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Publié le 10 mars 2023

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1

Miura, Yoshiaki, Takeshi Ishiyama, Masanosuke Nagao, Hian In, Masao Kitaoka, Kazuhiko Ohara, Masaaki Arakawa, Hideaki Takahashi et Ryuichi Kasai. « Serum levels of bone Gla-protein ». Journal of Japanese Society for Dialysis Therapy 21, n^o 9 (1988) : 861–70. http://dx.doi.org/10.4009/jsdt1985.21.861.

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Price, Paul A. « Gla-Containing Proteins of Bone ». Connective Tissue Research 21, n^o 1-4 (janvier 1989) : 51–60. http://dx.doi.org/10.3109/03008208909049995.

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3

OBRANT, KARL J., BLANDINE MERLE, JACQUES BEJUI et PIERRE D. DELMAS. « Serum Bone-Gla Protein After Fracture ». Clinical Orthopaedics and Related Research &NA;, n^o 258 (septembre 1990) : 300???303. http://dx.doi.org/10.1097/00003086-199009000-00035.

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4

Pastoureau, P., B. Merle et P. D. Delmas. « Specific radioimmunoassay for ovine bone gla-protein (osteocalcin) ». Acta Endocrinologica 119, n^o 1 (septembre 1988) : 152–60. http://dx.doi.org/10.1530/acta.0.1190152.

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Abstract. We developed a sensitive and specific radioimmunoassay for ovine bone gla-protein (osteocalcin) using a polyclonal rabbit antibody raised against ovine bone gla-protein. Bone from lambs was extracted in 0.5 mol/l EDTA and desalted on Sephadex G-25. Bone gla-protein was purified by gel filtration chromatography over Sephadex G-100 and ion-exchange chromatography on DEAE-Sephadex A-25. The protein, subjected to monodimensional electrophoresis migrated as a single spot in SDS PAGE with the same apparent molecular weight of 12 kD as bovine bone gla-protein. The amino acid composition of purified bone gla-protein was in agreement with a previous publication. The competitive RIA uses 125I-labelled bone gla-protein as a tracer and a complex of a second antibody and polyethylene glycol to separate free and antibody-bound 125I-labelled bone gla-protein. The intra- and inter-assay variations are less than 6 and 10%, respectively. There is no reactivity of our antisera with dog sera. The cross-reactivity is only partial with calf and human sera and complete with ovine sera. We measured bone gla-protein levels in serum of 96 normal male sheep of different ages. Serum bone gla-protein rapidly and significantly (P <0.001) decreased from 535 ± 169 μg/l at birth, to 240 ± 43 μg/l at 45 days, 152 ± 44 μg/l at 90 days, and 5.9 ± 0.7 μg/l at 7 years of age. In addition, bone gla-protein levels at birth were higher in normal birth weight than in hypotrophic lambs with low birth weight (535 ± 169 vs 271 ± 156 μg/l, P< 0.001). Furthermore, lambs raised outside in free conditions tended to have higher serum bone gla-protein levels than lambs raised under shelter (194 ± 53 vs 137 ± 34 μg/l), suggesting a role of breeding factors such as diet or relative immobilization on bone gla-protein levels. These results emphasize the interest of a RIA for the bone-specific protein bone gla-protein as a potential tool for experimental studies on skeletal growth and bone remodelling in a large animal.

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5

Johnson, Teresa L., Alan Y. Sakaguchi, Peter A. Lalley et Robin J. Leach. « Chromosomal assignment in mouse of matrix Gla protein and bone Gla protein genes ». Genomics 11, n^o 3 (novembre 1991) : 770–72. http://dx.doi.org/10.1016/0888-7543(91)90089-w.

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6

Kaipatur, N. R., M. Murshed et M. D. McKee. « Matrix Gla Protein Inhibition of Tooth Mineralization ». Journal of Dental Research 87, n^o 9 (septembre 2008) : 839–44. http://dx.doi.org/10.1177/154405910808700907.

