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Journal articles on the topic 'Carboxylase. Vitamine K'

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Published: 4 June 2021

Last updated: 5 February 2022

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1

Sun, Yan-Mei, Da-Yun Jin, Rodney M. Camire, and Darrel W. Stafford. "Vitamin K epoxide reductase significantly improves carboxylation in a cell line overexpressing factor X." Blood 106, no. 12 (2005): 3811–15. http://dx.doi.org/10.1182/blood-2005-06-2495.

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Previously we reported that we could increase the fraction of carboxylated factor X by reducing the affinity of the propeptide for its binding site on human gamma glutamyl carboxylase. We attributed this to an increased turnover rate. However, even with the reduced affinity propeptide, when sufficient overproduction of factor X is achieved, there is still a significant fraction of uncarboxylated recombinant factor X. We report here that the factor X of such a cell line was only 52% carboxylated but that the fraction of carboxylated factor X could be increased to 92% by coexpressing the recentl

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2

Darghouth, Dhouha, Kevin W. Hallgren, Rebecca L. Shtofman, et al. "Compound heterozygosity of novel missense mutations in the gamma-glutamyl-carboxylase gene causes hereditary combined vitamin K–dependent coagulation factor deficiency." Blood 108, no. 6 (2006): 1925–31. http://dx.doi.org/10.1182/blood-2005-12-010660.

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AbstractHereditary combined vitamin K–dependent (VKD) coagulation factor deficiency is an autosomal recessive bleeding disorder associated with defects in either the γ-carboxylase, 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 we report the fourth case resulting from mutations in the carboxylase gene, identified in a Tunisian girl who exhibited impaired function in hemostatic VKD factors that was not restored by vitamin K administration

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3

Van Haarlem, L. J. M., M. M. W. Ulrich, H. C. Hemker, B. A. M. Soute, and C. Vermeer. "Isolation and partial characterization of a vitamin K-dependent carboxylase from bovine aortae." Biochemical Journal 245, no. 1 (1987): 251–55. http://dx.doi.org/10.1042/bj2450251.

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Vitamin K-dependent carboxylase activity has been demonstrated in the crude microsomal fraction of the intima of bovine aortae. The procedure for the isolation of vessel wall carboxylase is a slight modification of the general preparation procedure for tissue microsomes. The highest activity of the non-hepatic enzyme was observed at 25 degrees C and hardly any NADH-dependent vitamin K reductase could be demonstrated. The optimal reaction conditions for both vessel wall as well as liver carboxylase were similar: 0.1 M-NaCl/0.05 M-Tris/HCl, pH 7.4, containing 8 mM-dithiothreitol, 0.4% 3-[(3-chol

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4

Fusaro, Maria, Giuseppe Cianciolo, Maria Luisa Brandi, et al. "Vitamin K and Osteoporosis." Nutrients 12, no. 12 (2020): 3625. http://dx.doi.org/10.3390/nu12123625.

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Vitamin K acts as a coenzyme of carboxylase, catalyzing the carboxylation of several vitamin K dependent proteins. Beyond its well-known effects on blood coagulation, it also exerts relevant effects on bone and the vascular system. In this review, we point out the relevance of an adequate vitamin K intake to obtain sufficient levels of carboxylated (active form) vitamin K dependent proteins (such as Osteocalcin and matrix Gla protein) to prevent bone health. Another bone-related action of Vitamin K is being a ligand of the nuclear steroid and xenobiotic receptor (SXR). We also discuss the reco

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5

Pudota, B. Nirmala, Eric L. Hommema, Kevin W. Hallgren, Beth A. McNally, Susan Lee та Kathleen L. Berkner. "Identification of Sequences within the γ-Carboxylase That Represent a Novel Contact Site with Vitamin K-dependent Proteins and That Are Required for Activity". Journal of Biological Chemistry 276, № 50 (2001): 46878–86. http://dx.doi.org/10.1074/jbc.m108696200.

