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Journal articles on the topic 'Γ-glutamyl carboxylase'

Author: Grafiati

Published: 28 May 2022

Last updated: 31 July 2025

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1

Zhu, Aihua, Hongmin Sun, Richard M. Raymond та ін. "Fatal hemorrhage in mice lacking γ-glutamyl carboxylase". Blood 109, № 12 (2007): 5270–75. http://dx.doi.org/10.1182/blood-2006-12-064188.

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Abstract The carboxylation of glutamic acid residues to γ-carboxyglutamic acid (Gla) by the vitamin K–dependent γ-glutamyl carboxylase (γ-carboxylase) is an essential posttranslational modification required for the biological activity of a number of proteins, including proteins involved in blood coagulation and its regulation. Heterozygous mice carrying a null mutation at the γ-carboxylase (Ggcx) gene exhibit normal development and survival with no evidence of hemorrhage and normal functional activity of the vitamin K–dependent clotting factors IX, X, and prothrombin. Analysis of a Ggcx+/− int

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2

Li, Tao, Chao-Tsung Yang, Dayun Jin та Darrel W. Stafford. "Identification of aDrosophilaVitamin K-dependent γ-Glutamyl Carboxylase". Journal of Biological Chemistry 275, № 24 (2000): 18291–96. http://dx.doi.org/10.1074/jbc.m001790200.

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3

Brenner, Benjamin, Beatriz Sánchez-Vega, Sheue-Mei Wu, Naomi Lanir, Darrel W. Stafford та Jesus Solera. "A Missense Mutation in γ-Glutamyl Carboxylase Gene Causes Combined Deficiency of All Vitamin K-Dependent Blood Coagulation Factors". Blood 92, № 12 (1998): 4554–59. http://dx.doi.org/10.1182/blood.v92.12.4554.

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Abstract To identify potential mutations in the γ-glutamyl carboxylase gene, the sequence of all exons and intron/exon borders was determined in 4 patients from a consanguineous kindred with combined deficiency of all vitamin K-dependent procoagulants and anticoagulants and results were compared with normal genomic sequence. All 4 patients were homozygous for a point mutation in exon 9 that resulted in the conversion of an arginine codon (CTG) to leucine codon (CGG) at residue 394. Screening of this mutation based on introduction of Alu I site in amplified fragment from normal allele but not f

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4

Brenner, Benjamin, Beatriz Sánchez-Vega, Sheue-Mei Wu, Naomi Lanir, Darrel W. Stafford та Jesus Solera. "A Missense Mutation in γ-Glutamyl Carboxylase Gene Causes Combined Deficiency of All Vitamin K-Dependent Blood Coagulation Factors". Blood 92, № 12 (1998): 4554–59. http://dx.doi.org/10.1182/blood.v92.12.4554.424k42_4554_4559.

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To identify potential mutations in the γ-glutamyl carboxylase gene, the sequence of all exons and intron/exon borders was determined in 4 patients from a consanguineous kindred with combined deficiency of all vitamin K-dependent procoagulants and anticoagulants and results were compared with normal genomic sequence. All 4 patients were homozygous for a point mutation in exon 9 that resulted in the conversion of an arginine codon (CTG) to leucine codon (CGG) at residue 394. Screening of this mutation based on introduction of Alu I site in amplified fragment from normal allele but not from the m

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5

Spronk, Henri M. H., Roula A. Farah, George R. Buchanan, Cees Vermeer та Berry A. M. Soute. "Novel mutation in the γ-glutamyl carboxylase gene resulting in congenital combined deficiency of all vitamin K–dependent blood coagulation factors". Blood 96, № 10 (2000): 3650–52. http://dx.doi.org/10.1182/blood.v96.10.3650.

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Abstract A mutation in the γ-glutamyl carboxylase gene leading to a combined congenital deficiency of all vitamin K-dependent coagulation factors was identified in a Lebanese boy. He is the first offspring of consanguineous parents and was homozygous for a unique point mutation in exon 11, resulting in the conversion of a tryptophan codon (TGG) to a serine codon (TCG) at amino acid residue 501. Oral vitamin K1 administration resulted in resolution of the clinical symptoms. Screening of several family members on this mutation with an RFLP technique revealed 10 asymptomatic members who were hete

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6

Spronk, Henri M. H., Roula A. Farah, George R. Buchanan, Cees Vermeer та Berry A. M. Soute. "Novel mutation in the γ-glutamyl carboxylase gene resulting in congenital combined deficiency of all vitamin K–dependent blood coagulation factors". Blood 96, № 10 (2000): 3650–52. http://dx.doi.org/10.1182/blood.v96.10.3650.h8003650_3650_3652.