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Extracellular matrix (ECM) mineralization is regulated by mineral ion availability, proteins, and other molecular determinants. To investigate protein regulation of mineralization in tooth dentin and cementum, and in alveolar bone, we expressed matrix Gla protein (MGP) ectopically in bones and teeth in mice, using an osteoblast/odontoblast-specific 2.3-kb Col1a1 promoter. Mandibles were analyzed by radiography, micro-computed tomography, light microscopy, histomorphometry, and transmission electron microscopy. While bone and tooth ECMs were established in the Col1a1-Mgp mice, extensive hypomineralization was observed, with values of unmineralized ECM from four- to eight-fold higher in dentin and alveolar bone when compared with that in wild-type tissues. Mineralization was virtually absent in tooth root dentin and cellular cementum, while crown dentin showed “breakthrough” areas of mineralization. Acellular cementum was lacking in Col1a1-Mgp teeth, and unmineralized osteodentin formed within the pulp. These results strengthen the view that bone and tooth mineralization is critically regulated by mineralization inhibitors.

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7

Thomsen, K., E. F. Eriksen, J. C. R. Jørgensen, P. Charles et L. Mosekilde. « Seasonal variation of serum bone GLA protein ». Scandinavian Journal of Clinical and Laboratory Investigation 49, n^o 7 (1 novembre 1989) : 605–11. http://dx.doi.org/10.3109/00365518909091535.

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Thomsen, K., E. F. Eriksen, J. C. R. Jørgensen, P. Charles et L. Mosekilde. « Seasonal variation of serum bone GLA protein ». Scandinavian Journal of Clinical and Laboratory Investigation 49, n^o 7 (janvier 1989) : 605–11. http://dx.doi.org/10.1080/00365518909091535.

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9

Bataille, Régis, Pierre Delmas et Jacques Sany. « Serum bone gla-protein in multiple myeloma ». Cancer 59, n^o 2 (15 janvier 1987) : 329–34. http://dx.doi.org/10.1002/1097-0142(19870115)59:2<329 ::aid-cncr2820590227>3.0.co;2-s.

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10

Delmas, P. D., C. Christiansen, K. G. Mann et P. A. Price. « Bone gla protein (osteocalcin) assay standardization report ». Journal of Bone and Mineral Research 5, n^o 1 (janvier 1990) : 5–11. http://dx.doi.org/10.1002/jbmr.5650050104.

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11

CHARHON, SAM A., PIERRE D. DELMAS, LUC MALAVAL, PASCALE M. CHAVASSIEUX, MONIQUE ARLOT, MARIE-CLAIRE CHAPUY et PIERRE J. MEUNIER. « Serum Bone Gla-Protein in Renal Osteodystrophy:Comparison with Bone Histomorphometry* ». Journal of Clinical Endocrinology & ; Metabolism 63, n^o 4 (octobre 1986) : 892–97. http://dx.doi.org/10.1210/jcem-63-4-892.

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12

Lwasaki, Renpei, Takao Yamamuro, Yoshihiko Kotoura, Hideo Okumura, Ryuichi Kasai et Yasuaki Nakashima. « Immunohistochemical study of bone GLA protein in primary bone tumors ». Cancer 70, n^o 3 (1 août 1992) : 619–24. http://dx.doi.org/10.1002/1097-0142(19920801)70:3<619 ::aid-cncr2820700313>3.0.co;2-5.

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13

Gorbunova, Victoria N., Natalia V. Buchinskaia, Grigorii A. Janus et Mikhail M. Kostik. « Lysosomal storage diseases. Sphingolipidoses — Fabry, Gaucher and Farber diseases ». Pediatrician (St. Petersburg) 13, n^o 2 (9 juillet 2022) : 61–88. http://dx.doi.org/10.17816/ped13261-88.

