A Study of the Association between Serum Bone-Specific Alkaline Phosphatase and Serum Phosphorus Concentration or Dietary Phosphorus Intake

Alkaline phosphatase (ALP) hydrolyzes a variety of monophosphate esters into phosphoric acid and alcohol at a high optimum pH (pH 8-10). Human ALPs are classified into four types: tissue-non specific (TNSALP, liver/bone/kidney), intestinal, placental, and germ cell types. Based on studies of hypopho...

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Published inJournal of Nutritional Science and Vitaminology Vol. 58; no. 6; pp. 442 - 445
Main Authors HOSOI, Takayuki, GOSEKI-SONE, Masae, HARAIKAWA, Mayu, KAWAMURA, Yuka, SUGIMOTO, Aoi, TANABE, Rieko, MICHIGAMI, Toshimi, SOGABE, Natsuko
Format Journal Article
LanguageEnglish
Published Tokyo Center for Academic Publications Japan 2012
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ISSN0301-4800
1881-7742
DOI10.3177/jnsv.58.442

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Abstract Alkaline phosphatase (ALP) hydrolyzes a variety of monophosphate esters into phosphoric acid and alcohol at a high optimum pH (pH 8-10). Human ALPs are classified into four types: tissue-non specific (TNSALP, liver/bone/kidney), intestinal, placental, and germ cell types. Based on studies of hypophosphatasia (HPP), which is a systemic bone disease caused by the presence of either one or two pathologic mutations in ALPL that encodes TNSALP, TNSALP was suggested to be indispensable for skeletal mineralization. In this study, we explored the possibility that dietary nutrients contribute to regulate serum bone-specific ALP (BAP) activity. Serum biochemical parameters, such as serum ALP, BAP, osteocalcin, and fibroblast growth factor 23 (FGF23), were measured in healthy young subjects (n=193). Dietary nutrient intakes were measured based on 3-d food records before the day of blood examinations. The presence of a carrier of the deletion of T at nucleotide 1559 (c.1559delT), which has been reported to be the most frequent in Japanese HPP, was not detected in any subject. By the analysis of BAP activity and other biochemical parameters or dietary nutrient intakes, we obtained significant correlations between BAP activity and serum phosphorus (r=−0.165, p=0.022), calcium intake (mg/1,000 kcal/d) (r=−0.186, p=0.010), or phosphorus intake (mg/1,000 kcal/d) (r=−0.226, p=0.002). Further study on the regulation of BAP activity and calcium and/or phosphorus homeostasis will provide useful data for improving skeletal health.
AbstractList Alkaline phosphatase (ALP) hydrolyzes a variety of monophosphate esters into phosphoric acid and alcohol at a high optimum pH (pH 8-10). Human ALPs are classified into four types: tissue-non specific (TNSALP, liver/bone/kidney), intestinal, placental, and germ cell types. Based on studies of hypophosphatasia (HPP), which is a systemic bone disease caused by the presence of either one or two pathologic mutations in ALPL that encodes TNSALP, TNSALP was suggested to be indispensable for skeletal mineralization. In this study, we explored the possibility that dietary nutrients contribute to regulate serum bone-specific ALP (BAP) activity. Serum biochemical parameters, such as serum ALP, BAP, osteocalcin, and fibroblast growth factor 23 (FGF23), were measured in healthy young subjects (n=193). Dietary nutrient intakes were measured based on 3-d food records before the day of blood examinations. The presence of a carrier of the deletion of T at nucleotide 1559 (c.1559delT), which has been reported to be the most frequent in Japanese HPP, was not detected in any subject. By the analysis of BAP activity and other biochemical parameters or dietary nutrient intakes, we obtained significant correlations between BAP activity and serum phosphorus (r=-0.165, p=0.022), calcium intake (mg/1,000 kcal/d) (r=-0.186, p=0.010), or phosphorus intake (mg/1,000 kcal/d) (r=-0.226, p=0.002). Further study on the regulation of BAP activity and calcium and/or phosphorus homeostasis will provide useful data for improving skeletal health.