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A mutation in the γ-glutamyl carboxylase gene leading to a combined congenital deficiency of all vitamin K-dependent coagulation factors was identified in a Lebanese boy. He is the first offspring of consanguineous parents and was homozygous for a unique point mutation in exon 11, resulting in the conversion of a tryptophan codon (TGG) to a serine codon (TCG) at amino acid residue 501. Oral vitamin K1 administration resulted in resolution of the clinical symptoms. Screening of several family members on this mutation with an RFLP technique revealed 10 asymptomatic members who were heterozygous

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7

Tie, Jianke, Sheue-Mei Wu, Dayun Jin, Christopher V. Nicchitta та Darrel W. Stafford. "A topological study of the human γ-glutamyl carboxylase". Blood 96, № 3 (2000): 973–78. http://dx.doi.org/10.1182/blood.v96.3.973.

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Abstract γ-Glutamyl carboxylase (GC), a polytopic membrane protein found in the endoplasmic reticulum (ER), catalyzes vitamin K–dependent posttranslational modification of glutamate to γ-carboxyl glutamate. In an attempt to delineate the structure of this important enzyme, in vitro translation and in vivo mapping were used to study its membrane topology. Using terminus-tagged full-length carboxylase, expressed in 293 cells, it was demonstrated that the amino-terminus of the GC is on the cytoplasmic side of the ER, while the carboxyl-terminus is on the lumenal side. In addition, a series of fus

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8

Tie, Jianke, Sheue-Mei Wu, Dayun Jin, Christopher V. Nicchitta та Darrel W. Stafford. "A topological study of the human γ-glutamyl carboxylase". Blood 96, № 3 (2000): 973–78. http://dx.doi.org/10.1182/blood.v96.3.973.015k55_973_978.

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γ-Glutamyl carboxylase (GC), a polytopic membrane protein found in the endoplasmic reticulum (ER), catalyzes vitamin K–dependent posttranslational modification of glutamate to γ-carboxyl glutamate. In an attempt to delineate the structure of this important enzyme, in vitro translation and in vivo mapping were used to study its membrane topology. Using terminus-tagged full-length carboxylase, expressed in 293 cells, it was demonstrated that the amino-terminus of the GC is on the cytoplasmic side of the ER, while the carboxyl-terminus is on the lumenal side. In addition, a series of fusions were

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9

Rost, S., C. R. Mueller, J. Oldenburg та K. Siegel. "Recombinant expression of wildtype and mutated γ-glutamyl carboxylase". Hämostaseologie 28, S 01 (2008): S104—S105. http://dx.doi.org/10.1055/s-0037-1621631.

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10

Johnson, J. S., B. A. Soute, C. S. Olver та D. C. Baker. "Defective γ-Glutamyl Carboxylase Activity and Bleeding in Rambouillet Sheep". Veterinary Pathology 43, № 5 (2006): 726–32. http://dx.doi.org/10.1354/vp.43-5-726.

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11

Wu, Sheue-Mei, Vasantha P. Mutucumarana, Scott Geromanos та Darrel W. Stafford. "The Propeptide Binding Site of the Bovine γ-Glutamyl Carboxylase". Journal of Biological Chemistry 272, № 18 (1997): 11718–22. http://dx.doi.org/10.1074/jbc.272.18.11718.

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12

González-Conejero, Rocío, Javier Corral, Vanessa Roldán та Vicente Vicente. "γ-glutamyl carboxylase R325Q polymorphism on the response of acenocoumarol". Thrombosis Research 122, № 3 (2008): 429–31. http://dx.doi.org/10.1016/j.thromres.2007.12.007.