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Sphingolipidoses are genetically heterogeneous group of rare monogenic metabolic diseasesб caused by inherreted deficiency of enzymes involved in the degradation of sphingolipids. Sphingolipids are catabolized in lysosomes, where glycohydrolases degrade them by separation of terminal sugars to core ceramide. All sphingolipidoses are characterized by abnormal deposition of a large amount of sphingolipids and other unsplit products of lipid metabolism, mainly in parenchymal organs, bone marrow and brain. Among sphingolipidoses, such groups of diseases as glycosphingolipidoses, gangliosidoses and leukodystrophies are distinguished. This review presents the epidemiology, clinical, biochemical and molecular characteristics of the three main types of glycosphingolipidoses Fabry disease, Gaucher disease and Farber disease, caused by the mutations in the genes of -galactosidase A (GLA), glucocerebrosidase (GBA) and acid ceramidase (ASAH1), respectively. Currently, there is an increased interest in glycosphingolipidoses due to the identification of the spectrum and frequencies of mutations in the GLA, GBA and ASAH1 genes in various populations, including Russia, and the practical availability of individual molecular diagnostic methods. A description of the existing experimental models, their role in the study of the biochemical basis of the pathogenesis of these severe hereditary diseases and the development of various therapeutic approaches are given. We discuss, firstly, the possibility of early diagnosis of Fabry disease, Gaucher and Farber based on neonatal screening and examination of high risk groups of patients in order to improve the effectiveness of their prevention and treatment, as well as (secondly) the advantages and disadvantages of the main approaches to the treatment of these serious diseases, such as bone marrow and hematopoietic stem cell transplantation, enzyme replacement therapy, substrate reduction therapy, gene therapy and genome editing.

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14

Rapado, A., C. De La Piedra et R. Torres. « BGP (osteocalcin, bone-Gla-protein) in involutional osteoporosis ». Clinical Rheumatology 8, S2 (juin 1989) : 30–34. http://dx.doi.org/10.1007/bf02207230.

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15

Zséli, János, Péter Bösze, Péter Lakatos, Péter Vargha, Gábor Tarján, Éva Kollin, Csaba Horváth, János László et István Holló. « Serum bone GLA protein in streak gonad syndrome ». Calcified Tissue International 48, n^o 6 (juin 1991) : 387–91. http://dx.doi.org/10.1007/bf02556451.

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Delmas, P. D., P. A. Price et K. G. Mann. « Validation of the bone gla protein (osteocalcin) assay ». Journal of Bone and Mineral Research 5, n^o 1 (janvier 1990) : 3–4. http://dx.doi.org/10.1002/jbmr.5650050103.

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GARREL, DOMINIQUE R., PIERRE D. DELMAS, LUC MALAVAL et JACQUES TOURNIAIRE. « Serum Bone Gla Protein : A Marker of BOne Turnover in Hyperthyroidism* ». Journal of Clinical Endocrinology & ; Metabolism 62, n^o 5 (mai 1986) : 1052–55. http://dx.doi.org/10.1210/jcem-62-5-1052.

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18

Delmas, P. D., L. Malaval, M. E. Arlot et P. J. Meunier. « Serum bone Gla-protein compared to bone histomorphometry in endocrine diseases ». Bone 6, n^o 5 (1985) : 339–41. http://dx.doi.org/10.1016/8756-3282(85)90326-6.

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19

MAGARO, M., L. ALTOMONTE, LUISA MIRONE, A. ZOLI et G. CORVINO. « BONE GLA PROTEIN (BGP) LEVELS AND BONE TURNOVER IN RHEUMATOID ARTHRITIS ». Rheumatology 28, n^o 3 (1989) : 207–11. http://dx.doi.org/10.1093/rheumatology/28.3.207.

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20

Obrant, Karl J., Urban Bengnér et Pierre D. Delmas. « Bone gla : Protein in blood derived directly from human bone tissue ». Calcified Tissue International 44, n^o 4 (juillet 1989) : 296–97. http://dx.doi.org/10.1007/bf02553764.

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Burky, Richard R., Donna L. Kirner, R. E. Taylor, P. E. Hare et John R. Southon. « 14C Dating of Bone Using γ-Carboxyglutamic Acid and α-Carboxyglycine (Aminomalonate) ». Radiocarbon 40, n^o 1 (1997) : 11–20. http://dx.doi.org/10.1017/s0033822200017823.