Alkaline phosphatase (ALP) hydrolyzes a variety of monophosphate esters into phosphoric acid and alcohol at a high optimum pH (pH 8-10). Human ALPs are classified into four types: tissue-non specific (TNSALP, liver/bone/kidney), intestinal, placental, and germ cell types. Based on studies of hypophosphatasia (HPP), which is a systemic bone disease caused by the presence of either one or two pathologic mutations in ALPL that encodes TNSALP, TNSALP was suggested to be indispensable for skeletal mineralization. In this study, we explored the possibility that dietary nutrients contribute to regulate serum bone-specific ALP (BAP) activity. Serum biochemical parameters, such as serum ALP, BAP, osteocalcin, and fibroblast growth factor 23 (FGF23), were measured in healthy young subjects (n=193). Dietary nutrient intakes were measured based on 3-d food records before the day of blood examinations. The presence of a carrier of the deletion of T at nucleotide 1559 (c.1559delT), which has been reported to be the most frequent in Japanese HPP, was not detected in any subject. By the analysis of BAP activity and other biochemical parameters or dietary nutrient intakes, we obtained significant correlations between BAP activity and serum phosphorus (r=−0.165, p=0.022), calcium intake (mg/1,000 kcal/d) (r=−0.186, p=0.010), or phosphorus intake (mg/1,000 kcal/d) (r=−0.226, p=0.002). Further study on the regulation of BAP activity and calcium and/or phosphorus homeostasis will provide useful data for improving skeletal health.
Author MICHIGAMI, Toshimi
GOSEKI-SONE, Masae
HARAIKAWA, Mayu
KAWAMURA, Yuka
HOSOI, Takayuki
SUGIMOTO, Aoi
TANABE, Rieko
SOGABE, Natsuko
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  organization: Department of Food and Nutrition, Faculty of Human Sciences and Design, Japan Women's University
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  fullname: HARAIKAWA, Mayu
  organization: Department of Food and Nutrition, Faculty of Human Sciences and Design, Japan Women's University
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  fullname: KAWAMURA, Yuka
  organization: Department of Food and Nutrition, Faculty of Human Sciences and Design, Japan Women's University
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  fullname: SUGIMOTO, Aoi
  organization: Department of Food and Nutrition, Faculty of Human Sciences and Design, Japan Women's University
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  fullname: TANABE, Rieko
  organization: Department of Food and Nutrition, Faculty of Human Sciences and Design, Japan Women's University
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  fullname: MICHIGAMI, Toshimi
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Cites_doi 10.2220/biomedres.29.213
10.1093/hmg/3.9.1683
10.1359/jbmr.1998.13.12.1827
10.1016/S0021-9258(18)43072-4
10.1016/0003-2697(67)90110-8
10.1016/0009-8981(72)90302-6
10.1111/j.1742-4658.2005.04597.x
10.1007/s00431-004-1612-9
10.1146/annurev.nu.08.070188.003025
10.1093/ajcn/67.6.1273
10.1359/JBMR.041229
10.1016/S0021-9258(18)37887-6
10.1016/S0021-9258(18)37885-2
10.1006/bbrc.1999.1624
10.1016/S0006-291X(02)02646-3
10.1007/s774-002-8443-4
10.1016/S0021-9258(18)37886-4
10.1359/jbmr.1999.14.12.2015
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Keywords Human
Alkaline phosphatase
Fibroblast growth factor
Correlation
fibroblast growth factor 2 3
Enzyme
Phosphoric monoester hydrolases
Metabolic diseases
Phosphorus
Esterases
Concentration
Enzymopathy
Hypophosphatasia
Genetic disease
Osteoarticular system
bone-specific alkaline phosphatase
Food intake
dietary nutrient intake
Hydrolases
Bone
serum phosphorus
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References 20) Goseki-Sone M, Yamada A, Asahi K, Hirota A, Ezawa I, Iimura T. 1999. Phosphate depletion enhances tissue-nonspecific alkaline phosphatase gene expression in a cultured mouse marrow stromal cell line ST2. Biochem Biophys Res Commun 265: 24-28.
13) Michigami T, Uchihashi T, Suzuki A, Tachikawa K, Nakajima S, Ozono K. 2005. Common mutations F310L and T1559del in the tissue-nonspecific alkaline phosphatase gene are related to distinct phenotypes in Japanese patients with hypophosphatasia. Eur J Pediatr 164: 277-282.
12) Komaru K, Ishida Y, Amaya Y, Goseki-Sone M, Orimo H, Oda K. 2005. Novel aggregate formation of a frame-shift mutant protein of tissue-nonspecific alkaline phosphatase is ascribed to three cysteine residues in the C-terminal extension. Retarded secretion and proteasomal degradation. FEBS J 272: 1704-1717.