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13

Shiba, Sachiko, Kazuhiro Ikeda, Kotaro Azuma та ін. "γ-Glutamyl carboxylase in osteoblasts regulates glucose metabolism in mice". Biochemical and Biophysical Research Communications 453, № 3 (2014): 350–55. http://dx.doi.org/10.1016/j.bbrc.2014.09.091.

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14

Kuo, Wen-Lin, Darrel W. Stafford, Jesús Cruces, Joe Gray та Solera Jesú. "Chromosomal localization of the γ-glutamyl carboxylase gene at 2p12". Genomics 25, № 3 (1995): 746–48. http://dx.doi.org/10.1016/0888-7543(95)80024-g.

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15

Wu, Sheue-Mei, Darrel W. Stafford, L. Dan Frazier та ін. "Genomic Sequence and Transcription Start Site for the Human γ-Glutamyl Carboxylase". Blood 89, № 11 (1997): 4058–62. http://dx.doi.org/10.1182/blood.v89.11.4058.

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Abstract The human gene for γ-glutamyl carboxylase is 13 kb in length and contains 15 exons. Transcription starts at a cytosine 217 base pair upstream of the first codon. There are two major transcripts in all tissues examined. They are distinguished by the presence of an Alu sequence in the 3′ nontranslated end of the longer species. Relative mRNA levels for 12 bovine tissues are presented.

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16

Schmidt-Krey, Ingeborg, Winfried Haase, Vasantha Mutucumarana, Darrel W. Stafford та Werner Kühlbrandt. "Two-dimensional crystallization of human vitamin K-dependent γ-glutamyl carboxylase". Journal of Structural Biology 157, № 2 (2007): 437–42. http://dx.doi.org/10.1016/j.jsb.2006.08.002.

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17

Romero, Elizabeth E., Umaima Marvi, Zachary E. Niman та David A. Roth. "The vitamin K–dependent γ-glutamyl carboxylase gene contains a TATA-less promoter with a novel upstream regulatory element". Blood 102, № 4 (2003): 1333–39. http://dx.doi.org/10.1182/blood-2002-12-3833.

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Abstract The expression of the vitamin K–dependent γ-glutamyl carboxylase gene in liver is developmentally regulated. Since the gene product catalyzes an essential post-translational modification of the vitamin K–dependent blood coagulation proteins, the regulation of carboxylase expression is critical for hemostasis. We analyzed the activity of the rat carboxylase gene 5′-regulatory DNA sequences in rat hepatoma cell lines at different states of differentiation. These studies demonstrated that the 2.6-kb 5′-flanking sequence has differentiation-dependent transcriptional activity. Transient ge

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18

SUTTIE, J. W., C. P. GROSSMAN та M. E. BENTON. "Specificity of the Vitamin K and Glutamyl Binding Sites of the Liver Microsomal γ-Glutamyl Carboxylase". Journal of Nutritional Science and Vitaminology 38, Special (1992): 405–8. http://dx.doi.org/10.3177/jnsv.38.special_405.

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19

Okazaki, Tomohiko, Keiji Nozaki, Nao Morimoto, et al. "Membrane topology inversion of GGCX mediates cytoplasmic carboxylation for antiviral defense." Science 389, no. 6755 (2025): 84–91. https://doi.org/10.1126/science.adk9967.

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Mitochondrial antiviral signaling protein (MAVS) is an adaptor involved in antiviral immunity, but its regulation is not fully understood. We identified carboxylation of MAVS by vitamin K (VK)–dependent γ-glutamyl carboxylase (GGCX), which was unexpected owing to the reported membrane topology of GGCX. We found that GGCX could undergo topology inversion to carboxylate MAVS within the cytoplasm. This carboxylation enhanced the ability of MAVS to induce type I interferons while suppressing the induction of apoptosis. Genetic knockout of GGCX, a VK-free diet, or depletion of VK by inhibiting VK e

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20

Presnell, Steven R., Ashutosh Tripathy, Barry R. Lentz, Da-Yun Jin та Darrel W. Stafford. "A Novel Fluorescence Assay To Study Propeptide Interaction with γ-Glutamyl Carboxylase†". Biochemistry 40, № 39 (2001): 11723–33. http://dx.doi.org/10.1021/bi010332w.