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Radiocarbon determinations have been obtained on γ-carboxyglutamic acid [Gla] and α-carboxyglycine (aminomalonate) [Am] as well as acid- and base-hydrolyzed total amino acids isolated from a series of fossil bones. As far as we are aware, Am has not been reported previously in fossil bone and neither Gla nor Am 14C values have been measured previously. Interest in Gla, an amino acid found in the non-collagen proteins osteocalcin and matrix Gla-protein (MGP), proceeds from the suggestion that it may be preferentially retained and more resistant to diagenetic contamination affecting 14C values in bones exhibiting low and trace amounts of collagen. Our data do not support these suggestions. The suite of bones examined showed a general tendency for total amino acid and Gla concentrations to decrease in concert. Even for bones retaining significant amounts of collagen, Gla (and Am extracts) can yield 14C values discordant with their expected age and with 14C values obtained on total amino-acid fractions isolated from the same bone sample.

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22

YONEDA, MASAHIRO, KENSUKE TAKATSUKI, YUTAKA OISO, TSUNENORI TAKANO, MASAEI KUROKAWA, AKIRA OTA, AKIO TOMITA, TOSHIRO OHNO, KEIKO OKANO et TAMOTSU KANAZAWA. « Clinical significance of serum bone Gla protein and urinary .GAMMA.-Gla as biochemical markers in primary hyperparathyroidism. » Endocrinologia Japonica 33, n^o 1 (1986) : 89–94. http://dx.doi.org/10.1507/endocrj1954.33.89.

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YONEDA, MASAHIRO, KENSUKE TAKATSUKI, KAZUYUKI YAMAUCHI, YUTAKA OISO, MASAEI KUROKAWA, AKITOSHI KAWAKUBO, KAZUHIRO IZUCHI et al. « Influence of Thyroid Function on Serum Bone Gla Protein. » Endocrinologia Japonica 35, n^o 1 (1988) : 121–29. http://dx.doi.org/10.1507/endocrj1954.35.121.

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YONEDA, MASAHIRO, KENSUKE TAKATSUKI, KAZUYUKI YAMAUCHI, YUTAKA OISO, MASAEI KUROKAWA, AKITOSHI KAWAKUBO, YUJI TORIMOTO, HIROOMI FUNAHASHI et AKIO TOMITA. « Effect of Parathyroid Function on Serum Bone Gla Protein. » Endocrinologia Japonica 35, n^o 1 (1988) : 39–45. http://dx.doi.org/10.1507/endocrj1954.35.39.

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25

Delmas, Pierre D., Pierre Chatelain, Luc Malaval et Graziela Bonne. « Serum bone GLA-protein in growth hormone deficient children ». Journal of Bone and Mineral Research 1, n^o 4 (3 décembre 2009) : 333–38. http://dx.doi.org/10.1002/jbmr.5650010406.

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26

Razny, Urszula, Joanna Goralska, Anna Zdzienicka, Anna Gruca, Barbara Zapala, Agnieszka Micek, Aldona Dembinska-Kiec, Bogdan Solnica et Malgorzata Malczewska-Malec. « High Fat Mixed Meal Tolerance Test Leads to Suppression of Osteocalcin Decrease in Obese Insulin Resistant Subjects Compared to Healthy Adults ». Nutrients 10, n^o 11 (1 novembre 2018) : 1611. http://dx.doi.org/10.3390/nu10111611.

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Nutrients influence bone turnover. Carboxylated osteocalcin (Gla-OC) participates in bone formation whereas its undercarboxylated form (Glu-OC) acts as a hormone in glucose metabolism. The aim of the study was to determine the responses of Gla-OC, Glu-OC, and total-OC (calculated as the sum of Gla-OC and Glu-OC) to a high fat mixed meal tolerance test (HFMTT) in non-obese (body mass index (BMI) < 30 kg/m2, n = 24) and obese subjects (30 < BMI < 40 kg/m2, n = 70) (both sexes, aged 25–65 years). Serum Gla-OC and Glu-OC were measured at baseline as well as at 2 and 6 h during a HFMTT by enzyme-linked immunosorbent assay (ELISA). Baseline Gla-OC, Glu-OC, and total-OC levels were lower in obese individuals compared to non-obese participants (p = 0.037, p = 0.016 and p = 0.005, respectively). The decrease in Gla-OC and total-OC, but not in Glu-OC, concentrations during the HFMTT was suppressed in obese, but not in non-obese controls (p < 0.05, p < 0.01, p = 0.08, respectively). Subjects with the highest homeostatic model assessment for insulin resistance (HOMA-IR) index values had a less pronounced decrease in total-OC compared to patients with values of HOMA-IR index in the 1st quartile (p < 0.05). Net incremental area under Gla-OC inversely correlated with adiponectin (rho = −0.35, p = 0.001). Increase in insulin sensitivity and adiponectin level in obese subjects could beneficially influence postprandial bone turnover expressed by osteocalcin concentration.

