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At least 19 recordsLinked to original sources
PubMed1995

Assessing adequacy of cholecalciferol supplementation in chicks using plasma cholecalciferol metabolite concentrations as an indicator.

Cholecalciferol (vitamin D) deficiency rickets remains an occasional problem in poultry. Diagnosis currently relies on analysis of feed and histopathological examination of bone. These experiments were designed to provide data that might allow diagnosis of cholecalciferol deficiency on the basis of plasma concentrations of 25-hydroxycholecalciferol, a circulating metabolite of cholecalciferol. Day-old broiler chicks were fed corn-soybean meal or purified ingredient cholecalciferol-deficient diets supplemented with 0, 5, 10, 15, 20, 25, 37.5 or 75 micrograms cholecalciferol/kg diet. Plasma and bone samples were collected 21 d later. Chicks fed the unsupplemented purified ingredient diet became truly deficient, having no detectable plasma concentrations of the cholecalciferol metabolites 25-hydroxycholecalciferol, 1,25-dihydroxycholecalciferol, or 24,25-dihydroxycholecalciferol. Chicks fed the corn-soybean meal diet without supplementation had low but detectable concentrations of both 25-hydroxycholecalciferol and 1,25-dihydroxycholecalciferol in plasma. Body weight, bone calcium and bone phosphorus concentrations of chicks fed the corn-soybean meal diet suggest that the cholecalciferol requirement of broiler chicks is at least 10 micrograms/kg diet. At this dietary level of cholecalciferol, plasma 25-dihydroxycholecalciferol concentration was 12.5 nmol/L. One hundred percent of the theoretical maximal response in body weight and bone calcium content was seen at 20 micrograms cholecalciferol/kg diet, which increased plasma 25-hydroxycholecalciferol concentration to 25 nmol/L in the chicks fed the corn-soybean meal diet. These data provide a nomogram of plasma 25-dihydroxycholecalciferol concentration that can be expected from including different concentrations of cholecalciferol in the diet, and also offer a means of diagnosing cholecalciferol deficiency in field cases of tickets.

24,25-Dihydroxyvitamin D 3↗
PubMed1995

Cholecalciferol 25-hydroxylation is similar in liver microsomes from male and female rats when cholecalciferol concentration is low.

We compared cholecalciferol 25-hydroxylation in liver microsomes of male and female rats. The rate of production of 25-hydroxycholecalciferol was similar in liver microsomes from female rats and those from male rats when cholecalciferol concentration ranged from 50 to 200 nmol/L. The liver cytosolic fraction stimulated the 25-hydroxylase activity of the microsomes up to 100% in both male and female rats at 44 nmol/L cholecalciferol. Cytosol metabolized cholecalciferol to a currently unidentified metabolite. At 300 nmol/L cholecalciferol, synthesis of the cytosolic metabolite was 100% greater than at 100 nmol/L and coincided with 32% lower synthesis of 25-hydroxycholecalciferol. These results suggest similar 25-hydroxy-lase activity in liver microsomes from male and female rats and similar ability of liver cytosol from these rats to stimulate 25-hydroxylation at low nanomolar concentrations of cholecalciferol, whereas inhibitory effects of cytosol at higher concentrations of cholecalciferol were shown.

Animals↗
PubMed1999

Cholecalciferol and 25-hydroxycholecalciferol content of chicken egg yolk as affected by the cholecalciferol content of feed.

The predominant source of vitamin D is the synthesis of cholecalciferol in the skin by the action of sunlight; however, due to the relative lack of sunlight, the intake of vitamin D from food is emphasized during winter, especially in the northern countries. Only a few foods (fish, eggs, wild mushrooms, meat, and milk) are natural sources of vitamin D. In addition, the content of vitamin D in foods is generally low, and some groups of people obtain amounts of vitamin D that are too small from their diet. The present study was designed to determine whether it is possible to increase the vitamin D content of egg yolk by giving hens feed containing elevated levels of cholecalciferol. Three cholecalciferol levels were tested: 26.6 (1064), 62.4 (2496), and 216 microgram (8640 IU)/kg feed. Egg yolk samples were taken after 0, 4, 5, and 6 weeks and were assayed for the presence of cholecalciferol and 25-hydroxycholecalciferol using an HPLC method. According to the present study, there was strong positive correlation between cholecalciferol content in poultry feed and cholecalciferol (r = 0. 995) and 25-hydroxycholecalciferol (r = 0.941) content in egg yolk.

