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Bone Disorder and Reduction of Ascorbic Acid Concentration Induced by Biotin Deficiency in Osteogenic Disorder Rats Unable to Synthesize Ascorbic Acid

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Bone Disorder and Reduction of Ascorbic Acid Concentration Induced by Biotin Deficiency in Osteogenic Disorder Rats Unable to Synthesize Ascorbic Acid J. Clin. Biochem. Nutr., 12, 171-182, 1992 Bone Disorder and Reduction of Ascorbic Acid Concentration Induced by Biotin Deficiency in Osteogenic Disorder Rats Unable to Synthesize Ascorbic Acid Yuji FURUKAWA,1,* Akiko KINOSHITA,1,•õ1 Hiroichi SATOH,1,•õ2 Hiroko KIKUCHI,1, •õ3 Shoko OHKOSHI,1,•õ4 Masaru MAEBASHI,2 Yoshio MAKINO,3 Takao SATO,4 Michiko ITO,1 and Shuichi KIMURA1 1 Laboratory of Nutrition, Department of Food Chemistry, Faculty of Agriculture, Tohoku University, Aoba-ku, Sendai 981, Japan 2 The Second Department of Internal Medicine, School of Medicine, Tohoku University, Aoba-ku, Sendai 980, Japan 3 Makino Dermatology Clinic, Aoba-ku, Sendai 981, Japan 4 Division of Internal Medicine, National Sendai Hospital, Miyagino-ku, Sendai 983, Japan (Received January 13, 1992) Summary The developmental mechanism of the bone disorder in- duced by biotin deficiency was studied in osteogenic disorder rats, animals that have a hereditary defect in ascorbic acid-synthesizing ability. The osteogenic disorder rats fed a biotin-deficient diet containing raw egg white were afflicted with bone abnormality including a hunch in the vertebral column. In the case of biotin deficiency, although the ascorbic acid content in the diet was in excess of the required amount, ascorbic acid levels of the plasma and the organs in the rats were significant lower than those of control rats. This suggests that the bone disorder induced by biotin deficiency in the rats may result from the promotion of ascorbic acid consumption or the impairment of ascorbic acid incorporation in the animal tissues. Key Words: osteogenic disorder rat, biotin deficiency, ascorbic acid, bone disorder, acetyl-CoA carboxylase Biotin serves as an essential cofactor for four carboxylases, namely, acetyl- *To whom correspondence should be addressed . Present address: •õ1Microbiological Science Laboratory, Institute for Fundamental Research , Suntory Ltd., Shimamoto, Osaka 618, Japan. •õ2Nippon Sanso Corporation, Technical Depart- ment, Food Division, Project Development Center, Yoshimi, Saitama 355-01, Japan . •õ3Yakult Central Institute for Microbiological Research, Kunitachi 186, Japan. •õ4The Second Department of Internal Medicine, School of Medicine, Tohoku University, Sendai 980, Japan. 171 172 Y. FURUKAWA et al. CoA carboxylase, pyruvate carboxylase, propionyl-CoA carboxylase, and 3- methylcrotonyl-CoA carboxylase, each of which catalyzes the incorporation of bicarbonate into a substrate as a carboxyl group in intermediary metabolism in mammals [1-3]. Heavy feeding of raw egg white, which contains avidin, a component protein in the egg white that strongly binds biotin, induces biotin deficiency in man and animals [4, 5]. Major characteristic pathological symptoms of biotin deficiency are growth reduction, anorexia, depigmentation, seborrheic dermatitis, and alopecia [6, 7]. In 1942, a bone disorder was observed by Sallivan et al. [8] in rats with experimentally produced biotin deficiency. They described in detail the abnormality of the posture and difficulty in walking. Since then, however, there have been reports of studies on the relationship between the biotin deficiency and the bone disorder in only mouse [9, 10] and chicken [11-13]. We previously showed that the lumbo-sacral portion of the spine of biotin- deficient Wistar strain rats become arched [14]. The result conformed with the observation previously mentioned by Sallivan et al. [8]. Dakshinamurti and Mistry [15] demonstrated that in biotin-deficient rats made so by feeding of a diet containing raw egg white, the liver and adrenals contained less than half of the total ascorbic acid of the control rats. They also indicated that a decrease in L-gulonolactone oxidase activity in the L-ascorbic acid synthesis system produced the reduction in ascorbic acid content. The bone disorder brought about by the biotin deficiency may be attributed to the depression in collagen synthesis, which synthesis requires ascorbic acid for the proline hydroxylation. In this study, osteogenic disorder Shionogi (ODS) rats [16, 17], which are hereditarily defective in ascorbic acid-synthesizing ability, were used. Use of this experimental animal will enable exclusion of the influence of the biotin deficiency on ascorbic acid synthesis. The purpose of the present study was to determine the relation between biotin deficiency and development of bone abnormality induced by the vitamin defi- ciency in these rats. MATERIALS AND METHODS Animals, diets and experimental design. ODS-od/od rats were generously supplied by Aburahi Laboratories, Shionogi & Co., Ltd., Osaka. In experiment 1, male ODS rats with an average starting weight of 70 g were divided into two groups of sixteen rats per group. All