19) Price PA. 1988. Role of vitamin-K-dependent proteins in bone metabolism. Annu Rev Nutr 8: 565-583.
22) Millán JL. 2006. Mammalian Alkaline Phosphatases. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
23) Kemi VE, Kärkkäinen MUM, Lamberg-Allardt CJE. 2006. High phosphorus intakes acutely and negatively affect Ca and bone metabolism in a dose-dependent manner in healthy young females. Br J Nutr 96: 545-552.
9) Goseki-Sone M, Orimo H, Iimura T, Takagi Y, Watanabe H, Taketa K, Sato S, Mayanagi H, Shimada T, Oida S. 1998. Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients. Hum Mutat 1: 263-267.
24) Martin A, David V, Quarles LD. 2012. Regulation and function of the FGF23/klotho endocrine pathways. Physiol Rev 92: 131-155.
25) Fardellone P, Brazier M, Kamel S, Guéris J, Graulet AM, Liénard J, Sebert JL. 1998. Biochemical effects of calcium supplementation in postmenopausal women: influence of dietary calcium intake. Am J Clin Nutr 67: 1273-1278.
21) Goseki-Sone M, Yamada A, Hamatani R, Mizoi L, Iimura T, Ezawa I. 2002. Phosphate depletion enhances bone morphogenetic protein-4 gene expression in a cultured mouse marrow stromal cell line ST2. Biochem Biophys Res Commun 299: 395-399.
11) Orimo H, Goseki-Sone M, Inoue M, Tsubakio Y, Sakiyama T, Shimada T. 2002. Importance of deletion of T at nucleotide 1559 in the tissue-nonspecific alkaline phosphatase gene in Japanese patients with hypophosphatasia. J Bone Miner Metab 20: 28-33.
3) Knoll BJ, Rothblum KN, Longley M. 1988. Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution. J Biol Chem 263: 12020-12027.
17) Gitelman HJ. 1967. An improved automated procedure for the determination of calcium in biological specimens. Anal Biochem 18: 521-531.
4) Whyte MP. 1989. Alkaline phosphatase: physiological role explored in hypophosphatasia. In: Bone and Mineral Research (Peck WA, ed), Vol. 6, p 175-218. Elesevier Science Publishers, Amsterdam.
5) Fedde KN, Blair L, Silverstein J, Coburn SP, Ryan LM, Weinstein RS, Waymire K, Narisawa S, Millán JL, MacGregor GR, Whyte MP. 1999. Alkaline phosphatase knock-out mice recapitulate the metabolic and skeletal defects of infantile hypophosphatasia. J Bone Miner Res 14: 2015-2026.
14) Ozono K, Michigami T. 2011. Hypophosphatasia now draws more attention of both clinicians and researchers: a commentary on prevalence of c.1559delT in ALPL, a common mutation resulting in the perinatal (lethal) form of hypophosphatasias in Japanese and effects of the mutation on heterozygous carriers. J Hum Genet 56: 174-176.
16) Bessey OA, Lowry OH, Brock MJ. 1946. A method for the rapid determination of alkaline phosphates with five cubic millimeter of serum. J Biol Chem 164: 321-329.
18) Drewes PA. 1972. Direct colorimetric determination of phosphorus in serum and urine. Clin Chim Acta 39: 81-88.
6) Goseki-Sone M, Sogabe N, Fukushi-Irie M, Mizoi L, Orimo H, Suzuki T, Nakamura H, Orimo H, Hosoi T. 2005. Functional analysis of the single nucleotide polymorphism (787T>C) in the tissue-nonspecific alkaline phosphatase gene associated with BMD. J Bone Miner Res 20: 773-782.
10) Goseki-Sone M, Orimo H, Iimura T, Miyazaki H, Oda K, Shibata H, Yanagishita M, Takagi Y, Watanabe H, Shimada T, Oida S. 1998. Expression of the mutant (1735T-DEL) tissue-nonspecific alkaline phosphatase gene from hypophosphatasia patients. J Bone Miner Res 13: 1827-1834.
1) Weiss MJ, Ray K, Henthorn PS, Lamb B, Kadesch T, Harris H. 1988. Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem 263: 12002-12010.
2) Henthorn PS, Raducha M, Kadesch T, Weiss MJ, Harris H. 1988. Sequence and characterization of the human intestinal alkaline phosphatase gene. J Biol Chem 263: 12011-12019.