Animal Feed↗
PubMed1980

The effect of various cholecalciferol-related substances on the biosynthesis of the cholecalciferol-dependent calcium-binding protein in the small intestine of the rachitic chick and its relation to rickets.

Rachitic chicks were injected with different dose-levels of cholecalciferol and several cholecalciferol-related substances, i.e., dihydrotachysterol 3, ergocalciferol, 5,6-transcholecalciferol and 25-hydroxycholecalciferol. The response to treatment was assayed by the amount of cholecalciferol-dependent calcium-binding protein produced in the mucosa of the small intestine. The biological activity of these substances in the healing of rickets in the rat was also estimated except for ergocalciferol. The relative potencies in stimulating calcium-binding protein production were: 25-hydroxycholecalciferol > cholecalciferol > 5,6-trans-cholecalciferol > ergocalciferol > dihydrotachysterol 3.

Animals↗
PubMed1976

High-performance liquid chromatographic analysis of vitamins I: quantitation of cholecalciferol or ergocalciferol in presence of photochemical isomers of the provitamin and application to cholecalciferol resins.

A high-performance liquid chromatographic (HPLC) procedure was developed for the quantitative determination of cholecalciferol or ergocalciferol in the presence of the photochemical isomers of the provitamin. Separation is also achieved from various common reaction products encountered in the vitamin synthesis as well as other fat-soluble vitamins. The method was applied to the routine analysis of cholecalciferol resins, and experimental data are set forth. A comparison of the HPLC method to the AOAC biological and chemical procedures shows that the HPLC method most closely approximates the antirachitic activity of a cholecalciferol sample. The specificity, sensitivity, and reproducibility of the method make it applicable to various vitamin samples containing cholecalciferol or ergocalciferol.

Biological Assay↗
PubMed1971

Synthesis of (1,2- 3 H 2 )cholecalciferol and metabolism of (4- 14 C,1,2- 3 H 2 )- and (4- 14 C,1- 3 H)-cholecalciferol in rachitic rats and chicks.

[1,2-(3)H(2)]Cholecalciferol has been synthesized with a specific radioactivity of 508mCi/mmol by using tristriphenylphosphinerhodium chloride, the homogeneous hydrogen catalyst. With doses of 125ng (5i.u.) of [4-(14)C,1-(3)H(2)]cholecalciferol the tissue distribution in rachitic rats of cholecalciferol and its metabolites (25-hydroxycholecalciferol and peak P material) was similar to that found in chicken with 500ng doses of the double-labelled vitamin. The only exceptions were rat kidney, with a very high concentration of vitamin D, and rat blood, with a higher proportion of peak P material, containing a substance formed from vitamin D with the loss of hydrogen from C-1. Substance P formed from [4-(14)C,1,2-(3)H(2)]cholecalciferol retained 36% of (3)H, the amount expected from its distribution between C-1 and C-2, the (3)H at C-1 being lost. 25-Hydroxycholecalciferol does not seem to have any specific intracellular localization within the intestine of rachitic chicks. The (3)H-deficient substance P was present in the intestine and bone 1h after a dose of vitamin D and 30min after 25-hydroxycholecalciferol. There was very little 25-hydroxycholecalciferol in intestine at any time-interval, but bone and blood continued to take it up over the 8h experimental period. It is suggested that the intestinal (3)H-deficient substance P originates from outside this tissue. The polar metabolite found in blood and which has retained its (3)H at C-1 is not a precursor of the intestinal (3)H-deficient substance P.

Animals↗
PubMed1978

Incorportion of oxygen-18 into the 25-position of cholecalciferol by hepatic cholecalciferol 25-hydroxylase.

The oxygen enzymically inserted as a hydroxy function by rat liver post-mitochondrial fraction into the 25-position of cholecalciferol to giver 25-hydroxycholecaliferol is derived exclusively from molecular O2. Therefore like the other two cholecalciferol hydroxylases, i.e. 25-hydroxycholecalciferol 1alpha-hydroxylase and 25-hydroxycholecalciferol 24-hydroxylase, the cholecalciferol 25-hydroxylase is also a mono-oxygenase ('mixed-function oxidase').

Animals↗
PubMed2003

A comparison between cholecalciferol and 25-OH-cholecalciferol on performance and eggshell quality of hens fed different levels of calcium and phosphorus.

