Platelet transmembrane signalling responses to collagen in familial hypercholesterolaemia

Cooper, Marie; Tan, K. C. B.; Betteridge, D. J.

doi:10.1111/j.1365-2362.1994.tb01070.x

Cited by 11 publications

(3 citation statements)

References 46 publications

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“…Briefly, platelet rich plasma was adjusted to a pH of 6·5 – to prevent fibrinogen binding to its receptor on platelets GPIIbIIIa – and co‐incubated with two units of apyrase per millilitre to prevent low‐level ADP‐stimulation during preparation. Platelets were pelleted and washed twice with an EGTA‐containing HEPES‐buffer (Cooper et al , 1994) supplemented with apyrase. Platelets were finally resuspended in HEPES‐buffer lacking EGTA and apyrase.…”

Section: Aggregatory Effects Of Vwf‐a1‐domain Expressing Cos‐7‐cells mentioning

confidence: 99%

Impact of O‐linked glycosylation of the VWF‐A1‐domain flanking regions on platelet interaction

et al. 2004

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This study investigated the functional impact of O-linked glycosylation of von Willebrand Factor (VWF) A1 domains on the interaction with platelet receptors. Native or mutant VWF-A1-domains were transiently overexpressed on COS-7 cells as membrane glycosylphosphatidylinositol (GPI)-anchored FLAG-tagged fusion proteins. Cytofluometric analysis assured comparable levels of A1-domain expression among native and mutant homologues as well as for different culture conditions. Expressing native VWF-A1-domains under O-linked glycosylation blocking conditions increased the platelet aggregatory responses observed for fully glycosylated forms. Utilizing a neuronal network for prediction of O-linked glycosylation of mammalian proteins, threonine (T) and serine (S) residues located in the VWF-A1-loop flanking regions - not in the loop itself - were determined to be glycosylated n-terminal at amino acids T485, S490, T492 and T493 and c-terminal at T705. Simultaneous selective charge-to-alanine mutation of S490, T492 and T493 led to gain in aggregatory responses. When compared with native forms, equivalent alterations of T485 did not dictate functional differences. Any alanine-substitution for T705 revealed a substantial loss in aggregatory effects - possibly as a result of structural desintegration of the VWF-A1-binding site for glycoprotein (GP) Ib. These data suggest specific O-linked glycosylation of the amino-terminal VWF-A1-loop-flanking region to have a negative regulatory impact on the A1-domain affinity of non-activated human VWF for human platelet-GPIb.

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Section: Aggregatory Effects Of Vwf‐a1‐domain Expressing Cos‐7‐cells mentioning

confidence: 99%

Impact of O‐linked glycosylation of the VWF‐A1‐domain flanking regions on platelet interaction

et al. 2004

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“…The involvement of platelet-LDL interactions herein is illustrated by observations in FH patients whose platelets are hyperreactive. This is demonstrated by increased ␣ -granule secretion [2,7] , increased superoxide anion production [8] , increased fi brinogen binding [9] and platelet aggregation [2,7,10] after stimulation. In addition, platelets have been found in the circulation of FH patients [11,12] and animals [13] in an activated state.…”

Section: The Interaction Of Platelets With Ldlmentioning

confidence: 99%

Platelet Activation by Low Density Lipoprotein and High Density Lipoprotein

Korporaal

Akkerman²

2006

Pathophysiol Haemos Thromb

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Cardiovascular disease is the main cause of death and disability in the Western society. Lipoproteins are important in the development of cardiovascular disease since they change the properties of different cells involved in atherosclerosis and thrombosis. The interaction of platelets with lipoproteins has been under intense investigation. Particularly the initiation of platelet signaling pathways by low density lipoprotein (LDL) has been studied thoroughly, since platelets of hypercholesterolemic patients, whose plasma contains elevated LDL levels due to absent or defective LDL receptors, show hyperaggregability in vitro and enhanced activity in vivo. These observations suggest that LDL enhances platelet responsiveness. Several signaling pathways induced by LDL have been revealed in vitro, such as signaling via p38 mitogen-activated protein kinase and p125 focal adhesion kinase. High density lipoprotein (HDL) consists of two subtypes, HDL₂ and HDL₃, which have opposing effects on platelet activation. This review provides a summary of the activation of signaling pathways after platelet-LDL and platelet-HDL interaction, with special emphasis on their role in the development of thrombosis and atherosclerosis.