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21

Soute, Berry A. M., Magda M. W. Ulrich, A. David J. Watson, Jill E. Maddison, Rob H. M. Ebberink, and Cees Vermeer. "Congenital Deficiency of All Vitamin K-Dependent Blood Coagulation Factors Due to a Defective Vitamin K-Dependent Carboxylase in Devon Rex Cats." Thrombosis and Haemostasis 68, no. 05 (1992): 521–25. http://dx.doi.org/10.1055/s-0038-1646311.

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SummaryTwo Devon Rex cats from the same litter, which had no evidence of liver disease, malabsorption of vitamin K or chronic ingestion of coumarin derivatives, were found to have plasma deficiencies of factors II, VII, IX and X. Oral treatment with vitamin K1 resulted in the normalization of these coagulation factors. After taking liver biopsies it was demonstrated that the coagulation abnormality was accompanied by a defective γ-glutamyl-carboxylase, which had a decreased affinity for both vitamin K hydroquinone and propeptide. This observation prompted us to study in a well-defined in vitro

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22

Ghosh, Suvoshree, Johannes Oldenburg, and Katrin J. Czogalla-Nitsche. "The Role of GRP and MGP in the Development of Non-Hemorrhagic VKCFD1 Phenotypes." International Journal of Molecular Sciences 23, no. 2 (2022): 798. http://dx.doi.org/10.3390/ijms23020798.

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Vitamin K dependent coagulation factor deficiency type 1 (VKCFD1) is a rare hereditary bleeding disorder caused by mutations in γ-Glutamyl carboxylase (GGCX) gene. The GGCX enzyme catalyzes the γ-carboxylation of 15 different vitamin K dependent (VKD) proteins, which have function in blood coagulation, calcification, and cell signaling. Therefore, in addition to bleedings, some VKCFD1 patients develop diverse non-hemorrhagic phenotypes such as skin hyper-laxity, skeletal dysmorphologies, and/or cardiac defects. Recent studies showed that GGCX mutations differentially effect γ-carboxylation of

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23

RIEDER, M. J., A. P. REINER та A. E. RETTIE. "γ-Glutamyl carboxylase (GGCX) tagSNPs have limited utility for predicting warfarin maintenance dose". Journal of Thrombosis and Haemostasis 5, № 11 (2007): 2227–34. http://dx.doi.org/10.1111/j.1538-7836.2007.02744.x.

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24

Dubovyk, Ye I., V. Yu Harbuzova, O. A. Obukhova та A. V. Ataman. "ANALYSIS OF γ-GLUTAMYL CARBOXYLASE GENE rs2592551 POLYMORPHISM ASSOCIATION WITH ISCHEMIC ATHEROTHROMBOTIC STROKE". Fiziolohichnyĭ zhurnal 63, № 1 (2017): 33–42. http://dx.doi.org/10.15407/fz63.01.033.

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25

Cozzolino, Mario, Michela Mangano, Andrea Galassi, Paola Ciceri, Piergiorgio Messa, and Sagar Nigwekar. "Vitamin K in Chronic Kidney Disease." Nutrients 11, no. 1 (2019): 168. http://dx.doi.org/10.3390/nu11010168.

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Vitamin K is a composite term referring to a group of fat-soluble vitamins that function as a cofactor for the enzyme γ-glutamyl carboxylase (GGCX), which activates a number of vitamin K-dependent proteins (VKDPs) involved in haemostasis and vascular and bone health. Accumulating evidence demonstrates that chronic kidney disease (CKD) patients suffer from subclinical vitamin K deficiency, suggesting that this represents a population at risk for the biological consequences of poor vitamin K status. This deficiency might be caused by exhaustion of vitamin K due to its high requirements by vitami

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26

Azuma, Kotaro, Tohru Tsukui, Kazuhiro Ikeda та ін. "Liver-Specific γ-Glutamyl Carboxylase-Deficient Mice Display Bleeding Diathesis and Short Life Span". PLoS ONE 9, № 2 (2014): e88643. http://dx.doi.org/10.1371/journal.pone.0088643.

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27

Mutucumarana, Vasantha P., Darrel W. Stafford, Thomas B. Stanley та ін. "Expression and Characterization of the Naturally Occurring Mutation L394R in Human γ-Glutamyl Carboxylase". Journal of Biological Chemistry 275, № 42 (2000): 32572–77. http://dx.doi.org/10.1074/jbc.m006808200.

