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  • 1.
    Centellas, Daniel Sanchez
    et al.
    Linköping University, Linköping, Sweden.
    Gudlur, Sushanth
    Linköping University, Linköping, Sweden; Nanyang Technology University, Singapore, Singapore..
    Vicente-Carrillo, Alejandro
    Linköping University, Linköping, Sweden.
    Ramström, Sofia
    Linköping University, Linköping, Sweden.
    Lindahl, Tomas L.
    Linköping University, Linköping, Sweden.
    A cluster of aspartic residues in the extracellular loop II of PAR 4 is important for thrombin interaction and activation of platelets2017In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 154, p. 84-92Article in journal (Refereed)
    Abstract [en]

    Thrombin activates platelets via proteolytic cleavage of protease-activated receptors (PARs) 1 and 4. The two PARs have distinct but complementary roles. The mechanisms responsible for PAR1 activation by thrombin have been extensively studied. However, much less is known regarding thrombin activation of PAR4, especially the potential involvement of regions of PAR4 other than the N-terminal, which is bound to the catalytic site of thrombin. We have studied PAR4 in S. cerevisiae strainMMY12, an expression system in which the GPCR receptors are connected to a Lac Z reporter gene resulting in increased beta-galactosidase activity. This approach was used to assess PAR4 mutants to evaluate the contribution of different aspartic residues in facilitating PAR4 activation. Furthermore, peptides mimicking parts of the PAR4 N-terminal and the second extracellular loop (ECLII) were tested for their ability to inhibit platelet activation by thrombin. Binding of these peptides to gamma-thrombin was studied by monitoring the decrease in tryptophan fluorescence intensity of thrombin. We conclude that not only the N-terminal but also the electronegative aspartic residues D224, D230 and D235 (located in ECLII) are be important for PAR4 binding to thrombin. We further suggest that they play a role for the tethered ligand binding to the receptor, as mutations also affected activation in response to a PAR4-activating peptide mimicking the new N-terminal formed after cleavage. This agrees with previous results on PAR1 and thrombin binding. We suggest that the ECLII of PAR4 could be a potential target for antithrombotic drug development.

  • 2.
    Deb, S.
    et al.
    Linköping University, Linköping, Sweden.
    Sjöström, C.
    Linköping University, Linköping, Sweden.
    Tharmakulanathan, A.
    Linköping University, Linköping, Sweden.
    Boknäs, N.
    Linköping University, Linköping, Sweden.
    Lotfi, K.
    Linköping University, Linköping, Sweden.
    Ramström, Sofia
    Linköping University, Linköping, Sweden.
    Individual variation in hemostatic alterations caused by tyrosine kinase inhibitors: a way to improve personalized cancer therapy?2016In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 140, no Suppl. 1, p. S196-S197, article id PO-55Article in journal (Refereed)
    Abstract [en]

    INTRODUCTION: During the last two decades, Bcr-Abl tyrosine kinase inhibitors (TKIs) have revolutionized the treatment of chronic myelogenous leukemia (CML), and are now considered standard treatment for this disease. However, TKIs can induce serious hemostatic side effects including cardiovascular disease and bleeding disorders. Blood platelet aggregation and formation of pro-coagulant platelets are important to allow a well-balanced hemostatic response. Therefore, a detailed understanding of what effect different TKIs exert on platelets and hemostasis could help to understand if there are differences of importance to minimize the risk of bleeding complications in treated patients.

    AIM: To investigate how TKIs used in CML (imatinib, dasatinib, nilotinib, bosutinib, and ponatinib) affect platelet activation and hemostasis.

    MATERIALS AND METHODS: We have developed a multi-parameter six color flow cytometry protocol to study different aspects of platelet function upon activation, e.g. formation of aggregatory (PAC-1-positive) and pro-coagulant (phosphatidylserine-exposing) platelets, exocytosis of alpha- and lysosomal granules and mitochondrial membrane potential.This protocol was performed in presence or absence of TKIs in blood from normal donors and in treated patients. Whole blood aggregometry (Multiplate®), thrombin generation in platelet-rich plasma and in vitro thrombus formation by free oscillation rheometry (ReoRox G2) was further evaluated in some situations.

    RESULTS: At clinically relevant concentrations, dasatinib significantly decreased the formation of procoagulant platelets. Ponatinib induced a slight decrease in formation of procoagulant platelets, whereas bosutinib and nilotinib showed opposite tendencies (n=7). Dasatinib also decreased platelet aggregation (n=4-6) and in vitro thrombus formation (n=3). Thrombin generation was not significantly affected by therapeutic levels of TKIs, whereas higher doses of dasatinib, bosutinib, ponatinib and imatinib significantly changed one or several of the thrombin generation parameters (n=7-8). Interestingly, large differences in response to the drugs were observed among the healthy donors, especially for dasatinib and bosutinib. Major inter-individual variations were also observed in dasatinib-treated patients, see Figure 1.