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Coutu, Daniel L., Jian Wui Wu, Georges-Etienne Rivard, Mark D. Blostein et Jacques Galipeau. « Periostin Is a Previously Uncharacterised Vitamin K Dependent γ-Carboxyglutamic Acid (Gla) Containing Protein Expressed by Marrow-Derived Mesenchymal Stromal Cells. » Blood 110, n^o 11 (16 novembre 2007) : 1927. http://dx.doi.org/10.1182/blood.v110.11.1927.1927.

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Abstract The modification of glutamic acid residues to g-carboxyglutamic acid (Gla) is a post-translational modification catalyzed by the vitamin K-dependent γ-glutamylcarboxylase enzyme. Despite ubiquitous expression of the γ-carboxylation machinery in mammalian tissues, only 12 Gla-containing proteins have so far been identified in humans. Because bone tissue is the second most abundant source of Gla-proteins after the liver, we sought to identify Gla proteins secreted by bone-marrow derived mesenchymal stromal cells (MSCs), a precursor to all non-hematopoietic cells in bones. We used a proteomics approach to screen the secretome of MSCs with a combination of 2D gel electrophoresis and tandem mass spectrometry. The most abundant Gla-protein secreted by MSCs was identified as periostin, a previously unrecognized γ-carboxylated protein. In silico aminoacid sequence analysis of periostin demonstrated the presence of four consensus γ-carboxylase recognition sites embedded within fasciclin-like protein domains. The carboxylation of periostin was confirmed by immunoprecipitation using anti-Gla antibodies and could be inhibited by warfarin in MSCs. In conclusion, periostin is a novel vitamin K-dependent γ-carboxylated protein distinguished from other Gla-proteins by the presence of multiple γ-carboxylase recognition sites and MSCs are an abundant source of periostin including its γ-carboxylated variant.

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Marazuela, M., B. Astigarraga, M. J. Tabuenca, J. Estrada, F. Mar�n et T. Lucas. « Serum bone Gla protein as a marker of bone turnover in acromegaly ». Calcified Tissue International 52, n^o 6 (juin 1993) : 419–21. http://dx.doi.org/10.1007/bf00571329.

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Johansen, Julia S., J. E. Mølholm Hansen et Claus Christiansen. « A radioimmunoassay for bone Gla protein (BGP) in human plasma ». Acta Endocrinologica 114, n^o 3 (mars 1987) : 410–16. http://dx.doi.org/10.1530/acta.0.1140410.

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Abstract. To study the value of bone Gla protein (BGP) as a biochemical marker of normal bone physiology and metabolic bone disorders, we have developed a radioimmunoassay (RIA) for the detection of BGP in human plasma. Antibodies were generated in rabbits immunized with purified calf BGP conjugated to thyroglobulin. Human plasma BGP reacted identically with the calf BGP standard, thus demonstrating the suitability of the assay to measure plasma BGP levels in man. The RIA is sensitive, accurate, and technically simple. Plasma BGP levels were determined in normal subjects (N = 35) and in patients with hypothyroidism (N = 10), hyperthyroidism (N = 22) and chronic renal failure (N = 35). The mean (± 1 sem) concentration of plasma BGP in normal subjects was 1.27 ± 0.07 nmol/l. Plasma BGP was significantly increased in patients with hyperthyroidism, 4.04 ± 0.78 nmol/l (P < 0.001) and chronic renal failure, 10.17 ± 2.47 nmol/l (P < 0.001). Low concentrations were found in patients with hypothyroidism, 0.74 ± 0.11 nmol/l (P <0.01). Our studies indicate that plasma BGP provides a useful technique in the diagnosis of patients with bone disease.