Two experiments were conducted to determine whether the presence of 25-OH-cholecalciferol (25-OH-D3) as compared to vitamin D3 produces any beneficial effect on shell quality of laying hens. Experiment 1 consisted of a 4 x 2 factorial arrangement of the treatments with four determined Ca levels (3.34, 4.3, 4.73, and 4.94%) and two sources of vitamin D (vitamin D3 and 25-OH-D3, which were used at 69 microg/kg diet or 2,760 IU/kg diet). Experiment 2 consisted of a 3 x 2 x 2 factorial arrangement of the treatments with three determined levels of nonphytate P (NPP) (0.11, 0.21, and 0.41%), two levels of phytase (0 and 300 U/kg diet), and two sources of vitamin D (vitamin D3 and 25-OH-D3, which were used at 69 microg/kg diet, the equivalent of 2,760 IU/kg diet). Substitution of vitamin D3 with 25-OH-D3 in neither of the experiments produced any beneficial effect on shell quality. A Ca level of 3.34%, which provided the birds with 3.63 g Ca/hen per d, was adequate for performance and eggshell quality. The NPP level of 0.11% was not sufficient to support performance. However, a NPP level of 0.21% was adequate and resulted in performance that was comparable to that of birds fed the 0.41% NPP diet. The presence of phytase did not have an effect on performance but reduced several indices of the shell quality. In conclusion, under the conditions of the current experiments, the use of 25-OH-D3 did not provide any advantage for shell quality or production performance.

6-Phytase↗
PubMed1991

Cholecalciferol has no effect on calcium and inorganic phosphorus balance in a naturally cholecalciferol-deplete subterranean mammal, the naked mole rat (Heterocephalus glaber).

Naked mole rats, Heterocephalus glaber, have no obvious source of cholecalciferol (D3) available to them, given their underground habitat and tubiferous diet. They have undetectable levels of 25-OH-D3 and as such appear to be naturally deplete in D3. The effect of an oral D3 supplement on mineral balance and homeostasis was therefore investigated. This D3 treatment did not affect circulating levels of Ca2+ and inorganic phosphorus (P(i]. Nor did D3 treatment affect mineral intake and absorption. The Ca2+ and P(i) present in the food was efficiently extracted and absorbed, resulting in an apparent fractional absorption (AFA) efficiency exceeding 98%. Irrespective of D3 treatment, the amount of Ca2+ and P(i) absorbed was positively correlated with the amount ingested, suggesting that intestinal uptake is by a passive D3-independent process. After D3 supplementation urinary Ca2+ secretion was unchanged; however, the amount of P(i) excreted in the urine increased (P less than or equal to 0.05). This resulted in a concomitant decline in P(i) AFR (P less than or equal to 0.02 from 99.95 +/- 0.02% to 99.82 +/- 0.03%). Almost all the Ca2+ and P(i) in the glomerular filtrate were reabsorbed, facilitating AFR efficiencies that approach physiological maxima (greater than 99%). Changes in AFR efficiency with D3 supplementation are therefore of no biological significance. Net mineral flux of both elements, irrespective of D3 treatment, was positive. It is speculated that the ever-growing incisors of these animals act as mineral dumps and assist in the tight regulation of plasma Ca2+ and P(i). These data suggest that naked mole rats utilize mechanisms independent of D3 in regulating mineral homeostasis and are therefore well-adapted to an environment devoid of sunlight.

Animals↗
PubMed1983

Effects of cholecalciferol (vitamin D3)-binding proteins and anti-cytochrome b5 immunoglobulin on cholecalciferol 25-hydroxylase activities of rabbit liver microsomes and mitochondria.

The effects of cholecalciferol (vitamin D3)-binding proteins and anti-cytochrome b5 immunoglobulin were studied on vitamin D3 25-hydroxylase activities of microsomes and mitochondria under various experimental conditions. The vitamin D3-binding protein in serum as well as in the liver postmicrosomal supernatant (cellular vitamin D3-binding protein), but not serum albumin and ovalbumin, stimulated vitamin D3 25-hydroxylase activities of microsomes and mitochondria. The optimum pH range was from 7.3 to 8.0. Anti-cytochrome b5 immunoglobulin did not affect microsomal vitamin D3 25-hydroxylase activity.

Animals↗
PubMed1978

Comparative studies on the 25-hydroxylations of cholecalciferol and 1 alpha-hydroxycholecalfierol in perfused rat liver.

