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  1. Article: The Importance of the Binding of Factor Xa to Phospholipids in the Inhibitory Mechanism of Tissue Factor Pathway Inhibitor: The Transmembrane and Cytoplasmic Domains of Tissue Factor Are not Essential for the Inhibitory Action of Tissue Factor Pathway Inhibitor

    Kazama, Yoshiaki

    Thrombosis and Haemostasis

    1997  Volume 77, Issue 03, Page(s) 492–497

    Abstract: To investigate the inhibitory mechanism of tissue factor pathway inhibitor (TFPI), an attempt was made to examine the inhibitory activity of TFPI toward the factor Vila-truncated tissue factor (TF 1-219 ) complex, which lacks its transmembrane and ... ...

    Abstract To investigate the inhibitory mechanism of tissue factor pathway inhibitor (TFPI), an attempt was made to examine the inhibitory activity of TFPI toward the factor Vila-truncated tissue factor (TF 1-219 ) complex, which lacks its transmembrane and cytoplasmic domains. Factor VIIa-TF 1-219 activity was significantly inhibited by TFPI-factor Xa complex in the presence of phospholipids, but was not in the absence of phospholipids. In addition, TFPI did not inhibit factor VIIa-TF 1-219 activity in the presence of γ-carboxyglutamic acid-domainless factor Xa. The ability of TFPI-factor Xa complex to inhibit factor VIIa-TF 1-219 activity was totally dependent on the presence of phospholipids and was neutralized by prothrombin fragment 1 in a dose-dependent manner. These results indicate that the transmembrane and cytoplasmic domains of tissue factor are not essential for the inhibitory mechanism of TFPI and confirm that the binding of factor Xa to phospholipids through its γ-carboxyglutamic acid domain is essential for this reaction.
    Language English
    Publishing date 1997-01-01
    Publisher Schattauer GmbH
    Publishing place Stuttgart ; New York
    Document type Article
    ZDB-ID 518294-3
    ISSN 2567-689X ; 0340-6245
    ISSN (online) 2567-689X
    ISSN 0340-6245
    DOI 10.1055/s-0038-1655995
    Database Thieme publisher's database

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  2. Article: Modulation of Protein C Inhibitor Activity by Histidine-Rich Glycoprotein and Platelet Factor 4: Role of Zinc and Calcium Ions in the Heparin-Neutralizing Ability of Histidine-Rich Glycoprotein

    Kazama, Yoshiaki / Koide, Takehiko

    Thrombosis and Haemostasis

    1992  Volume 67, Issue 01, Page(s) 50–55

    Abstract: Effects of zinc and calcium ions on the heparin-neutralizing abilities of histidine-rich glycoprotein (HRG) and platelet factor 4 (PF4) were examined. Both HRG and PF4 effectively neutralized the ability of heparin to accelerate the activated protein C ( ... ...

    Abstract Effects of zinc and calcium ions on the heparin-neutralizing abilities of histidine-rich glycoprotein (HRG) and platelet factor 4 (PF4) were examined. Both HRG and PF4 effectively neutralized the ability of heparin to accelerate the activated protein C (APC) and the thrombin inhibitions by protein C inhibitor (PCI). The heparin-neutralizing ability of HRG in the APC inhibition by PCI, however, was decreased in a Ca 2+ -dependent manner and apparently lost at 1 mM Ca 2+, while it was enhanced by Zn 2+ regardless of the presence or absence of Ca 2+. The heparinneutralizing ability of HRG in the thrombin inhibition by PCI was not affected by Ca 2+.In contrast to HRG, there was no significant difference in the heparin-neutralizing ability of PF4 in the presence or absence of 1 mM Ca 2+. These results strongly suggest additional physiological functions of HRG and PF4 as modulators of PCI.
    Language English
    Publishing date 1992-01-01
    Publisher Schattauer GmbH
    Publishing place Stuttgart ; New York
    Document type Article
    ZDB-ID 518294-3
    ISSN 2567-689X ; 0340-6245
    ISSN (online) 2567-689X
    ISSN 0340-6245
    DOI 10.1055/s-0038-1648378
    Database Thieme publisher's database

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  3. Article: Nucleotide Sequence of the Gene Encoding Murine Tissue Factor Pathway Inhibitor-2

    Kazama, Yoshiaki / Kamei, Shintaro / Kuijper, Joseph L. / Foster, Donald C. / Kisiel, Walter

    Thrombosis and Haemostasis

    2000  Volume 83, Issue 01, Page(s) 141–147

    Abstract: Summary Tissue factor pathway inhibitor-2 (TFPI-2), also known as placental protein 5, is a 32 kDa extracellular matrix-associated serine proteinase inhibitor consisting of three tandemly-arranged Kunitz-type domains. Two overlapping genomic clones ... ...