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30

Stock, Michael, et Georg Schett. « Vitamin K-Dependent Proteins in Skeletal Development and Disease ». International Journal of Molecular Sciences 22, n^o 17 (28 août 2021) : 9328. http://dx.doi.org/10.3390/ijms22179328.

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Vitamin K and Vitamin K-dependent proteins (VKDPs) are best known for their pivotal role in blood coagulation. Of the 14 VKPDs identified in humans to date, 6 play also important roles in skeletal biology and disease. Thus, osteocalcin, also termed bone Gla-protein, is the most abundant non-collagenous protein in bone. Matrix Gla protein and Ucma/GRP on the other hand are highly abundant in cartilage. Furthermore, periostin, protein S, and growth arrest specific 6 protein (GAS 6) are expressed in skeletal tissues. The roles for these VKDPs are diverse but include the control of calcification and turnover of bone and cartilage. Vitamin K plays an important role in osteoporosis and serum osteocalcin levels are recognized as a promising marker for osteoporosis. On the other hand, matrix Gla protein and Ucma/GRP are associated with osteoarthritis. This review focuses on the roles of these three VKDPs, osteocalcin, matrix Gla protein and Ucma/GRP, in skeletal development and disease but will also summarize the roles the other skeletal VKDPs (periostin, protein S and GAS6) in skeletal biology.

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Masoud, Mirzaie, Josefina Kusnirova, Johann Philipp Addicks et Sheila Fatehpur. « Matrix-GLA-Protein and Vascular Calcification : Can Diet Influence the Consequences of Matrix GLA Protein Inactivation ? A Review ». International Journal of Innovative Research in Medical Science 6, n^o 10 (5 octobre 2021) : 678–86. http://dx.doi.org/10.23958/ijirms/vol06-i10/1235.

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In vascular calcification, as a physiological process, intimal arterial calcification (IAC) associated with increased cardiovascular risk is distinguished from medial arterial calcification (MAC) localized mainly in the lamina elatica interna, which are not only based on different pathophysiological mechanisms. They also lead to different cardiovascular diseases. While intimal arterial calcification involves inflammation and lipid accumulation, a calcification process similar to desmal ossification plays the main role in medial arterial calcification. In this context, the phenotype change of smooth muscle cells from muscular type to synthesizing form in the tunica media is considered to be of great importance, which puts the matrix GLA protein, mainly involved in bone metabolism, in the center of interest. The present review work elucidates the molecular biological basis of interaction of matrix GLA protein subunits in the pathogenesis of vascular calcifications and the influence of diet on the consequences of underactivation of matrix GLA protein.

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Delmas, Pierre D., Pierre J. Meunier, E. Faysse et E. C. Saubier. « Bone histomorphometry and serum bone gla-protein in the diagnosis of primary hyperparathyroidism ». World Journal of Surgery 10, n^o 4 (août 1986) : 572–77. http://dx.doi.org/10.1007/bf01655528.

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Ziemińska, Marta, Dariusz Pawlak, Beata Sieklucka, Katarzyna Chilkiewicz et Krystyna Pawlak. « Vitamin K-Dependent Carboxylation of Osteocalcin in Bone—Ally or Adversary of Bone Mineral Status in Rats with Experimental Chronic Kidney Disease ? » Nutrients 14, n^o 19 (1 octobre 2022) : 4082. http://dx.doi.org/10.3390/nu14194082.

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Chronic kidney disease (CKD) commonly occurs with vitamin K (VK) deficiency and impaired bone mineralization. However, there are no data explaining the metabolism of endogenous VK and its role in bone mineralization in CKD. In this study, we measured serum levels of phylloquinone (VK1), menaquinone 4 and 7 (MK4, MK7), and VK-dependent proteins: osteocalcin, undercarboxylated osteocalcin (Glu-OC), and undercarboxylated matrix Gla protein (ucMGP). The carboxylated osteocalcin (Gla-OC), Glu-OC, and the expression of genes involved in VK cycle were determined in bone. The obtained results were juxtaposed with the bone mineral status of rats with CKD. The obtained results suggest that the reduced VK1 level observed in CKD rats may be caused by the accelerated conversion of VK1 to the form of menaquinones. The bone tissue possesses all enzymes, enabling the conversion of VK1 to menaquinones and VK recycling. However, in the course of CKD with hyperparathyroidism, the intensified osteoblastogenesis causes the generation of immature osteoblasts with impaired mineralization. The particular clinical significance seems to have a finding that serum osteocalcin and Glu-OC, commonly used biomarkers of VK deficiency, could be inappropriate in CKD conditions, whereas Gla-OC synthesized in bone appears to have an adverse impact on bone mineral status in this model.