7) Sogabe N, Oda K, Nakamura H, Orimo H, Watanabe H, Hosoi T, Goseki-Sone M. 2008. Molecular effects of the tissue-nonspecific alkaline phosphatase gene polymorphism (787T>C) associated with bone mineral density. Biomed Res 29: 213-219.
8) Orimo H, Hayashi Z, Watanabe A, Hirayama T, Shimada T. 1994. Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia. Hum Mol Genet 3: 1683-1684.
15) Watanabe A, Karasugi T, Sawai H, Naing BT, Ikegawa S, Orimo H, Shimada T. 2011. Prevalence of c.1559delT in ALPL, a common mutation resulting in the perinatal (lethal) form of hypophosphatasia in Japanese and effects of the mutation on heterozygous carriers. J Hum Genet 56: 166-168.
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References_xml – reference: 12) Komaru K, Ishida Y, Amaya Y, Goseki-Sone M, Orimo H, Oda K. 2005. Novel aggregate formation of a frame-shift mutant protein of tissue-nonspecific alkaline phosphatase is ascribed to three cysteine residues in the C-terminal extension. Retarded secretion and proteasomal degradation. FEBS J 272: 1704-1717.
– reference: 21) Goseki-Sone M, Yamada A, Hamatani R, Mizoi L, Iimura T, Ezawa I. 2002. Phosphate depletion enhances bone morphogenetic protein-4 gene expression in a cultured mouse marrow stromal cell line ST2. Biochem Biophys Res Commun 299: 395-399.
– reference: 2) Henthorn PS, Raducha M, Kadesch T, Weiss MJ, Harris H. 1988. Sequence and characterization of the human intestinal alkaline phosphatase gene. J Biol Chem 263: 12011-12019.
– reference: 8) Orimo H, Hayashi Z, Watanabe A, Hirayama T, Shimada T. 1994. Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia. Hum Mol Genet 3: 1683-1684.
– reference: 7) Sogabe N, Oda K, Nakamura H, Orimo H, Watanabe H, Hosoi T, Goseki-Sone M. 2008. Molecular effects of the tissue-nonspecific alkaline phosphatase gene polymorphism (787T>C) associated with bone mineral density. Biomed Res 29: 213-219.
– reference: 10) Goseki-Sone M, Orimo H, Iimura T, Miyazaki H, Oda K, Shibata H, Yanagishita M, Takagi Y, Watanabe H, Shimada T, Oida S. 1998. Expression of the mutant (1735T-DEL) tissue-nonspecific alkaline phosphatase gene from hypophosphatasia patients. J Bone Miner Res 13: 1827-1834.
– reference: 15) Watanabe A, Karasugi T, Sawai H, Naing BT, Ikegawa S, Orimo H, Shimada T. 2011. Prevalence of c.1559delT in ALPL, a common mutation resulting in the perinatal (lethal) form of hypophosphatasia in Japanese and effects of the mutation on heterozygous carriers. J Hum Genet 56: 166-168.
– reference: 25) Fardellone P, Brazier M, Kamel S, Guéris J, Graulet AM, Liénard J, Sebert JL. 1998. Biochemical effects of calcium supplementation in postmenopausal women: influence of dietary calcium intake. Am J Clin Nutr 67: 1273-1278.
– reference: 11) Orimo H, Goseki-Sone M, Inoue M, Tsubakio Y, Sakiyama T, Shimada T. 2002. Importance of deletion of T at nucleotide 1559 in the tissue-nonspecific alkaline phosphatase gene in Japanese patients with hypophosphatasia. J Bone Miner Metab 20: 28-33.
– reference: 13) Michigami T, Uchihashi T, Suzuki A, Tachikawa K, Nakajima S, Ozono K. 2005. Common mutations F310L and T1559del in the tissue-nonspecific alkaline phosphatase gene are related to distinct phenotypes in Japanese patients with hypophosphatasia. Eur J Pediatr 164: 277-282.
– reference: 1) Weiss MJ, Ray K, Henthorn PS, Lamb B, Kadesch T, Harris H. 1988. Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem 263: 12002-12010.
– reference: 17) Gitelman HJ. 1967. An improved automated procedure for the determination of calcium in biological specimens. Anal Biochem 18: 521-531.
– reference: 3) Knoll BJ, Rothblum KN, Longley M. 1988. Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution. J Biol Chem 263: 12020-12027.