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The vitamin K-dependent (VKD) carboxylase converts clusters of Glu residues to γ-carboxylated Glu residues (Glas) in VKD proteins, which is required for their activity. VKD precursors are targeted to the carboxylase by their carboxylase recognition site, which in most cases is a propeptide. We have identified a second tethering site for carboxylase and VKD proteins that is required for carboxylase activity, called the vitamin K-dependent protein site of interaction (VKS). Several VKD proteins specifically bound an immobilized peptide comprising amino acids 343–355 of the human carboxylase (CVY

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6

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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7

Berg, Marian de Boer-van den, Henk H. W. Thijssen, and Cees Vermeer. "The In Vivo Effects of Oral Anticoagulants in Man: Comparison Between Liver and Non-Hepatic Tissues." Thrombosis and Haemostasis 59, no. 02 (1988): 147–50. http://dx.doi.org/10.1055/s-0038-1642744.

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SummaryThe in vivo effects of oral anticoagulant therapy with 4–hydroxycoumarins on various vitamin K–dependent enzyme systems in man were compared. In hepatic microsomes obtained from donors who has been treated with 4–hydroxycoumarins for more than 6 months, the vitamin K 2,3 epoxide reductase activity and the DTT–dependent vitamin K quinone reductase activity were diminished to 35% and 20% of the corresponding normal values. In the non–hepatic tissues, only a small decrease in vitamin K 2,3 epoxide reductase activity could be demonstrated, while no differences were found in the vitamin K qu

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8

Coutu, Daniel L., Jian Wui Wu, Georges-Etienne Rivard, Mark D. Blostein та 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, № 11 (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 prot

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9

MORITA, Takashi. "Vitamin K-Dependent Carboxylase." Japanese Journal of Thrombosis and Hemostasis 1, no. 4 (1990): 362–66. http://dx.doi.org/10.2491/jjsth.1.362.

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10

Suttie, J. W. "Vitamin K-Dependent Carboxylase." Annual Review of Biochemistry 54, no. 1 (1985): 459–77. http://dx.doi.org/10.1146/annurev.bi.54.070185.002331.

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11

LARUE, VALÉRY, JOSYANE GHARBI-BENAROUS, FRANCINE ACHER, ROBERT AZERAD, and JEAN-PIERRE GIRAULT. "Vitamin K-dependent carboxylase." Journal of Peptide Research 49, no. 1 (2009): 28–45. http://dx.doi.org/10.1111/j.1399-3011.1997.tb01118.x.

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12

Popa, Daniela-Saveta, Galya Bigman, and Marius Emil Rusu. "The Role of Vitamin K in Humans: Implication in Aging and Age-Associated Diseases." Antioxidants 10, no. 4 (2021): 566. http://dx.doi.org/10.3390/antiox10040566.

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As human life expectancy is rising, the incidence of age-associated diseases will also increase. Scientific evidence has revealed that healthy diets, including good fats, vitamins, minerals, or polyphenolics, could have antioxidant and anti-inflammatory activities, with antiaging effects. Recent studies demonstrated that vitamin K is a vital cofactor in activating several proteins, which act against age-related syndromes. Thus, vitamin K can carboxylate osteocalcin (a protein capable of transporting and fixing calcium in bone), activate matrix Gla protein (an inhibitor of vascular calcificatio

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13

Presnell, Steven, and Darrel Stafford. "The Vitamin K-dependent Carboxylase." Thrombosis and Haemostasis 87, no. 06 (2002): 937–46. http://dx.doi.org/10.1055/s-0037-1613115.

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14

Berkner, Kathleen L. "The Vitamin K–Dependent Carboxylase." Journal of Nutrition 130, no. 8 (2000): 1877–80. http://dx.doi.org/10.1093/jn/130.8.1877.

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15

Berkner, Kathleen L. "THE VITAMIN K–DEPENDENT CARBOXYLASE." Annual Review of Nutrition 25, no. 1 (2005): 127–49. http://dx.doi.org/10.1146/annurev.nutr.25.050304.092713.

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16

Tie, Jian-Kie, Mei-Yan Zheng, Darrel W. Stafford, and David L. Straight. "Expression of a Two Chain Gamma-Glutamyl Carboxylase: Importance of Disulfide Bond Formation and Transmembrane Domain Interactions." Blood 108, no. 11 (2006): 1694. http://dx.doi.org/10.1182/blood.v108.11.1694.1694.