animals were fed ad libitum a biotin-deficient diet (20% freeze-dried raw egg white as protein source) contain- ing 200 mg of ascorbic acid per 100 g diet. During the experiment the rats were given free access to distilled water. The control group and the biotin-deficient group were given intraperitoneal injection of 0.5 ml saline containing 100 ,ug biotin and saline each week, respectively. Animals were kept in individual cages with wire-mesh floors. Diet bowls, water bottles, and the cages were kept as clean as possible for the prevention of coprophagy. On day 56 of the dietary regimen, the J. Clin. Biochem. Nutr. BIOTIN DEFICIENCY IN OSTEOGENIC DISORDER RATS 173 control and biotin-deficient rats were each divided into two groups. One group of each received a diet devoid of ascorbic acid (AsA- groups) for 10 days. The other group of each type was fed the diet supplemented with 200 mg ascorbic acid per 100 g diet, i.e., the same diet as the starting diet in this experiment, for 10 days. The experiment was carried out to determine the liver acetyl-CoA carboxylase activity and ascorbic acid concentration in the plasma. In experiment 2, animals, diet and the conditions of maintenance of the animals were the same as experiment 1. On day 94, the control and biotin-deficient rats were each divided into two groups, and each group of the counterpart of experiment 1 was fed the same diet as in experiment 1 for 5 days. The animals of this experiment were used for the observation of bone abnormality and the determination of pyruvic acid and lactic acid in the plasma and ascorbic acid concentration in the plasma and liver. The percentage composition of the diet was as follows: sucrose, 10; corn starch, 50; soybean oil, 6; mineral mixture, 6; vitamin mixture (biotin free), 2; cellulose powder, 6; and freeze-dried egg white, 20. One hundred grams of the vitamin mixture contains 100 mg of vitamin A acetate, 120 mg of thiamine' HC1, 400 mg of riboflavin, 80 mg of pyridoxine • HC1, 0.05 mg of vitamin B12,300 mg of ascorbic acid, 500 mg of vitamin E acetate, 10,000 IU of vitamin D3, 520 mg of vitamin K3, 20 mg of folic acid, 500 mg of D-pantothenic acid, 500 mg of p- aminobenzoic acid, 600 mg of nicotinic acid, 600 mg of inositol, 20 g of choline chloride and cellulose powder to make 100 g (Prescription by Oriental Yeast Co., Ltd., Tokyo). Mineral mixtures according to Harper [18] were obtained from Oriental Yeast. On day 65 (Exp. 1) and 99 (Exp. 2), the rats were anesthetized with ether and blood was drawn into heparinized syringes from the abdominal aorta. After washing of the liver with saline, the liver, kidney, and adrenal glands were removed and weighed. Determination of biotin contents of plasma and organs. Biotin concentra- tions in plasma and organs were determined microbiologically. The test organism was Lactobacillus plantarum (ATCC 8014). Samples of plasma or organ homog- enates were acid hydrolyzed prior to the assay. Two hundred microliters of 5.6 N sulfuric acid was added to 200 1 of plasma or the homogenate in a screw-capped tube. After the tubes had been autoclaved at 1.0 kg/cm2 pressure for 2 h under N2, the hydrolysates were neutralized with 5 N sodium hydroxide. Determination of acetyl-CoA carboxylase activity. The activity of liver acetyl-CoA carboxylase was measured with KH14CO3 (specific activity, 0.25 mCi/ mmol) essentially according to the method described by Tanabe et al. [19]. The rat livers were dipped in ice-cold saline and cut into small pieces and homogenized in two volumes of the buffer A with a Teflon-glass homogenizer under cooling in an ice-water bath. Buffer A was 50 mM Tris-HCI buffer, pH 8.0, containing 0.25 M sucrose, 1 mM EDTA, 5 mM mercaptoethanol, 0.5 mM phenylmethylsulfonylfluo- ride (inhibitor of serine proteases), 5 p g/ml each of several protease inhibitors Vol. 12, No. 3, 1992 174 Y. FURUKAWA et al. (leupeptin, antipain, chymostatin, pepstatin A), and 50 mM sodium fluoride. The homogenates were centrifuged at 13,000><g for 45 min. The fat layer at the top was discarded, and 0.5 ml of the supernatant was passed through a Sephadex G-50 column (10 mm x 60 mm) equilibrated with buffer A to remove endogenous sub- strates. One milliliter of the eluates was collected in each fraction tube. The eluates of fractions 3 and 4 were pooled as the crude enzyme preparation. Activation of the crude enzyme and measurement of the enzyme activity were carried out essentially according to the method of Tanabe et al. [19]. Ascorbic acid determination of plasma and organs. Plasma ascorbic acid was quantified by the o-phenylenediamine fluorescence method [20], and measure- ment of total ascorbic acid in the liver was performed with 2,4-dinitrophenylhydra- zine [21]. Determination of pyruvic acid and lactic acid in blood and liver. High- performance liquid chromatography was used to determine the blood levels of pyruvate and lactate. The apparatus was a Hitachi 655-11 Liquid Chromatograph (Hitachi, Tokyo) equipped with a UV detector (Waters Lambda-Max Model 481 LC spectrophotometer, Nihon Waters, Tokyo) set at 214 nm.
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