrescine synthesis in chick duodenum induced by 1 a,25-dihydroxycholecalciferol (calcitriol) [Shinki, T., Kadofuku, T., Sato, T. and Suda, T. (1986) J. Biol. Chem. 261, In the present study, spermidine N'-acetyltransferase was purified from the duodenal cytosol of calcitriol-treated chicks to homogeneity judged by SDS/polyacrylamide gel electrophoresis. The purified enzyme converted spermidine only to N'-acetylspermidine. The apparent molecular mass of the purified spermidine N'-acetyltransferase was found to be 36 kDa by gel filtration on Sephacryl S-200 and 18 kDa by SDS/polyacrylamide gel electrophoresis. When duodenal crude 105000 x g extracts were directly applied to a Sephacryl S-200 column without prior purification, three peaks with spermidine N'-acetyltransferase activity appeared. The first peak was in the void volume, the second peak was in the fraction corresponding to an apparent molecular mass of 70 kDa, and the third peak was in the fraction corresponding to 36 kDa. These results suggest that spermidine N'-acetyltransferase exists as a dimer of the 38 kDa subunits and is stabilized in (a) form(s) bound to other components or proteins in intact cells.Recently, a number of reports have indicated the presence of enzymes acetylating polyamines and histones [l -101. Some of them catalyze the acetylation reaction of either polyamines or histones, but some can catalyse both. Thus, intact cells and crude cell preparations contain a mixture of enzymes capable of catalyzing the formation of acetylated spermidine and spermine using acetylcoenzyme A as a substrate. Of these, enzymes acetylating both polyamines and histones form N8-acetylspermidine, which are not native metabolites in the interconversion of polyamines. Only spermidine/spermine N'-acetyltransferase is considered to play an important role in the regulation of intracellular concentrations of polyamines [4,5,8, 111. This enzyme catalyzes the rate-limiting step of the interconversion of polyamines to form N'-acetylspermidine and N'-acetylspermine, which are further converted to putrescine and spermidine, respectively, by polyamine oxidase [12, 131. Calcitriol, the most potent metabolite of calciol, is now considered to be a hormone which mediates calcium transport in target tissues such as intestine and bone [14-161.

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The relationship between vitamin D-stimulated calcium transport and intestinal calcium-binding protein in the chicken

Cited by 160 publications

References 25 publications

Evidence for multiple effects of vitamin D3 on calcium absorption: response of rachitic chicks, with or without partial vitamin D3 repletion, to 1,25-dihydroxyvitamin D3.

Evidence for multiple effects of vitamin D3 on calcium absorption: response of rachitic chicks, with or without partial vitamin D3 repletion, to 1,25-dihydroxyvitamin D3.

Cholecalcin (a 9‐kDa cholecalciferol‐induced calcium‐binding protein) messenger RNA

Purification and characterization of spermidine N¹‐acetyltransferase from chick duodenum

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The relationship between vitamin D-stimulated calcium transport and intestinal calcium-binding protein in the chicken

Cited by 160 publications

References 25 publications

Evidence for multiple effects of vitamin D3 on calcium absorption: response of rachitic chicks, with or without partial vitamin D3 repletion, to 1,25-dihydroxyvitamin D3.

Evidence for multiple effects of vitamin D3 on calcium absorption: response of rachitic chicks, with or without partial vitamin D3 repletion, to 1,25-dihydroxyvitamin D3.

Cholecalcin (a 9‐kDa cholecalciferol‐induced calcium‐binding protein) messenger RNA

Purification and characterization of spermidine N1‐acetyltransferase from chick duodenum

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Purification and characterization of spermidine N¹‐acetyltransferase from chick duodenum