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Abstract The vitamin K-dependent carboxylase is an integral membrane protein with five transmembrane domains (TMDs). It catalyzes the post-translational modification of specific glutamic acid residues of vitamin K-dependent proteins to gamma-carboxyglutamic acid residues. This posttranslational modification is critical for the biological functions of blood coagulation. The native enzyme is a single chain molecule with one disulfide bond. In this study, we have expressed carboxylase as two chains: residues 1–345 and 346–758 in the same insect cells. Our results show that these two fragments are

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17

Wallin, Reidar, Nadeem Wajih та John Owen. "Enhanced Synthesis of Functional Recombinant Factors IX and VII by BHK Cells Engineered to Overexpress VKORC1 Combined with siRNA Silencing of the γ-Carboxylation Inhibitor Calumenin." Blood 108, № 11 (2006): 1707. http://dx.doi.org/10.1182/blood.v108.11.1707.1707.

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Abstract Because of the importance and demand for recombinant factors IX, VII and protein C in prophylactic medicine, our laboratory is focused on engineering eukaryotic cells with enhanced capacity to produce fully γ-carboxylated functional forms of these recombinant vitamin K-dependent proteins. Here we report our work on recombinant human factor IX (r-hFIX) and recombinant human factor VII (r-hFVII). Successful engineering was accomplished by overexpressing the vitamin K cofactor producing enzyme VKORC1 of the vitamin K cycle in BHK cells stably overexpressing r-hFIX and r-hFVII respectivel

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18

Chatron, Nolan, Abdessalem Hammed, Etienne Benoît, and Virginie Lattard. "Structural Insights into Phylloquinone (Vitamin K1), Menaquinone (MK4, MK7), and Menadione (Vitamin K3) Binding to VKORC1." Nutrients 11, no. 1 (2019): 67. http://dx.doi.org/10.3390/nu11010067.

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Vitamin K family molecules—phylloquinone (K1), menaquinone (K2), and menadione (K3)—act as γ-glutamyl carboxylase (GGCX)-exclusive cofactors in their hydroquinone state, activating proteins of main importance for blood coagulation in the liver and for arterial calcification prevention and energy metabolism in extrahepatic tissues. Once GGCX is activated, vitamin K is found in the epoxide state, which is then recycled to quinone and hydroquinone states by vitamin K epoxide reductase (VKORC1). Nevertheless, little information is available concerning vitamin K1, K2, or K3 tissue distribution and

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19

Bristol, JA, JV Ratcliffe, DA Roth, MA Jacobs, BC Furie, and B. Furie. "Biosynthesis of prothrombin: intracellular localization of the vitamin K-dependent carboxylase and the sites of gamma-carboxylation." Blood 88, no. 7 (1996): 2585–93. http://dx.doi.org/10.1182/blood.v88.7.2585.bloodjournal8872585.

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Prothrombin is a vitamin K-dependent blood coagulation protein that undergoes posttranslational gamma-carboxylation and propeptide cleavage during biosynthesis. The propeptide contains the gamma-carboxylation recognition site that directs gamma-carboxylation. To identify the intracellular sites of carboxylation and propeptide cleavage, we monitored the synthesis of prothrombin in Chinese hamster ovary cells stably transfected with the prothrombin cDNA by immunofluorescent staining. The vitamin K-dependent carboxylase was located in the endoplasmic reticulum and Golgi complex. Antibodies specif

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20

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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21

SUGIURA, Isamu. "Vitamin K-dependent .GAMMA.-glutamyl Carboxylase." Japanese Journal of Thrombosis and Hemostasis 10, no. 1 (1999): 22–35. http://dx.doi.org/10.2491/jjsth.10.22.

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22

de Boer-van den Berg, Marian A. G., Cees P. H. J. Verstijnen, and Cees Vermeer. "Vitamin K-Dependent Carboxylase in Skin." Journal of Investigative Dermatology 87, no. 3 (1986): 377–80. http://dx.doi.org/10.1111/1523-1747.ep12524848.

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23

Ulrich, Magda M. W., Berry A. M. Soute, Marian A. G. de Boer-van den Berg, and Cees Vermeer. "Isoenzymes of vitamin-K-dependent carboxylase." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 830, no. 1 (1985): 105–8. http://dx.doi.org/10.1016/0167-4838(85)90138-4.

