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  1. Article: Peptide Antagonists for P-selectin Discriminate between Sulfatide-Dependent Platelet Aggregation and PSGL-1-Mediated Cell Adhesion.

    Korporaal, Suzanne J A / Molenaar, Tom J M / Lutters, Bianca C H / Meurs, Illiana / Drost-Verhoef, Sandra / Kuiper, Johan / van Berkel, Theo J C / Biessen, Erik A L

    Journal of clinical medicine

    2019  Volume 8, Issue 8

    Abstract: Background: Membrane-exposed sulfatides are proposed to contribute to P-selectin-dependent platelet aggregation. Here, we demonstrated that P-selectin-mediated platelet aggregation on a collagen-coated surface under flow indeed depended on sulfatides ... ...

    Abstract Background: Membrane-exposed sulfatides are proposed to contribute to P-selectin-dependent platelet aggregation. Here, we demonstrated that P-selectin-mediated platelet aggregation on a collagen-coated surface under flow indeed depended on sulfatides and that this interaction differed considerably from the interaction of P-selectin with P-selectin Glycoprotein Ligand-1 (PSGL-1), which underlies leukocyte-endothelium adhesion.
    Methods and results: Upon platelet activation, sulfatides were translocated to the platelet surface to form focal hot-spots. Interestingly, P-selectin was observed to exclusively interact with liposomes with a sulfatide density higher than 21% (
    Conclusions: Our data suggest that the sulfatide/P-selectin interaction implicates multiple binding pockets, which only partly overlap with that of PSGL-1. These observations open ways to selectively interfere with sulfatide/P-selectin-dependent platelet aggregation without affecting PSGL-1-dependent cell adhesion.
    Language English
    Publishing date 2019-08-20
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2662592-1
    ISSN 2077-0383
    ISSN 2077-0383
    DOI 10.3390/jcm8081266
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: beta 2 Glycoprotein I--a key player in the antiphospholipid syndrome.

    Lutters, Bianca C H / de Groot, Philip G / Derksen, Ronald H W M

    The Israel Medical Association journal : IMAJ

    2002  Volume 4, Issue 11 Suppl, Page(s) 958–962

    MeSH term(s) Animals ; Antibodies, Anticardiolipin/immunology ; Antibodies, Antiphospholipid/immunology ; Antigen-Antibody Complex/immunology ; Antigen-Antibody Reactions/immunology ; Antiphospholipid Syndrome/complications ; Antiphospholipid Syndrome/immunology ; Disease Models, Animal ; Glycoproteins/chemistry ; Glycoproteins/immunology ; Humans ; Lupus Coagulation Inhibitor/immunology ; Mice ; Mice, Knockout ; Protein Structure, Tertiary/physiology ; Receptors, Fc/immunology ; Thrombosis/etiology ; beta 2-Glycoprotein I ; src Homology Domains/immunology
    Chemical Substances Antibodies, Anticardiolipin ; Antibodies, Antiphospholipid ; Antigen-Antibody Complex ; Glycoproteins ; Lupus Coagulation Inhibitor ; Receptors, Fc ; beta 2-Glycoprotein I
    Language English
    Publishing date 2002-11
    Publishing country Israel
    Document type Journal Article ; Review
    ZDB-ID 2008291-5
    ISSN 1565-1088 ; 0021-2180
    ISSN 1565-1088 ; 0021-2180
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5470: Show issues Location:
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  3. Article ; Online: Gallic acid antagonizes P-selectin-mediated platelet-leukocyte interactions: implications for the French paradox.

    Appeldoorn, Chantal C M / Bonnefoy, Arnaud / Lutters, Bianca C H / Daenens, Kim / van Berkel, Theo J C / Hoylaerts, Marc F / Biessen, Erik A L

    Circulation

    2005  Volume 111, Issue 1, Page(s) 106–112

    Abstract: ... by online video microscopy (ED50, 1.7+/-0.3 and 1.5+/-0.4 mg x kg(-1) x h(-1), respectively).: Conclusions ...