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Gendreau, M. A., S. Krishnaswamy et K. G. Mann. « The Interaction of Bone Gla Protein (Osteocalcin) with Phospholipid Vesicles ». Journal of Biological Chemistry 264, n^o 12 (avril 1989) : 6972–78. http://dx.doi.org/10.1016/s0021-9258(18)83526-8.

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Eqsmose, C., E. Fink Eriksen, S. Krause et O. R. Madsen. « Bone GLA protein in human fetal tissue. An immunohistochemical study ». Bone 16, n^o 3 (mars 1995) : 399. http://dx.doi.org/10.1016/8756-3282(95)90448-4.

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36

Fiore, C. E., G. Di Stefano, M. Romeo, L. S. Malatino, D. R. Grimaldi et R. Foti. « Calcium-induced serum bone Gla protein variations in preterm newborns ». Journal of Endocrinological Investigation 10, n^o 5 (octobre 1987) : 443–46. http://dx.doi.org/10.1007/bf03348167.

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Engelke, Jean A., John E. Hale, J. W. Suttie et Paul A. Price. « Vitamin K-dependent car☐ylase : utilization of decar☐ylated bone Gla protein and matrix Gla protein as substrates ». Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1078, n^o 1 (mai 1991) : 31–34. http://dx.doi.org/10.1016/0167-4838(91)90088-h.

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JOWELL, PAUL S., SOL EPSTEIN, MICHAEL D. FALLON, TIMOTHY A. REINHARDT et FIRHAAD ISMAIL. « 1,25-Dihydroxyvitamin D3Modulates Glucocorticoid-Induced Alteration in Serum Bone Gla Protein and Bone Histomorphometry ». Endocrinology 120, n^o 2 (février 1987) : 531–36. http://dx.doi.org/10.1210/endo-120-2-531.

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Bügel, Susanne. « Vitamin K and bone health ». Proceedings of the Nutrition Society 62, n^o 4 (novembre 2003) : 839–43. http://dx.doi.org/10.1079/pns2003305.

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Vitamin K, originally recognised as a factor required for normal blood coagulation, is now receiving more attention in relation to its role in bone metabolism. Vitamin K is a coenzyme for glutamate carboxylase, which mediates the conversion of glutamate to γ-carboxyglutamate (Gla). Gla residues attract Ca2+ and incorporate these ions into the hydroxyapatite crystals. There are at least three Gla proteins associated with bone tissue, of which osteocalcin is the most abundant and best known. Osteocalcin is the major non-collagenous protein incorporated in bone matrix during bone formation. However, approximately 30% of the newly-produced osteocalcin stays in the circulation where it may be used as an indicator of bone formation. Vitamin K deficiency results in an increase in undercarboxylated osteocalcin, a protein with low biological activity. Several studies have demonstrated that low dietary vitamin K intake is associated with low bone mineral density or increased fractures. Additionally, vitamin K supplementation has been shown to reduce undercarboxylated osteocalcin and improve the bone turnover profile. Some studies have indicated that high levels of undercarboxylated osteocalcin (as a result of low vitamin K intake?) are associated with low bone mineral density and increased hip fracture. The current dietary recommendation for vitamin K is 1 μ/kg body weight per d, based on saturation of the coagulation system. The daily dietary vitamin K intake is estimated to be in the range 124–375 μg/d in a European population. Thus, a deficiency based on the hepatic coagulation system would be unusual, but recent data suggest that the requirement in relation to bone health might be higher.

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Faber, J., H. Perrild et J. Johansen. « Serum Bone Gla Protein (BGP) During Treatment of Hyperthyroidism and Hypothyroidism ». Hormone and Metabolic Research 23, n^o 03 (mars 1991) : 135–38. http://dx.doi.org/10.1055/s-2007-1003633.