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24

Ulrich, Magda M. W., Berry A. M. Soute, L. Johan M. van Haarlem, and Cees Vermeer. "Substrate Recognition by Vitamin K-Dependent Carboxylase." Thrombosis and Haemostasis 57, no. 01 (1987): 017–19. http://dx.doi.org/10.1055/s-0038-1651053.

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SummaryDecarboxylated osteocalcins were prepared and purified from bovine, chicken, human and monkey bones and assayed for their ability to serve as a substrate for vitamin K-dependent carboxylase from bovine liver. Substantial differences were observed, especially between bovine and monkey d-osteocalcin. Since these substrates differ only in their amino acid residues 3 and 4, it seems that these residues play a role in the recognition of a substrate by hepatic carboxylase.

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25

McTigue, John J., and J. W. Suttie. "Oxygen dependence of vitamin K-dependent carboxylase and vitamin K epoxidase." FEBS Letters 200, no. 1 (1986): 71–75. http://dx.doi.org/10.1016/0014-5793(86)80513-0.

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26

Wallin, R., and L. F. Martin. "Warfarin poisoning and vitamin K antagonism in rat and human liver. Design of a system in vitro that mimics the situation in vivo." Biochemical Journal 241, no. 2 (1987): 389–96. http://dx.doi.org/10.1042/bj2410389.

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The present paper describes a system in vitro that has been developed to mimic vitamin K metabolism and vitamin K function in liver. In this system the two pathways that are known to participate in vitamin K reduction are active and the vitamin K-dependent carboxylase accepts a synthetic pentapeptide as substrate. With this system in vitro the effect of warfarin on both pathways was examined under conditions which simulated a warfarin-poisoned liver. Identical experiments were completed with rat and human liver. All activities currently associated with vitamin K metabolism and vitamin K functi

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27

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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28

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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29

Berkner, K. L., and B. N. Pudota. "Vitamin K-dependent carboxylation of the carboxylase." Proceedings of the National Academy of Sciences 95, no. 2 (1998): 466–71. http://dx.doi.org/10.1073/pnas.95.2.466.

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30

Shah, DV, JA Engelke, and JW Suttie. "Abnormal prothrombin in the plasma of rats carrying hepatic tumors." Blood 69, no. 3 (1987): 850–54. http://dx.doi.org/10.1182/blood.v69.3.850.850.

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Abstract Vitamin K is required for the posttranslational formation of gamma- carboxyglutamyl residues in a number of plasma clotting factors. Interference with vitamin K action results in the appearance of abnormal (des-gamma-carboxy) forms of prothrombin in human plasma. Vitamin K-sufficient patients with primary hepatocellular carcinoma also secrete significant quantities of abnormal prothrombin; this response has now been studied in a rat model. Normal Buffalo strain rats had 9 micrograms/mL of circulating plasma abnormal prothrombin, whereas Buffalo strain rats carrying the transplantable

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31

Shah, DV, JA Engelke, and JW Suttie. "Abnormal prothrombin in the plasma of rats carrying hepatic tumors." Blood 69, no. 3 (1987): 850–54. http://dx.doi.org/10.1182/blood.v69.3.850.bloodjournal693850.

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Vitamin K is required for the posttranslational formation of gamma- carboxyglutamyl residues in a number of plasma clotting factors. Interference with vitamin K action results in the appearance of abnormal (des-gamma-carboxy) forms of prothrombin in human plasma. Vitamin K-sufficient patients with primary hepatocellular carcinoma also secrete significant quantities of abnormal prothrombin; this response has now been studied in a rat model. Normal Buffalo strain rats had 9 micrograms/mL of circulating plasma abnormal prothrombin, whereas Buffalo strain rats carrying the transplantable Morris he

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32

von Brederlow, B., A. Fregin, S. Rost, et al. "Congenital Deficiency of Vitamin K Dependent Coagulation Factors in Two Families Presents as a Genetic Defect of the Vitamin K-Epoxide-Reductase-Complex." Thrombosis and Haemostasis 84, no. 12 (2000): 937–41. http://dx.doi.org/10.1055/s-0037-1614152.