    Abstract Summary Tissue factor pathway inhibitor-2 (TFPI-2), also known as placental protein 5, is a 32 kDa extracellular matrix-associated serine proteinase inhibitor consisting of three tandemly-arranged Kunitz-type domains. Two overlapping genomic clones containing sequences encoding murine TFPI-2 were isolated from a A FIXII 129 SVJ mouse genomic library, and the complete nucleotide sequence of the gene was determined. The murine TFPI-2 gene spans approximately 9.3 kilobases and consists of five exons and four introns. The nucleotide sequences surrounding all the exon-intron boundaries are highly conserved and obey the GT-AG rule. Each Kunitz-type domain is encoded by a single exon, similar to that observed for other Kunitz-type proteinase inhibitors. A total of 1,577 bp of the 3’-flanking region contains a probable polyadenylation site (ATTAAA) at +5,759 and an apparent cleavage or termination site (CATTG) at +6,170. The 5’-flanking region of the murine TFPI-2 gene contains a prototypical TATA box, a GC box and two CAAT boxes. In addition, several candidate transcription factor binding sites responsible for placenta-, endothelial cell-, and smooth muscle cell-specific expression of the TFPI-2 gene were also identified.
    Keywords Tissue factor pathway inhibitor-2 ; Kunitz-type proteinase inhibitor ; gene ; mouse
    Language English
    Publishing date 2000-01-01
    Publisher Schattauer GmbH
    Publishing place Stuttgart ; New York
    Document type Article
    ZDB-ID 518294-3
    ISSN 2567-689X ; 0340-6245
    ISSN (online) 2567-689X
    ISSN 0340-6245
    DOI 10.1055/s-0037-1613770
    Database Thieme publisher's database

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  4. Article: Expression of the granzyme B inhibitor, protease inhibitor 9, by tumor cells in patients with non-Hodgkin and Hodgkin lymphoma: a novel protective mechanism for tumor cells to circumvent the immune system?

    Bladergroen, Bellinda A / Meijer, Chris J L M / ten Berge, Rosita L / Hack, C Erik / Muris, Jettie J F / Dukers, Danny F / Chott, Andreas / Kazama, Yoshiaki / Oudejans, Joost J / van Berkum, Oskar / Kummer, J Alain

    Blood

    2002  Volume 99, Issue 1, Page(s) 232–237

    Abstract: In tumor cells, the serine protease granzyme B is the primary mediator of apoptosis induced by cytotoxic T lymphocytes (CTLs)/natural killer (NK) cells. The human intracellular serpin proteinase inhibitor 9 (PI9) is the only known human protein able to ... ...

    Abstract In tumor cells, the serine protease granzyme B is the primary mediator of apoptosis induced by cytotoxic T lymphocytes (CTLs)/natural killer (NK) cells. The human intracellular serpin proteinase inhibitor 9 (PI9) is the only known human protein able to inhibit the proteolytic activity of granzyme B. When present in the cytoplasm of T lymphocytes, PI9 is thought to protect CTLs against apoptosis induced by their own misdirected granzyme B. Based on the speculation that tumors may also express PI9 to escape CTL/NK cell surveillance, immunohistochemical studies on the expression of PI9 in various lymphomas were performed. Ninety-two cases of T-cell non-Hodgkin lymphoma (NHL), 75 cases of B-cell NHL, and 57 cases of Hodgkin lymphomas were stained with a PI9-specific monoclonal antibody. In T-cell NHL, highest PI9 expression was found in the extranodal T-cell NHL. In nearly 90% of enteropathy-type T-cell NHLs and 80% of NK/T-cell, nasal-type lymphomas, the majority of the tumor cells expressed PI9. In nodal T-anaplastic large cell lymphomas and peripheral T-cell lymphomas (not otherwise specified), PI9 expression occurred less frequently. In B-cell NHL, PI9 expression was associated with high-grade malignancy; 43% of diffuse large B-cell lymphomas showed PI9(+) tumor cells. Finally, PI9 expression was also found in 10% of Hodgkin lymphomas. This is the first report describing the expression of the granzyme B inhibitor PI9 in human neoplastic cells in vivo. Expression of this inhibitor is yet another mechanism used by tumor cells to escape their elimination by cytotoxic lymphocytes.
    MeSH term(s) Antibodies, Monoclonal ; Apoptosis ; Granzymes ; Histocytochemistry ; Hodgkin Disease/immunology ; Hodgkin Disease/metabolism ; Humans ; Immunohistochemistry ; Killer Cells, Natural/immunology ; Lymphoma, B-Cell/immunology ; Lymphoma, B-Cell/metabolism ; Lymphoma, Non-Hodgkin/immunology ; Lymphoma, Non-Hodgkin/metabolism ; Lymphoma, T-Cell/immunology ; Lymphoma, T-Cell/metabolism ; Serine Endopeptidases/metabolism ; Serpins/analysis ; T-Lymphocytes, Cytotoxic/enzymology ; T-Lymphocytes, Cytotoxic/immunology ; T-Lymphocytes, Cytotoxic/pathology
    Chemical Substances Antibodies, Monoclonal ; SERPINB9 protein, human ; Serpins ; GZMB protein, human (EC 3.4.21.-) ; Granzymes (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-)
    Language English
    Publishing date 2002-01-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood.v99.1.232
    Database MEDical Literature Analysis and Retrieval System OnLINE

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