    Abstract Background: Current paradigm attributes the low incidence of cardiovascular disorders in Mediterranean countries despite a high saturated fat intake, the "French paradox," to the antioxidant capacity of red wine polyphenols. Conceivably, other antiinflammatory pathways may contribute to at least a similar extent to the atheroprotective activity of these polyphenols. We have investigated whether gallic acid (GA), an abundant red wine polyphenol, modulates the activity of P-selectin, an adhesion molecule that is critically involved in the recruitment of inflammatory cells to the vessel wall and thus in atherosclerosis.
    Methods and results: GA potently inhibited the binding of a peptide antagonist (IC50, 7.2 micromol/L) and biotin-PAA-Le(a)-SO3H, an established high-affinity ligand, to P-selectin (IC50, 85 micromol/L). Under dynamic flow conditions, GA markedly and dose dependently attenuated the rolling of monocytic HL60 cells over P-selectin-transfected Chinese hamster ovary cells (EC50, 14.5 micromol/L) while increasing the velocity of P-selectin-dependent rolling of human blood leukocytes over a platelet monolayer. In vivo tests established that GA administration to normolipidemic C57/Bl6 and aged atherosclerotic apolipoprotein E-deficient mice impaired the baseline rolling of conjugates between activated platelets and circulating monocytes over femoral vein endothelium, as judged by online video microscopy (ED50, 1.7+/-0.3 and 1.5+/-0.4 mg x kg(-1) x h(-1), respectively).
    Conclusions: Our findings provide a solid mechanistic foundation through which GA intervenes in major inflammatory pathobiologies by binding and antagonizing P-selectin.
    MeSH term(s) Acrylamides/pharmacology ; Amino Acid Sequence ; Animals ; Antioxidants/pharmacology ; Apolipoproteins E/deficiency ; Apolipoproteins E/genetics ; Binding, Competitive ; Biotin/analogs & derivatives ; Biotin/pharmacology ; Blood Platelets/cytology ; Blood Platelets/drug effects ; CHO Cells/drug effects ; Calcium/metabolism ; Carrier Proteins/pharmacology ; Cell Adhesion/drug effects ; Chemotaxis, Leukocyte/drug effects ; Collagen/pharmacology ; Cricetinae ; Cricetulus ; Diet, Atherogenic ; Endothelial Cells/cytology ; Endothelial Cells/drug effects ; Endothelium, Vascular/cytology ; Femoral Vein/pathology ; Gallic Acid/pharmacology ; HL-60 Cells/drug effects ; Humans ; Hyperlipoproteinemia Type II/blood ; Inhibitory Concentration 50 ; Ion Transport ; Leukocytes/cytology ; Leukocytes/drug effects ; Mice ; Mice, Inbred C57BL ; Microscopy, Video ; Molecular Sequence Data ; P-Selectin/drug effects ; Peptides ; Platelet Adhesiveness/drug effects ; Wine/analysis
    Chemical Substances Acrylamides ; Antioxidants ; Apolipoproteins E ; Carrier Proteins ; P-Selectin ; Peptides ; TM11 peptide ; biotinylated sulfo-Lewis A derivatized polyacrylamide ; Gallic Acid (632XD903SP) ; Biotin (6SO6U10H04) ; Collagen (9007-34-5) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2005-01-04
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80099-5
    ISSN 1524-4539 ; 0009-7322 ; 0069-4193 ; 0065-8499
    ISSN (online) 1524-4539
    ISSN 0009-7322 ; 0069-4193 ; 0065-8499
    DOI 10.1161/01.CIR.0000151307.10576.02
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Ui IV Zs.60: Show issues Location:
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  4. Article: Blocking endothelial adhesion molecules: a potential therapeutic strategy to combat atherogenesis.

    Lutters, Bianca C H / Leeuwenburgh, Michiel A / Appeldoorn, Chantal C M / Molenaar, Tom J M / Van Berkel, Theo J C / Biessen, Erik A L

    Current opinion in lipidology

    2003  Volume 15, Issue 5, Page(s) 545–552

    Abstract: Purpose of review: This review provides a concise update of the involvement of endothelial adhesion molecules in atherogenesis, an overview of current advances in the development of adhesion molecule blocking agents, as well as an insight into the ... ...