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“…Blood was anticoagulated with ACD and processed within 1 hour of collection. Washed platelets were separated from platelet rich plasma as previously described [25] and platelet count was adjusted to 200×10 9 l -1 by suspending in HEPES buffered saline (HBS), containing NaCl (140 mM), KCl (2.7 mM), Glucose (5mM), BSA (1mg/ml), CaCl 2 (1mM), MgCl 2 (1 mM) and HEPES (10 mM) (pH 7.3).…”

Section: Preparation Of Washed Plateletsmentioning

confidence: 99%

Interactions between cell surface protein disulphide isomerase and S-nitrosoglutathione during nitric oxide delivery

et al. 2007

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This is an electronic version of an article published in Nitric Oxide, 16 (1). pp. 135-142., February 2007. The definitive publisher-authenticated version is available from the journal homepage at:http://www.sciencedirect.com/science/journal/10898603The WestminsterResearch online digital archive at the University of Westminster aims to make the research output of the University available to a wider audience. Copyright and Moral Rights remain with the authors and/or copyright owners. Users are permitted to download and/or print one copy for non-commercial private study or research. Further distribution and any use of material from within this archive for profit-making enterprises or for commercial gain is strictly forbidden.Whilst further distribution of specific materials from within this archive is forbidden, you may freely distribute the URL of WestminsterResearch.(http://www.wmin.ac.uk/westminsterresearch).In case of abuse or copyright appearing without permission e-mail wattsn@wmin.ac.uk. 1 INTERACTIONS BETWEEN CELL SURFACE PROTEIN DISULPHIDE ISOMERASE AND S-NITROSOGLUTATHIONE DURING NITRIC OXIDE DELIVERY AbstractIn this study, we investigated the role of protein disulphide isomerase (PDI) in rapid metabolism of S-nitrosoglutathione (GSNO) and S-nitrosoalbumin (albSNO) and in NO delivery from these compounds into cells. Incubation of GSNO or albSNO (1 μM) with the megakaryocyte cell line MEG-01 resulted in a cell-mediated removal of each compound which was inhibited by blocking cell surface thiols with 5, 5'-dithiobis 2-nitrobenzoic acid (DTNB) (100 μM) or inhibiting PDI with bacitracin (5 mM). GSNO, but not albSNO, rapidly inhibited platelet aggregation and stimulated cyclic GMP (cGMP) accumulation (used as a measure of intracellular NO entry). cGMP accumulation in response to GSNO (1 μM) was inhibited by MEG-01 treatment with bacitracin or DTNB, suggesting a role for PDI and surface thiols in NO delivery. PDI activity was present in MEG-01 conditioned medium, and was inhibited by high concentrations of GSNO (500 μM). A number of cell surface thiol-containing proteins were labelled using the impermeable thiol specific probe 3-(N-maleimido-propionyl) biocytin (MPB). Pretreatment of cells with GSNO resulted in a loss of thiol reactivity on some but not all proteins, suggesting selective cell surface thiol modification.Immunoprecipitation experiments showed that GSNO caused a concentrationdependent loss of thiol reactivity of PDI. Our data indicate that PDI is involved in both rapid metabolism of GSNO and intracellular NO delivery and that during this process PDI is itself altered by thiol modification. In contrast, the relevance of PDI-mediated albSNO metabolism to NO signalling is uncertain.3

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Platelet transmembrane signalling responses to collagen in familial hypercholesterolaemia

Cited by 11 publications

References 46 publications

Impact of O‐linked glycosylation of the VWF‐A1‐domain flanking regions on platelet interaction

Impact of O‐linked glycosylation of the VWF‐A1‐domain flanking regions on platelet interaction

Platelet Activation by Low Density Lipoprotein and High Density Lipoprotein

Interactions between cell surface protein disulphide isomerase and S-nitrosoglutathione during nitric oxide delivery

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