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28

Azuma, Kotaro, Sachiko Shiba, Tomoka Hasegawa та ін. "Osteoblast-Specific γ-Glutamyl Carboxylase-Deficient Mice Display Enhanced Bone Formation With Aberrant Mineralization". Journal of Bone and Mineral Research 30, № 7 (2015): 1245–54. http://dx.doi.org/10.1002/jbmr.2463.

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29

HOUBEN, Roger J. T. J., Dirk T. S. RIJKERS, Thomas B. STANLEY та ін. "Characteristics and composition of the vitamin K-dependent γ-glutamyl carboxylase-binding domain on osteocalcin". Biochemical Journal 364, № 1 (2002): 323–28. http://dx.doi.org/10.1042/bj3640323.

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Two different sites on vitamin K-dependent γ-glutamyl carboxylase (VKC) are involved in enzyme—substrate interaction: the propeptide-binding site required for high-affinity substrate binding and the active site for glutamate carboxylation. Synthetic descarboxy osteocalcin (d-OC) is a low-Km substrate for the VKC, but unique since it possesses a high-affinity recognition site for the VKC, distinct from the propeptide which is essential as a binding site for VKC. However, the exact location and composition of this VKC-recognition domain on d-OC has remained unclear until now. Using a stereospeci

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30

YAMAGATA, HIDEHARU, TOSHIMI NAKANISHI, MIDORI FURUKAWA, HIROAKI OKUDA та HIROSHI OBATA. "Levels of vitamin K, immunoreactive prothrombin, des-γ-carboxy prothrombin and γ-glutamyl carboxylase activity in hepatocellular carcinoma tissue". Journal of Gastroenterology and Hepatology 10, № 1 (1995): 8–13. http://dx.doi.org/10.1111/j.1440-1746.1995.tb01040.x.

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31

Hallgren, K. W., D. Zhang, M. Kinter, B. Willard та K. L. Berkner. "Methylation of γ-Carboxylated Glu (Gla) Allows Detection by Liquid Chromatography–Mass Spectrometry and the Identification of Gla Residues in the γ-Glutamyl Carboxylase". Journal of Proteome Research 12, № 6 (2013): 2365–74. http://dx.doi.org/10.1021/pr3003722.

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32

Darghouth, Dhouha, Kevin W. Hallgren, Rebecca L. Hain та ін. "Compound Heterozygosity in the Novel Mutations W157R and T591K in the γ-Glutamyl Carboxylase Gene Causes Hereditary Combined Vitamin K-Dependent Coagulation Factor Deficiency in a Tunisian Family." Blood 106, № 11 (2005): 2147. http://dx.doi.org/10.1182/blood.v106.11.2147.2147.

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Abstract Combined deficiency in vitamin K-dependent (VKD) coagulation factors is an autosomal recessive bleeding disorder associated with defects in either the VKD carboxylase which converts Glus to Glas in VKD proteins to render them active or the vitamin K epoxide reductase (VKORC1) which supplies the reduced vitamin K cofactor required for carboxylation. Such defects are rare, and we now report the fourth case of deficiency caused by mutations in the carboxylase gene. The mutations were identified in a two year old Tunisian girl who exhibited impaired function in several VKD procoagulant an

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33

Ueda, Naoki, Hidenori Shiraha, Tatsuya Fujikawa та ін. "Exon 2 deletion splice variant of γ-glutamyl carboxylase causes des-γ-carboxy prothrombin production in hepatocellular carcinoma cell lines". Molecular Oncology 2, № 3 (2008): 241–49. http://dx.doi.org/10.1016/j.molonc.2008.06.004.

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34

Price, Paul A., та Matthew K. Williamson. "Substrate recognition by the vitamin k-dependent γ-glutamyl carboxylase: Identification of a sequence homology between the carboxylase and the carboxylase recognition site in the substrate". Protein Science 2, № 11 (1993): 1987–88. http://dx.doi.org/10.1002/pro.5560021120.