    Abstract Purpose of review: This review provides a concise update of the involvement of endothelial adhesion molecules in atherogenesis, an overview of current advances in the development of adhesion molecule blocking agents, as well as an insight into the potential of these molecules in cardiovascular therapy.
    Recent findings: As endothelial adhesion molecules are deemed to play an important role in the development and progression of atherosclerotic lesions, they are interesting targets for therapeutic intervention in this process. In particular, P-selectin and vascular cell adhesion molecule 1 are widely considered to hold promise in this regard. Current research efforts centre on the design of agents that directly block the interaction of the receptor with its ligand (e.g. soluble P-selectin glycoprotein ligand 1, blocking antibodies, EWVD-based peptides) or that interfere with their synthesis (e.g. antisense oligonucleotides) or their regulatory control by nuclear factor kappa B or peroxisome proliferator-activated receptor gamma. Furthermore, adhesion molecules have been exploited as a target for the specific delivery of drug carriers (e.g. biodegradable particles with entrapped dexamethasone) or therapeutic compounds (e.g. dexamethasone) to the plaque. All approaches have been shown to be effective in blocking adhesion molecule function in in-vitro studies and in-vivo models for inflammation or atherosclerosis.
    Summary: Although the field has achieved considerable progress in recent years, leading to the development of a number of interesting leads, final proof of their efficacy in cardiovascular therapy is eagerly awaited.
    MeSH term(s) Animals ; Arteriosclerosis/pathology ; Arteriosclerosis/therapy ; Cell Adhesion ; Endothelium, Vascular/pathology ; Humans ; Immunoglobulins/metabolism ; Integrins/metabolism ; Leukocytes/metabolism ; Selectins
    Chemical Substances Immunoglobulins ; Integrins ; Selectins
    Language English
    Publishing date 2003-07-15
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1045394-5
    ISSN 1473-6535 ; 0957-9672
    ISSN (online) 1473-6535
    ISSN 0957-9672
    DOI 10.1097/00041433-200410000-00008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 3010: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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    Jg. 1995 - 2021: Lesesall (2.OG)
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  5. Article: Dimers of beta 2-glycoprotein I increase platelet deposition to collagen via interaction with phospholipids and the apolipoprotein E receptor 2'.

    Lutters, Bianca C H / Derksen, Ronald H W M / Tekelenburg, Winnie L / Lenting, Peter J / Arnout, Jef / de Groot, Philip G

    The Journal of biological chemistry

    2003  Volume 278, Issue 36, Page(s) 33831–33838

    Abstract: Patients with prolonged clotting times caused by lupus anticoagulant (LAC) are at risk for thrombosis. This paradoxal association is not understood. LAC is frequently caused by anti-beta2-glycoprotein I (beta 2GPI) antibodies. Antibody-induced ... ...

    Abstract Patients with prolonged clotting times caused by lupus anticoagulant (LAC) are at risk for thrombosis. This paradoxal association is not understood. LAC is frequently caused by anti-beta2-glycoprotein I (beta 2GPI) antibodies. Antibody-induced dimerization of beta 2GPI increases the affinity of beta 2GPI for phospholipids, explaining the observed prolonged clotting times. We constructed dimers of beta 2GPI that mimic effects of beta 2GPI-anti-beta 2GPI antibody complexes, and we studied their effects on platelet adhesion and thrombus formation in a flow system. Dimeric beta 2GPI increased platelet adhesion to collagen by 150% and increased the number of large aggregates. We also observed increased platelet adhesion to collagen when whole blood was spiked with patient-derived polyclonal anti-beta 2GPI or some, but not all, monoclonal anti-beta 2GPI antibodies with LAC activity. These effects could be abrogated by inhibition of thromboxane synthesis. A LAC-positive monoclonal anti-beta 2GPI antibody, which did not affect platelet adhesion, prevented the induced increase in platelet adhesion by beta 2GPI dimers. Furthermore, increased platelet adhesion disappeared after preincubation with receptor-associated protein, a universal inhibitor of interaction of ligands with members of the low density lipoprotein receptor family. Using co-immunoprecipitation, it was shown that dimeric beta 2GPI can interact with apolipoprotein E receptor 2 (apoER2'), a member of the low density lipoprotein receptor family present on platelets. These results demonstrate that dimeric beta 2GPI induces increased platelet adhesion and thrombus formation, which depends on activation via apoER2'.
    MeSH term(s) Antibodies, Monoclonal/chemistry ; Antiphospholipid Syndrome/immunology ; Blood Platelets/metabolism ; Cell Adhesion/drug effects ; Collagen/chemistry ; Collagen/metabolism ; Dimerization ; Female ; Fibrinogen/chemistry ; Fibronectins/chemistry ; Fibronectins/metabolism ; Glycoproteins/chemistry ; Humans ; LDL-Receptor Related Proteins ; Ligands ; Microscopy, Fluorescence ; Perfusion ; Phospholipids/chemistry ; Platelet Aggregation ; Precipitin Tests ; Protein Binding ; Receptors, LDL/metabolism ; Receptors, Lipoprotein/chemistry ; Receptors, Lipoprotein/metabolism ; Signal Transduction ; Thromboxanes/antagonists & inhibitors ; Transfection ; beta 2-Glycoprotein I
    Chemical Substances Antibodies, Monoclonal ; Fibronectins ; Glycoproteins ; LDL-Receptor Related Proteins ; Ligands ; Phospholipids ; Receptors, LDL ; Receptors, Lipoprotein ; Thromboxanes ; beta 2-Glycoprotein I ; low density lipoprotein receptor-related protein 8 ; Fibrinogen (9001-32-5) ; Collagen (9007-34-5)
    Language English
    Publishing date 2003-06-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M212655200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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  6. Article: The binding site in {beta}2-glycoprotein I for ApoER2' on platelets is located in domain V.