The 25-hydroxylations of [(3)H]cholecalciferol and 1alpha-hydroxy[(3)H]cholecalciferol in perfused rat liver were compared. Results showed that about twice as much 1alpha(OH)D(3) (1alpha-hydroxycholecalciferol) was incorporated into the liver as cholecalciferol. 25-Hydroxy[(3)H]cholecalciferol and 1alpha-25-dihydroxy[(3)H]cholecalciferol were not incorporated significantly. Livers isolated from vitamin D-deficient rats formed the 25-hydroxy derivatives of cholecalciferol and 1alpha(OH)D(3) respectively linearly with time for at least 120min. The rate of 1alpha,25(OH)(2)D(3) (1alpha,25-dihydroxycholecalciferol) production increased exactly 10-fold on successive 10-fold increases in the dose of 1alpha(OH)D(3), suggesting that hepatic 25-hydroxylation of 1alpha(OH)D(3) is not under metabolic control. On the other hand, the rate of conversion of cholecalciferol into 25(OH)D(3) (25-hydroxycholecalciferol) did not increase linearly with increase in the amount of cholecalciferol in the perfusate. The 25-hydroxylation of cholecalciferol seemed to proceed at a similar rate to that of 1alpha(OH)D(3) at doses of less than 1nmol, but with doses of more than 2.5nmol, the conversion of cholecalciferol into 25(OH)D(3) became much less efficient, though the linear relation between the amounts of substrate and product was maintained. A reciprocal plot of data on the 25-hydroxylation of cholecalciferol gave two K(m) values of about 5.6nm and 1.0mum, whereas that for the 25-hydroxylation of 1alpha(OH)D(3) gave a single K(m) value of about 2.0mum. These results suggest that there are two modes of 25-hydroxylation of cholecalciferol in the liver, which seem to be closely related to the mechanism of control of 25(OH)D(3) production by the liver.

Animals↗
PubMed1998

Cholecalciferol induces prostaglandin E2 biosynthesis and transglutaminase activity in human keratinocytes.

In this study, we examined the effects of cholecalciferol, a primary keratinocyte metabolite and precursor of the hydroxylated form of vitamin D3, 1alpha,25-dihydroxyvitamin D3 [1alpha,25(OH)2D3], on prostaglandin E2 (PGE2) production in human keratinocytes by examining its respective effects on cyclooxygenase-1 (COX-1), cyclooxygenase-2 (COX-2), and cytosolic phospholipase A2 (cPLA2) expression, the rate-limiting enzymes regulating PGE2 biosynthesis and differentiation of keratinocytes. Cholecalciferol induced PGE2 production, whereas 1alpha,25(OH)2D3 had no effect on PGE2 production both in normal human epidermal keratinocytes and in the immortalized human keratinocyte cell line, HaCaT. In HaCaT cells, neither COX-1 mRNA nor protein was detectable without stimulation and COX-1 expression did not increase in response to cholecalciferol treatment. Although cPLA2 mRNA and protein were constitutively expressed in untreated HaCaT cells, expression levels did not increase in response to cholecalciferol treatment; however, unlike COX-1 and cPLA2 expression, COX-2 mRNA and COX-2 protein expression increased in response to cholecalciferol treatment. Calphostin C, a potent protein kinase C inhibitor, significantly reduced cholecalciferol-induced PGE2 production by inhibiting cholecalciferol-enhanced COX-2 mRNA and protein expression. These results indicate that (i) 1alpha,25(OH)2D3 does not induce PGE2 biosynthesis in keratinocytes, (ii) cholecalciferol-induced PGE2 production is primarily COX-2 dependent, and (iii) cholecalciferol enhances both COX-2 mRNA and protein expression, via a protein kinase C-dependent mechanism in human keratinocytes. Furthermore, cholecalciferol increased total cellular transglutaminase activity dose dependently, suggesting a potential role for cholecalciferol in regulating the differentiation of human keratinocytes.

Arachidonic Acid↗
PubMed1997

Effect of 1,25-dihydroxycholecalciferol, cholecalciferol, and fluorescent lights on the development of tibial dyschondroplasia and rickets in broiler chickens.