    CONCLUSIONS: Different TKIs show varying potency to affect platelet-based hemostasis. In addition, we found large inter-individual variations in how some drugs affected platelet function. Therefore, we suggest that development of a clinically useful protocol for platelet function testing could help to identify patients more susceptible to adverse drug reactions. Such a protocol could potentially help clinicians to gain insight into the risk of side effects, which could help to choose the most suitable drug for each individual patient.

  • 3. Eriksson, Maria
    et al.
    Johnson, Owe
    Boman, Kurt
    Hallmans, Göran
    Hellsten, Gideon
    Nilsson, Torbjörn K
    Örebro University, School of Health and Medical Sciences.
    Söderberg, Stefan
    Improved fibrinolytic activity during exercise may be an effect of the adipocyte-derived hormones leptin and adiponectin2008In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 122, no 5, p. 701-708Article in journal (Refereed)
    Abstract [en]

    INTRODUCTION: Physical activity is associated with improved fibrinolytic activity and reduced risk for cardiovascular disease. High levels of leptin and low levels of adiponectin, both adipocyte-derived hormones, or adipokines, are related to dysfibrinolysis and risk for cardiovascular disease. In this study, we explored if improved fibrinolytic activity during exercise could be linked to changes in leptin and adiponectin levels.

    MATERIALS AND METHODS: Twenty healthy men (mean age 36 years) participated in a 14-day long skiing expedition in the Swedish mountains. They were randomly assigned to either a 40% or a 30% fat-based diet. Anthropometry, lipids, fibrinolytic activity (PAI-1 activity, tPA activity and mass) and adipokines (leptin and adiponectin) were measured before, during and six weeks after the expedition.

    RESULTS: PAI-1 activity and circulating levels of leptin decreased whereas levels of adiponectin increased during exercise. The fall in PAI-1 activity showed a strong linear association with changes in leptin and adiponectin levels (p = 0.001 and p < 0.001, respectively). Changes in leptin and adiponectin levels were independent of decreasing waist circumference. However, the association between anthropometric measures and adipokines changed considerably during the expedition. Adiponectin was weakly and negatively associated with BMI at baseline. In contrast, there was a strong positive association between adiponectin and BMI after two weeks of exercise, whereas the association between leptin and BMI became less pronounced. In addition, increasing leptin and decreasing adiponectin levels were associated with increasing PAI-1 activity during the six weeks following the expedition. After six weeks of normal activity, fibrinolytic activity and hormone levels returned towards baseline levels.

    CONCLUSION: Heavy exercise induced improved fibrinolytic activity, which was associated independently with changes in circulating levels of the adipocyte-derived hormones leptin and adiponectin. Improved fibrinolytic activity (and reduced risk for cardiovascular disease) related to physical activity could possibly be mediated by leptin and adiponectin. 

  • 4.
    Hagnelius, Nils-Olof
    et al.
    Örebro University, School of Health and Medical Sciences. Dept of Geriatrics, Örebro University Hospital, Örebro, Sweden.
    Boman, Kurt
    Dept Med, Skellefteå Cty Hosp, Skellefteå, Sweden.
    Nilsson, Torbjörn K.
    Örebro University, School of Health and Medical Sciences. Dept of Laboratory Medicine, Div of Clinical Chemistry, Örebro University Hospital, Örebro, Sweden.
    Fibrinolysis and von Willebrand factor in Alzheimer's disease and vascular dementia: a case-referent study2010In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 126, no 1, p. 35-38Article in journal (Refereed)
  • 5.
    Hernestal-Boman, Jenny
    et al.
    Dept Publ Hlth & Clin Med, Umeå Univ, Umeå, Sweden.
    Jansson, Jan-Hakan
    Dept Publ Hlth & Clin Med, Umeå Univ, Umeå, Sweden; Dept Med & Geriatr, Skellefteå Cty Hosp, Skellefteå, Sweden.
    Nilsson, Torbjörn K.
    Örebro University, School of Health and Medical Sciences. Örebro University Hospital, Örebro, Sweden.
    Eliasson, Mats
    Dept Publ Hlth & Clin Med, Umeå Univ, Umeå, Sweden; Dept Med, Sunderby Hosp, Luleå, Sweden.
    Johansson, Lars
    Dept Publ Hlth & Clin Med, Umeå Univ, Umeå, Sweden; Dept Med & Geriatr, Skellefteå Cty Hosp, Skellefteå, Sweden.
    Long-term stability of fibrinolytic factors stored at-80 degrees C2010In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 125, no 5, p. 451-456Article in journal (Refereed)
    Abstract [en]