    van Lummel, Menno / Pennings, Maarten T T / Derksen, Ronald H W M / Urbanus, Rolf T / Lutters, Bianca C H / Kaldenhoven, Niels / de Groot, Philip G

    The Journal of biological chemistry

    2005  Volume 280, Issue 44, Page(s) 36729–36736

    Abstract: The antiphospholipid syndrome is caused by autoantibodies directed against beta(2)-glycoprotein I (beta(2)GPI). Dimerization of beta(2)GPI results in an increased platelet deposition to collagen. We found that apolipoprotein E receptor 2' (apoER2'), a ... ...

    Abstract The antiphospholipid syndrome is caused by autoantibodies directed against beta(2)-glycoprotein I (beta(2)GPI). Dimerization of beta(2)GPI results in an increased platelet deposition to collagen. We found that apolipoprotein E receptor 2' (apoER2'), a member of the low density lipoprotein receptor family, is involved in activation of platelets by dimeric beta(2)GPI. To identify which domain of dimeric beta(2)GPI interacts with apoER2', we have constructed domain deletion mutants of dimeric beta(2)GPI, lacking domain I (DeltaI), II (DeltaII), or V (DeltaV), and a mutant with a W316S substitution in the phospholipid (PL)-insertion loop of domain V. DeltaI and DeltaII prolonged the clotting time, as did full-length dimeric beta(2)GPI; DeltaV had no effect on the clotting time. Second, DeltaI and DeltaII bound to anionic PL, comparable with full-length dimeric beta(2)GPI. DeltaV and the W316S mutant bound with decreased affinity to anionic PL. Platelet adhesion to collagen increased significantly when full-length dimeric beta(2)GPI, DeltaI, or DeltaII (mean increase 150%) were added to whole blood. No increase was found with plasma beta(2)GPI, DeltaV, or the W316S mutant. Immunoprecipitation indicated that full-length dimeric beta(2)GPI, DeltaI, DeltaII, and the W316S mutant can interact with apoER2' on platelets. DeltaV did not associate with apoER2'. We conclude that domain V is involved in both binding beta(2)GPI to anionic PL and in interaction with apoER2' and subsequent activation of platelets. The binding site in beta(2)GPI for interaction with apoER2' does not overlap with the hydrophobic insertion loop in domain V.
    MeSH term(s) Amino Acid Substitution ; Animals ; Binding Sites ; Blood Coagulation ; Blood Platelets/metabolism ; Cells, Cultured ; Collagen/metabolism ; Cricetinae ; Dimerization ; Glycoproteins/genetics ; Glycoproteins/isolation & purification ; Glycoproteins/metabolism ; Humans ; Immunoprecipitation ; Kidney/cytology ; Kidney/metabolism ; LDL-Receptor Related Proteins ; Megakaryocytes/cytology ; Megakaryocytes/metabolism ; Peptide Fragments/pharmacology ; Phospholipids/metabolism ; Plasmids ; Platelet Activation ; Protein Structure, Tertiary ; Receptors, Lipoprotein/genetics ; Receptors, Lipoprotein/isolation & purification ; Receptors, Lipoprotein/metabolism ; Sequence Deletion ; Umbilical Cord/cytology ; Umbilical Cord/metabolism ; beta 2-Glycoprotein I
    Chemical Substances Glycoproteins ; LDL-Receptor Related Proteins ; Peptide Fragments ; Phospholipids ; Receptors, Lipoprotein ; beta 2-Glycoprotein I ; low density lipoprotein receptor-related protein 8 ; Collagen (9007-34-5)
    Language English
    Publishing date 2005-08-09
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M504172200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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