Experiments were conducted to determine whether dietary 1,25-dihydroxycholecalciferol [1,25-(OH)2D3] will alleviate a cholecalciferol deficiency induced by low dietary cholecalciferol and no fluorescent lighting and to determine cholecalciferol requirements as influenced by fluorescent lighting or 1,25-(OH)2D3. In each study, nutritionally complete basal diets were fed to broiler cockerels from 1 to 16 d of age. Experiment 1 had a 2 x 2 x 2 factorial arrangement of treatments with 1,25-(OH)2D3 at 0 and 10 micrograms/kg, cholecalciferol at 2.75 and 27.5 micrograms/kg, and fluorescent lights on or off. Experiments 2 to 4 had four levels of dietary cholecalciferol (0, 5.0, 27.5, and 50.0 micrograms/kg) and fluorescent lights on or off (Experiment 2) or 1,25-(OH)2D3 at 0 and 10 micrograms/kg (Experiments 3 and 4). In Experiment 1, fluorescent lighting increased bone ash, and decreased the incidence and severity of rickets at 2.75 micrograms/kg cholecalciferol and 0 microgram/kg 1,25-(OH)2D3 and reduced the severity of TD at both levels of cholecalciferol and 0 microgram/kg 1,25-(OH)2D3. In all cases 1,25-(OH)2D3 improved bone ash. The metabolite also decreased the incidence and severity of TD at both cholecalciferol levels with lights off and decreased the incidence and severity of rickets at 2.75 micrograms/kg cholecalciferol and lights off. In the absence of fluorescent lighting and 1,25-(OH)2D3 27.5 micrograms/kg cholecalciferol reduced the incidence and severity of rickets to levels equivalent to those produced by either fluorescent lighting or 1,25-(OH)2D3 alone (Experiments 2, 3, and 4). However, even 50.0 micrograms/kg cholecalciferol was not as effective as fluorescent lights or 1,25-(OH)2D3 in reducing the incidence and severity of TD.

Animals↗
PubMed1978

Synthesis of 1 alpha-hydroxy[7-3H]cholecalciferol and its metabolism in the chick.

1. 1 alpha-Hydroxy[7-3H]cholecalciferol (specific radioactivity of 2-Ci/mmol) was synthesized, and its metabolism in chicks studied. 2. 1 alpha-Hydroxy[7-3H]cholecalciferol was metabolized very rapidly in the chick to 1 alpha,25-dihydroxy[7-3H]cholecalciferol and to a metabolite less polar than 1 alpha-hydroxycholecalciferol. Intestine exhibited highest accumulation of 1 alpha-25-dihydroxy[7-3H]cholecalciferol, and liver exhibited highest accumulation of the non-polar metabolite. 3. Tissue uptake of 1 alpha-hydroxy[7-3H]cholecalciferol and its metabolites in chicks that were dosed continuously for 16 days with 1 alpha-hydroxy[7-3H]cholecalciferol did not exceed by very much that observed in tissues obtained from chicks that were dosed with a single injection of 1 alpha-hydroxy[7-3H]cholecalciferol 24 h before killing, except for liver and kidney. 4. Lowest accumulation of metabolites was noted in muscle and bone, and for the latter, highest uptake of 1 alpha,25-dihydroxy[7-3H]cholecalciferol was noted in the epiphysial periosteum and the metaphysis. 5. Formation of 1 alpha,24,25-trihydroxy[7-3H]cholecalciferol was not observed in the chicks that were dosed continuously with 1 alpha-hydroxy[7-3H]cholecalciferol, despite the fact that plasma calcium and phosphorus were normal and despite the presence of renal 24-hydroxylase activity. 6. The vitamin D status of the chicks did not appear to affect the metabolic profile of the administered 1 alpha-hydroxy[7-3H]cholecalciferol.

Animals↗
PubMed2000

Evaluation of cholecalciferol sources using broiler chick bioassays.

Three experiments were conducted to test the potencies of nine sources of cholecalciferol using a chick bioassay. The tested products were compared with a Sigma Reference Standard (SRS). All of the diets fed to the chicks were prepared from corn-soybean meal. Each of the products was in premix form containing cholecalciferol. Their physical characteristics reflected the methods used to produce the premixes. They were categorized as spray-dried or drum-dried in the beadlet or flake form. Basal diets without cholecalciferol were used in all experiments. For Experiments 1 and 2, the designs were a 2 x 3 factorial arrangement using three different cholecalciferol products and two levels of 200 and 400 IU/kg dietary cholecalciferol. For both experiments, three additional SRS levels of 600, 800, and 1,000 IU/kg were included in the studies as positive controls as there is a possibility that the cholecalciferol products being tested may exhibit activity higher than the amount stated. In Experiment 3, a 3 x 4 factorial arrangement was used, which was represented by three cholecalciferol products and four levels of dietary cholecalciferol at 150, 300, 600, and 1,200 IU/kg. By using the slope ratio analysis, the potencies of the products from the three experiments were between 86 and 118%. In Experiment 3, the requirement of chicks for cholecalciferol using the three tested products, as determined by a nonlinear regression model based on bone ash, were 843+/-85, 911+/-106, and 986+/-131 IU/kg of diet as compared with 915+/-82 IU/kg when using the SRS. The results from these studies indicate that the chemical assays used to determine the cholecalciferol activity of these products were very reliable.

Animal Feed↗