– reference: 20) Goseki-Sone M, Yamada A, Asahi K, Hirota A, Ezawa I, Iimura T. 1999. Phosphate depletion enhances tissue-nonspecific alkaline phosphatase gene expression in a cultured mouse marrow stromal cell line ST2. Biochem Biophys Res Commun 265: 24-28.
– reference: 5) Fedde KN, Blair L, Silverstein J, Coburn SP, Ryan LM, Weinstein RS, Waymire K, Narisawa S, Millán JL, MacGregor GR, Whyte MP. 1999. Alkaline phosphatase knock-out mice recapitulate the metabolic and skeletal defects of infantile hypophosphatasia. J Bone Miner Res 14: 2015-2026.
– reference: 18) Drewes PA. 1972. Direct colorimetric determination of phosphorus in serum and urine. Clin Chim Acta 39: 81-88.
– reference: 14) Ozono K, Michigami T. 2011. Hypophosphatasia now draws more attention of both clinicians and researchers: a commentary on prevalence of c.1559delT in ALPL, a common mutation resulting in the perinatal (lethal) form of hypophosphatasias in Japanese and effects of the mutation on heterozygous carriers. J Hum Genet 56: 174-176.
– reference: 9) Goseki-Sone M, Orimo H, Iimura T, Takagi Y, Watanabe H, Taketa K, Sato S, Mayanagi H, Shimada T, Oida S. 1998. Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients. Hum Mutat 1: 263-267.
– reference: 16) Bessey OA, Lowry OH, Brock MJ. 1946. A method for the rapid determination of alkaline phosphates with five cubic millimeter of serum. J Biol Chem 164: 321-329.
– reference: 4) Whyte MP. 1989. Alkaline phosphatase: physiological role explored in hypophosphatasia. In: Bone and Mineral Research (Peck WA, ed), Vol. 6, p 175-218. Elesevier Science Publishers, Amsterdam.
– reference: 19) Price PA. 1988. Role of vitamin-K-dependent proteins in bone metabolism. Annu Rev Nutr 8: 565-583.
– reference: 23) Kemi VE, Kärkkäinen MUM, Lamberg-Allardt CJE. 2006. High phosphorus intakes acutely and negatively affect Ca and bone metabolism in a dose-dependent manner in healthy young females. Br J Nutr 96: 545-552.
– reference: 24) Martin A, David V, Quarles LD. 2012. Regulation and function of the FGF23/klotho endocrine pathways. Physiol Rev 92: 131-155.
– reference: 6) Goseki-Sone M, Sogabe N, Fukushi-Irie M, Mizoi L, Orimo H, Suzuki T, Nakamura H, Orimo H, Hosoi T. 2005. Functional analysis of the single nucleotide polymorphism (787T>C) in the tissue-nonspecific alkaline phosphatase gene associated with BMD. J Bone Miner Res 20: 773-782.
– reference: 22) Millán JL. 2006. Mammalian Alkaline Phosphatases. Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.
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  doi: 10.1359/jbmr.1999.14.12.2015
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Snippet Alkaline phosphatase (ALP) hydrolyzes a variety of monophosphate esters into phosphoric acid and alcohol at a high optimum pH (pH 8-10). Human ALPs are...
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SubjectTerms Alkaline Phosphatase - blood
Alkaline Phosphatase - genetics
Asian Continental Ancestry Group - genetics
Biological and medical sciences
bone-specific alkaline phosphatase
Calcium, Dietary - administration & dosage
Calcium, Dietary - blood
Diet
dietary nutrient intake
Energy Intake - genetics
Feeding. Feeding behavior
Female
fibroblast growth factor 23
Fibroblast Growth Factors - blood
Fibroblast Growth Factors - genetics
Fundamental and applied biological sciences. Psychology
Gene Deletion
Humans
hypophosphatasia
Hypophosphatasia - blood
Hypophosphatasia - genetics
Male
Osteocalcin - blood
Osteocalcin - genetics
Phosphorus, Dietary - administration & dosage
Phosphorus, Dietary - blood
serum phosphorus
Vertebrates: anatomy and physiology, studies on body, several organs or systems
Young Adult
Title A Study of the Association between Serum Bone-Specific Alkaline Phosphatase and Serum Phosphorus Concentration or Dietary Phosphorus Intake
URI https://www.jstage.jst.go.jp/article/jnsv/58/6/58_442/_article/-char/en
https://www.ncbi.nlm.nih.gov/pubmed/23419404
Volume 58
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