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Di Virgilio, Roberto, Manuela De Lazzari, Giorgio Da Rin, Pietro Legovini, Giancarlo Foscolo, Ignazio Roiter et Nicola Conte. « Serum Bone Gla-Protein in Hypercalcemia of Primary Hyperparathyroidism and Malignancy ». Tumori Journal 76, n^o 1 (février 1990) : 32–34. http://dx.doi.org/10.1177/030089169007600108.

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Egsmose, Charlotte, Henrik Daugaard et Birger Lund. « Determination of bone Gla protein (osteocalcin) by enzyme-linked immunosorbent assay ». Clinica Chimica Acta 184, n^o 3 (octobre 1989) : 279–87. http://dx.doi.org/10.1016/0009-8981(89)90061-2.

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Zebboudj, Amina F., Minori Imura et Kristina Boström. « Matrix GLA Protein, a Regulatory Protein for Bone Morphogenetic Protein-2 ». Journal of Biological Chemistry 277, n^o 6 (6 décembre 2001) : 4388–94. http://dx.doi.org/10.1074/jbc.m109683200.

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GEVERS, G., P. DEVOS, M. DE ROO et J. DEQUEKER. « INCREASED LEVELS OF OSTEOCALCIN (SERUM BONE GLA-PROTEIN) IN RHEUMATOID ARTHRITIS ». Rheumatology 25, n^o 3 (1986) : 260–62. http://dx.doi.org/10.1093/rheumatology/25.3.260.

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Hauschka, P. V., J. B. Lian, D. E. Cole et C. M. Gundberg. « Osteocalcin and matrix Gla protein : vitamin K-dependent proteins in bone ». Physiological Reviews 69, n^o 3 (1 juillet 1989) : 990–1047. http://dx.doi.org/10.1152/physrev.1989.69.3.990.

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Pankratova, Yu В., E. A. Pigarova et L. K. Dzeranova. « Vitamin K-dependent proteins : osteocalcin, matrix Gla-protein and extra osseous effects ». Obesity and metabolism 10, n^o 2 (15 juin 2013) : 11–18. http://dx.doi.org/10.14341/2071-8713-4818.

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Vitamin K - is a fat-soluble vitamin which plays an important role in the metabolism of bone and connective tissue, maintenance blood clotting properties. Vitamin K is involved in carboxylation of glutamic acid residues in the polypeptide chains of 14 human proteins, providing them with the necessary functional properties. Lack of vitamin K-dependent carboxylation of these proteins leads to changes in their biological activity. In this literature review we cover the mechanisms of vitamin K-dependent carboxylation and none bone actions of osteocalcin and matrix Gla-protein with different degrees of carboxylation.

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Delmas, P. D., B. Demiaux, L. Malaval, M. C. Chapuy et P. J. Meunier. « Serum bone GLA-protein is not a sensitive marker of bone turnover in Paget's disease of bone ». Calcified Tissue International 38, n^o 1 (janvier 1986) : 60–61. http://dx.doi.org/10.1007/bf02556596.

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UMEDA, MISAKO. « Evaluation of Serum Bone Gla Protein(BGP) and Bone Stiffness Measured by Ultra Sound Method. » Japanese journal of MHTS 22, n^o 1 (1995) : 31–35. http://dx.doi.org/10.7143/jhep1985.22.31.

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Nakatsuka, Kiyoshi, Takami Miki, Shigeichi Shoji, Yoshiki Nishizawa et Hirotoshi Morii. « Serum intact molecule of bone Gla-protein in patients with abnormal bone and calcium metabolism ». Journal of Bone and Mineral Metabolism 10, n^o 2 (septembre 1992) : 18–27. http://dx.doi.org/10.1007/bf02378979.

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Merle, B., et P. D. Delmas. « Normal car☐ylation of circulating osteocalcin (bone Gla-protein) in Paget's disease of bone ». Bone and Mineral 11, n^o 2 (novembre 1990) : 237–45. http://dx.doi.org/10.1016/0169-6009(90)90062-k.

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