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SummaryHereditary combined deficiency of the vitamin K dependent coagulation factors is a rare bleeding disorder. To date, only eleven families have been reported in the literature. The phenotype varies considerably with respect to bleeding tendency, response to vitamin K substitution and the presence of skeletal abnormalities, suggesting genetic heterogeneity. In only two of the reported families the cause of the disease has been elucidated as either a defect in the γ-carboxylase enzyme (1) or in a protein of the vitamin K 2,3-epoxide reductase (VKOR) complex (2).Here we present a detailed ph

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33

Rannels, S. R., M. L. Cancela, E. B. Wolpert, and P. A. Price. "Matrix Gla protein mRNA expression in cultured type II pneumocytes." American Journal of Physiology-Lung Cellular and Molecular Physiology 265, no. 3 (1993): L270—L278. http://dx.doi.org/10.1152/ajplung.1993.265.3.l270.

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Matrix Gla protein (MGP) was first isolated from the matrix fraction of bone. This highly conserved vitamin K-dependent protein of 14 kDa has been identified in numerous tissues and cells, and its mRNA was recently found to be abundant in rat lung. Relatively low MGP protein levels in many soft tissues where its mRNA is high suggests an important secretory function for this protein. We have found a high specific activity of vitamin K-dependent carboxylase in microsomes of rat pulmonary type II cells and the presence of numerous endogenous substrates, including one of 13-15 kDa. To investigate

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34

Kuliopulos, Athan, Brian R. Hubbard, Zamas Lam, et al. "Dioxygen transfer during vitamin K dependent carboxylase catalysis." Biochemistry 31, no. 33 (1992): 7722–28. http://dx.doi.org/10.1021/bi00148a037.

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35

Romiti, Steven, and William K. Kappel. "Modification of the vitamin K-dependent carboxylase assay." Journal of Biochemical and Biophysical Methods 11, no. 1 (1985): 59–68. http://dx.doi.org/10.1016/0165-022x(85)90041-7.

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36

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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37

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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38

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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39

Gilbert, Kirk A., and Stephen R. Rannels. "Glucocorticoid effects on vitamin K-dependent carboxylase activity and matrix Gla protein expression in rat lung." American Journal of Physiology-Lung Cellular and Molecular Physiology 285, no. 3 (2003): L569—L577. http://dx.doi.org/10.1152/ajplung.00426.2002.

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The role of glucocorticoids in the regulation of vitamin K-dependent carboxylase activity was investigated in fetal and adult lung. Glucocorticoid deficiency induced by adrenalectomy (ADX) stimulated adult lung growth and reduced carboxylation in a tissue-specific manner. Type II epithelial cells were enriched in carboxylase activity, where ADX-induced downregulation was retained in freshly isolated cells. Carboxylase activity in fetal type II cells was one-half that found in fetal fibroblasts isolated from the same lungs, and both populations increased activity with time in culture. Both carb

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40

Wu, Sangwook, Shubin Liu, Charles H. Davis, Darrel W. Stafford, John D. Kulman, and Lee G. Pedersen. "A hetero-dimer model for concerted action of vitamin K carboxylase and vitamin K reductase in vitamin K cycle." Journal of Theoretical Biology 279, no. 1 (2011): 143–49. http://dx.doi.org/10.1016/j.jtbi.2011.03.030.

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41

Tie, Jian-Ke, Da-Yun Jin, David L. Straight, and Darrel W. Stafford. "Functional study of the vitamin K cycle in mammalian cells." Blood 117, no. 10 (2011): 2967–74. http://dx.doi.org/10.1182/blood-2010-08-304303.

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Abstract We describe a cell-based assay for studying vitamin K–cycle enzymes. A reporter protein consisting of the gla domain of factor IX (amino acids 1-46) and residues 47-420 of protein C was stably expressed in HEK293 and AV12 cells. Both cell lines secrete carboxylated reporter when fed vitamin K or vitamin K epoxide (KO). However, neither cell line carboxylated the reporter when fed KO in the presence of warfarin. In the presence of warfarin, vitamin K rescued carboxylation in HEK293 cells but not in AV12 cells. Dicoumarol, an NAD(P)H-dependent quinone oxidoreductase 1 (NQO1) inhibitor,

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Wallin, R., and R. Turner. "Propeptide recognition by the vitamin K-dependent carboxylase in early processing of prothrombin and factor X." Biochemical Journal 272, no. 2 (1990): 473–78. http://dx.doi.org/10.1042/bj2720473.