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35

Czerwiec, Eva, Gail S. Begley, Mila Bronstein та ін. "Expression and characterization of recombinant vitamin K-dependent γ-glutamyl carboxylase from an invertebrate, Conus textile". European Journal of Biochemistry 269, № 24 (2002): 6162–72. http://dx.doi.org/10.1046/j.1432-1033.2002.03335.x.

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36

Romero, Elizabeth E., Rajat Deo, Leonardo J. Velazquez-Estades та David A. Roth. "Cloning, Structural Organization, and Transcriptional Activity of the Rat Vitamin K-Dependent γ-Glutamyl Carboxylase Gene". Biochemical and Biophysical Research Communications 248, № 3 (1998): 783–88. http://dx.doi.org/10.1006/bbrc.1998.8987.

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37

Bouchard, Beth A., Bruce Furie та Barbara C. Furie. "Glutamyl Substrate-Induced Exposure of a Free Cysteine Residue in the Vitamin K-Dependent γ-Glutamyl Carboxylase Is Critical for Vitamin K Epoxidation†". Biochemistry 38, № 29 (1999): 9517–23. http://dx.doi.org/10.1021/bi9907375.

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38

Li, Shuying, Barbara C. Furie, Bruce Furie та Christopher T. Walsh. "The Propeptide of the Vitamin K-Dependent Carboxylase Substrate Accelerates Formation of the γ-Glutamyl Carbanion Intermediate†". Biochemistry 36, № 21 (1997): 6384–90. http://dx.doi.org/10.1021/bi962816b.

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39

Lin, Pen-Jen, Da-Yun Jin, Jian-Ke Tie, Steven R. Presnell, David L. Straight та Darrel W. Stafford. "The Putative Vitamin K-dependent γ-Glutamyl Carboxylase Internal Propeptide Appears to Be the Propeptide Binding Site". Journal of Biological Chemistry 277, № 32 (2002): 28584–91. http://dx.doi.org/10.1074/jbc.m202292200.

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40

Romero, Elizabeth E., Leonardo J. Velazquez-Estades, Rajat Deo, Brian Schapiro та David A. Roth. "Cloning of Rat Vitamin K-Dependent γ-Glutamyl Carboxylase and Developmentally Regulated Gene Expression in Postimplantation Embryos". Experimental Cell Research 243, № 2 (1998): 334–46. http://dx.doi.org/10.1006/excr.1998.4151.

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41

Al-Doory, Sura Ahmed, Mahmoud Ahmed Radaideh, Shafeeka Mohamed Saleh, and Mohammed Ali Al Sabbah. "Congenital Vitamin K-Dependent Clotting Factors Deficiency Type 1: A Rare Bleeding Disorder." Dubai Medical Journal 3, no. 1 (2020): 8–12. http://dx.doi.org/10.1159/000506457.

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Combined deficiency of vitamin K-dependent clotting factors is usually an acquired clinical problem, often resulting from liver disease, malabsorption or warfarin overdose. However, an inherited form of the disease is very rare. Here we report a 4-month-old girl who presented with a 2-week history of multiple bruises and a 1-day history of right thigh swelling after receiving her 4th month vaccine. Laboratory investigations showed anemia (Hb 6.0 g/dL) with extremely prolonged PT and APTT. Factor assay revealed deficiency of vitamin K-dependent clotting factors II, VII, IX, X as well as protein

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42

Furie, Barbara C., та Bruce Furie. "Structure and Mechanism of Action of the Vitamin K-Dependent γ-Glutamyl Carboxylase: Recent Advances from Mutagenesis Studies". Thrombosis and Haemostasis 78, № 01 (1997): 595–98. http://dx.doi.org/10.1055/s-0038-1657595.

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43

Karl, Peter I., та Paul A. Friedman. "Responses of renal and hepatic vitamin k dependent γ-glutamyl carboxylase substrates to warfarin and vitamin k treatments". International Journal of Biochemistry 17, № 12 (1985): 1313–16. http://dx.doi.org/10.1016/0020-711x(85)90053-9.

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44

Roncaglioni, Maria Carla, Anna Paola Bolognese Dalessandro, Bruno Casali, Cees Vermeer та Maria Benedetta Donati. "γ-Glutamyl Carboxylase Activity in Experimental Tumor Tissues: A Biochemical Basis for Vitamin K Dependence of Cancer Procoagulant". Pathophysiology of Haemostasis and Thrombosis 16, № 3-4 (1986): 295–99. http://dx.doi.org/10.1159/000215301.

