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  1. Article: Molecular basis of vitamin K-dependent gamma-carboxylation.

    Furie, B / Furie, B C

    Blood

    1990  Volume 75, Issue 9, Page(s) 1753–1762

    MeSH term(s) Amino Acid Sequence ; Blood Proteins/genetics ; Blood Proteins/metabolism ; Carbon-Carbon Ligases ; Humans ; Ligases/metabolism ; Molecular Sequence Data ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Vitamin K/metabolism ; Vitamin K/pharmacology
    Chemical Substances Blood Proteins ; Vitamin K (12001-79-5) ; Ligases (EC 6.-) ; Carbon-Carbon Ligases (EC 6.4.-) ; glutamyl carboxylase (EC 6.4.-)
    Language English
    Publishing date 1990-05-01
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

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  2. Article: Molecular basis of gamma-carboxylation. Role of the propeptide in the vitamin K-dependent proteins.

    Furie, B / Furie, B C

    Annals of the New York Academy of Sciences

    1991  Volume 614, Page(s) 1–10

    MeSH term(s) Amino Acid Sequence ; Animals ; Blood Coagulation Factors/genetics ; Humans ; Molecular Sequence Data ; Protein Precursors/genetics ; Protein Precursors/metabolism ; Protein Processing, Post-Translational ; Vitamin K/pharmacology ; Vitamin K/physiology
    Chemical Substances Blood Coagulation Factors ; Protein Precursors ; Vitamin K (12001-79-5)
    Language English
    Publishing date 1991
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 211003-9
    ISSN 1749-6632 ; 0077-8923
    ISSN (online) 1749-6632
    ISSN 0077-8923
    DOI 10.1111/j.1749-6632.1991.tb43687.x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Pseudoxanthoma elasticum: molecular genetics and putative pathomechanisms.

    Uitto, Jouni / Li, Qiaoli / Jiang, Qiujie

    The Journal of investigative dermatology

    2009  Volume 130, Issue 3, Page(s) 661–670

    Abstract: ... gla-protein (MGP) levels. MGP requires to be activated by gamma-glutamyl carboxylation, a vitamin K ... hypothesized that a critical vitamin K derivative, such as reduced vitamin K conjugated with glutathione, is ... dependent reaction, to serve in an anti-mineralization role in the peripheral connective tissue cells ...

    Abstract Pseudoxanthoma elasticum (PXE), a prototypic heritable disorder with ectopic mineralization, manifests with characteristic skin findings, ocular involvement and cardiovascular problems, with considerable morbidity and mortality. The classic forms of PXE are due to loss-of-function mutations in the ABCC6 gene, which encodes ABCC6, a transmembrane efflux transporter expressed primarily in the liver. Several lines of evidence suggest that PXE is a primary metabolic disorder, which in the absence of ABCC6 transporter activity, displays reduced plasma anti-mineralization capacity due to reduced fetuin-A and matrix gla-protein (MGP) levels. MGP requires to be activated by gamma-glutamyl carboxylation, a vitamin K-dependent reaction, to serve in an anti-mineralization role in the peripheral connective tissue cells. Although the molecules transported from the hepatocytes to circulation by ABCC6 in vivo remain unidentified, it has been hypothesized that a critical vitamin K derivative, such as reduced vitamin K conjugated with glutathione, is secreted to circulation physiologically, but not in the absence of ABCC6 transporter activity. As a result, activation of MGP by gamma-glutamyl carboxylase is diminished, allowing slow yet progressive mineralization of connective tissues characteristic of PXE. Understanding of the pathomechanistic details of PXE provides a basis for the development of targeted molecular therapies for this currently intractable disease.
    MeSH term(s) ATP-Binding Cassette Transporters/genetics ; ATP-Binding Cassette Transporters/metabolism ; Animals ; Blood Proteins/metabolism ; Calcium-Binding Proteins/metabolism ; Carbon-Carbon Ligases/metabolism ; Connective Tissue/metabolism ; Extracellular Matrix Proteins/metabolism ; Humans ; Liver/metabolism ; Mice ; Mice, Knockout ; Multidrug Resistance-Associated Proteins/genetics ; Multidrug Resistance-Associated Proteins/metabolism ; Phenotype ; Pseudoxanthoma Elasticum/genetics ; Pseudoxanthoma Elasticum/metabolism ; Pseudoxanthoma Elasticum/therapy ; Vitamin K/metabolism ; alpha-2-HS-Glycoprotein ; Matrix Gla Protein
    Chemical Substances ABCC6 protein, human ; AHSG protein, human ; ATP-Binding Cassette Transporters ; Abcc6 protein, mouse ; Ahsg protein, mouse ; Blood Proteins ; Calcium-Binding Proteins ; Extracellular Matrix Proteins ; Multidrug Resistance-Associated Proteins ; alpha-2-HS-Glycoprotein ; Vitamin K (12001-79-5) ; Carbon-Carbon Ligases (EC 6.4.-) ; glutamyl carboxylase (EC 6.4.-)
    Language English
    Publishing date 2009-12-24
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80136-7
    ISSN 1523-1747 ; 0022-202X
    ISSN (online) 1523-1747
    ISSN 0022-202X
    DOI 10.1038/jid.2009.411
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: Molecular basis of hemophilia B: a defective enzyme due to an unprocessed propeptide is caused by a point mutation in the factor IX precursor.

    Diuguid, D L / Rabiet, M J / Furie, B C / Liebman, H A / Furie, B

    Proceedings of the National Academy of Sciences of the United States of America

    1986  Volume 83, Issue 16, Page(s) 5803–5807

    Abstract: ... sequence in substrate recognition by the vitamin K-dependent carboxylase. This represents an example ... and interferes with gamma-carboxylation of the factor IX, indicating the importance of the leader ... the molecular basis of some forms of hemophilia and other hereditary enzyme deficiencies. ...

    Abstract A mutant factor IX, designated factor IXCambridge, was isolated from a patient with hemophilia B. This protein includes an 18-residue propeptide attached to the NH2 terminus of factor IX. A point mutation at residue -1, from an arginine to a serine, precludes cleavage of the propeptide by a processing protease and interferes with gamma-carboxylation of the factor IX, indicating the importance of the leader sequence in substrate recognition by the vitamin K-dependent carboxylase. This represents an example of an enzyme defect due to the presence of a point mutation in a precursor protein (preproenzyme) that is the cause of a human hereditary disease. This defect will serve as a prototype for understanding the molecular basis of some forms of hemophilia and other hereditary enzyme deficiencies.
    MeSH term(s) Amino Acid Sequence ; DNA/analysis ; Factor IX/genetics ; Factor IX/metabolism ; Hemophilia A/blood ; Hemophilia A/genetics ; Humans ; Kinetics ; Mutation ; Phospholipids/blood ; Protein Binding ; Protein Conformation ; Protein Precursors/genetics ; Protein Precursors/metabolism
    Chemical Substances Phospholipids ; Protein Precursors ; factor IX Cambridge ; Factor IX (9001-28-9) ; DNA (9007-49-2)
    Language English
    Publishing date 1986-08
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.83.16.5803
    Database MEDical Literature Analysis and Retrieval System OnLINE

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