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Precursors of vitamin K-dependent proteins are synthesized with a propeptide that is believed to target these proteins for gamma-carboxylation by the vitamin K-dependent carboxylase. In this study synthetic propeptides were used to investigate gamma-carboxylation of the prothrombin and factor X precursors in rat liver microsomes. The extent of prothrombin processing by the carboxylase was also investigated. Antisera raised against the human prothrombin and factor X propeptides only recognized precursors with the respective propeptide regions. The data demonstrate structural differences in the

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Naganathan, Sriram, Roger Hershline, Seung Wook Ham, and Paul Dowd. "The Active Site of Vitamin K and the Role of the Vitamin K-Dependent Carboxylase." Journal of the American Chemical Society 116, no. 22 (1994): 9831–39. http://dx.doi.org/10.1021/ja00101a003.

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Liu, Ying, Albert N. Nelson, and James J. Lipsky. "Vitamin K-Dependent Carboxylase: mRNA Distribution and Effects of Vitamin K-Deficiency and Warfarin Treatment." Biochemical and Biophysical Research Communications 224, no. 2 (1996): 549–54. http://dx.doi.org/10.1006/bbrc.1996.1063.

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Suttie, J. W., and P. C. Preusch. "Studies of the Vitamin K-Dependent Carboxylase and Vitamin K Epoxide Reductase in Rat Liver." Pathophysiology of Haemostasis and Thrombosis 16, no. 3-4 (1986): 193–215. http://dx.doi.org/10.1159/000215293.

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McGee, Maria P., Reidar Wallin, Robert Devlin, and Henry Rothberger. "Identification of mRNA Coding for Factor VII Protein in Human Alveolar Macrophages - Coagulant Expression May Be Limited Due to Deficient Postribosomal Processing." Thrombosis and Haemostasis 61, no. 02 (1989): 170–74. http://dx.doi.org/10.1055/s-0038-1646553.

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Clotting factors synthesized by monocytes and macrophages may initiate coagulation reactions during inflammation. Functional vitamin K-dependent coagulation factors have been found to be associated with human monocytes/macrophages, but there are no reports identifying mRNA coding for vitamin K-dependent proteins in these cells. In the present studies, factor VII mRNA was found in total RNA extracted from freshly isolated human alveolar macrophages using hybridization with a complementary DNA probe. On the other hand, vitamin K-dependent carboxylase activity which is required for postribosomal

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Grossman, Carol P., and J. W. Suttie. "Vitamin K-dependent carboxylase: Inhibitory action of polychlorinated phenols." Biochemical Pharmacology 40, no. 6 (1990): 1351–55. http://dx.doi.org/10.1016/0006-2952(90)90403-8.

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Vermeer, C. "Comparison between Hepatic and Nonhepatic Vitamin K-Dependent Carboxylase." Pathophysiology of Haemostasis and Thrombosis 16, no. 3-4 (1986): 239–45. http://dx.doi.org/10.1159/000215296.

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Cheung, Alex, J. W. Suttie, and M. Bernatowicz. "Vitamin K-dependent carboxylase: structural requirements for propeptide activation." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1039, no. 1 (1990): 90–93. http://dx.doi.org/10.1016/0167-4838(90)90230-d.

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Wallin, R., and S. R. Rannels. "Identification of vitamin K-dependent carboxylase activity in lung type II cells but not in lung macrophages." Biochemical Journal 250, no. 2 (1988): 557–63. http://dx.doi.org/10.1042/bj2500557.

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Fluorography of 14C-labelled glutamic acid residues in vitamin K-dependent protein precursors in lung microsomes (microsomal fractions) shows that the lung has several substrates that are not found in the liver. These precursor proteins unique to the lung have apparent molecular masses of 65, 53, 50, 36, 31 and 13 kDa. Type II epithelial cells appear to synthesize most of the vitamin K-dependent proteins in the lung. The 36 and the 31 kDa precursors also found in Type-II-cell microsomes have a similar molecular mass to those of surfactant-associated proteins, and we have previously shown [Rann

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