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45

Chin, Kok-Yong. "The Relationship between Vitamin K and Osteoarthritis: A Review of Current Evidence." Nutrients 12, no. 5 (2020): 1208. http://dx.doi.org/10.3390/nu12051208.

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Vitamin K is a cofactor of γ-glutamyl carboxylase, which plays an important role in the activation of γ-carboxyglutamate (gla)-containing proteins that negatively regulate calcification. Thus, vitamin K status might be associated with osteoarthritis (OA), in which cartilage calcification plays a role in the pathogenesis of the disease. This review collates the evidence on the relationship between vitamin K status (circulating or dietary intake level of vitamin K, or circulating uncarboxylated gla proteins) and OA from human observational studies and clinical trial, to examine its potential as

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46

Rost, Simone, Andreas Fregin, Dieter Koch, Markus Compes, Clemens R. Müller та Johannes Oldenburg. "Compound heterozygous mutations in the γ -glutamyl carboxylase gene cause combined deficiency of all vitamin K-dependent blood coagulation factors". British Journal of Haematology 126, № 4 (2004): 546–49. http://dx.doi.org/10.1111/j.1365-2141.2004.05071.x.

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47

Parker, Christine H., Christopher R. Morgan, Kasper D. Rand, John R. Engen, James W. Jorgenson та Darrel W. Stafford. "A Conformational Investigation of Propeptide Binding to the Integral Membrane Protein γ-Glutamyl Carboxylase Using Nanodisc Hydrogen Exchange Mass Spectrometry". Biochemistry 53, № 9 (2014): 1511–20. http://dx.doi.org/10.1021/bi401536m.

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48

Darghouth, Dhouha, Kevin W. Hallgren, Odile Issertial та ін. "Compound Heterozygosity of a W493C Substitution and R704/Premature Stop Codon within the γ-Glutamyl Carboxylase in Combined Vitamin K-Dependent Coagulation Factor Deficiency in a French Family." Blood 114, № 22 (2009): 1302. http://dx.doi.org/10.1182/blood.v114.22.1302.1302.

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Abstract Abstract 1302 Poster Board I-324 Combined vitamin K-dependent (VKD) coagulation factor deficiency is an autosomal recessive bleeding disorder associated with defects in either the γ-carboxylase (GGCX) which carboxylates VKD proteins to render them active or the vitamin K epoxide reductase (VKORC1) which supplies the reduced vitamin K cofactor required for carboxylation. Such deficiencies are rare, and due to mutations within either gene. Of note some mutations within the GGCX gene have recently been found associated with the pseudoxanthoma elasticum (PXE) syndrome, suggesting a role f

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CROSIER, Michael D., Inga PETER, Sarah L. BOOTH, Grace BENNETT, Bess DAWSON-HUGHES та Jose M. ORDOVAS. "Association of Sequence Variations in Vitamin K Epoxide Reductase and γ-Glutamyl Carboxylase Genes with Biochemical Measures of Vitamin K Status". Journal of Nutritional Science and Vitaminology 55, № 2 (2009): 112–19. http://dx.doi.org/10.3177/jnsv.55.112.

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Hirota, Yoshihisa, and Yoshitomo Suhara. "New Aspects of Vitamin K Research with Synthetic Ligands: Transcriptional Activity via SXR and Neural Differentiation Activity." International Journal of Molecular Sciences 20, no. 12 (2019): 3006. http://dx.doi.org/10.3390/ijms20123006.

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Vitamin K is classified into three homologs depending on the side-chain structure, with 2-methyl-1,4-naphthoqumone as the basic skeleton. These homologs are vitamin K1 (phylloquinone: PK), derived from plants with a phythyl side chain; vitamin K2 (menaquinone-n: MK-n), derived from intestinal bacteria with an isoprene side chain; and vitamin K3 (menadione: MD), a synthetic product without a side chain. Vitamin K homologs have physiological effects, including in blood coagulation and in osteogenic activity via γ-glutamyl carboxylase and are used clinically. Recent studies have revealed that vit

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