    Introduction: Blood samples in epidemiological studies are often stored for several years and analysed at different occasions. The reagent kits are continually modified for better precision and accuracy. Our hypothesis was that epidemiological studies are affected by long-term storage and/or modifications of reagent kits. Materials and Methods: Plasma samples stored at -80 degrees C from two populations were used: A case-referent study with samples collected from 1985 to 2000 and analysed 2005 (n=1598) were used to study influence of long-term storage. A cross-sectional study analysed 1990 (n=1558) and re-analysed 2001 (n=78) and 2005 (n=828) was used to study influence of reagent kit modifications. Fibrinolytic analyses included immunoassays of tPA, PAI-1 and tPA-PAI-1 complex and chromogenic substrate assays of the activities of tPA and PAI-1. Results: Long-term storage for a median time of 11.6 years (range 5 to 20) showed an effect of time on tPA antigen R-2=0.01, PAI-1 antigen R-2=0.01 and tPA-PAI-1 complex R-2=0.02. Modifications in reagent kits affected the levels of fibrinolytic factors; for tPA antigen the slope coefficients were between 0.72 and 0.95 (R-2 0.47-0.75), whereas tPA activity showed an agreement with slope coefficients 1.06 to 1.09 (R-2 0.67-0.93). Conclusions: This study showed that long-term storage affects fibrinolytic variables to a negligible extent, but modifications in reagent kits introduced an element of bias. We conclude that analysis of samples on a single occasion is preferable to multiple occasions, as storage has negligible effect. (C) 2009 Elsevier Ltd. All rights reserved.

  • 6.
    Lindkvist, Madelene
    et al.
    Örebro University, School of Medical Sciences.
    Fernberg, Ulrika
    Örebro University, School of Medical Sciences.
    Ljungberg, Liza
    Örebro University, School of Medical Sciences.
    Fälker, Knut
    Örebro University, School of Medical Sciences.
    Fernström, Maria
    Örebro University, School of Health Sciences.
    Hurtig-Wennlöf, Anita
    Örebro University, School of Health Sciences.
    Grenegård, Magnus
    Örebro University, School of Medical Sciences.
    Individual variations in platelet reactivity towards ADP, epinephrine, collagen and nitric oxide, and the association to arterial function in young, healthy adults2019In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 174, p. 5-12Article in journal (Refereed)
    Abstract [en]

    INTRODUCTION: Platelet aggregation and secretion can be induced by a large number of endogenous activators, such as collagen, adenosine diphosphate (ADP) and epinephrine. Conversely, the blood vessel endothelium constitutively release platelet inhibitors including nitric oxide (NO) and prostacyclin. NO and prostacyclin are also well-known vasodilators and contribute to alterations in local blood flow and systemic blood pressure.

    MATERIALS AND METHODS: In this study we investigated individual variations in platelet reactivity and arterial functions including blood pressure and flow-mediated vasodilation (FMD) in 43 young, healthy individuals participating in the Lifestyle, Biomarkers and Atherosclerosis (LBA) study. Platelet aggregation and dense granule secretion were measured simultaneously by light transmission and luminescence. FMD was measured with ultrasound.

    RESULTS: The platelet function assay showed inter-individual differences in platelet reactivity. Specifically, a sub-group of individuals had platelets with an increased response to low concentrations of ADP and epinephrine, but not collagen. When the NO-donor S-nitroso-N-acetyl-DL-penicillamine (SNAP) was combined with high doses of these platelet activators, the results indicated for sub-groups of NO-sensitive and NO-insensitive platelets. The individuals with NO-sensitive platelets in response to SNAP in combination with collagen had a higher capacity of FMD of the arteria brachialis.

    CONCLUSIONS: Platelet reactivity towards ADP, epinephrine and NO differs between young, healthy individuals. Some individuals have a more effective response towards NO, both in the aspect of platelet inhibition ex vivo, as well as vasodilation in vivo.

  • 7.
    Nylander, Martina
    et al.
    Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
    Osman, Abdimajid
    Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
    Ramström, Sofia
    Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
    Aklint, Emma
    Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
    Larsson, Anders
    Department of Medical Sciences, University Hospital, Uppsala, Sweden.
    Lindahl, Tomas L.
    Department of Clinical and Experimental Medicine, Linköping University, Linköping, Sweden.
    The role of thrombin receptors PAR1 and PAR4 for PAI-1 storage, synthesis and secretion by human platelets2012In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 129, no 4, p. E51-E58Article in journal (Refereed)
    Abstract [en]

    Introduction: Arterial thrombi contain more platelets than venous thrombi and are more resistant to fibrinolysis. This resistance could partly be due to plasminogen activator inhibitor 1 (PAI-1) secreted by platelets. The aim of this study was to elucidate differences between thrombin receptors protease-activated receptor (PAR) 1 and 4 and platelet storage, secretion and synthesis of platelet PAI-1, as compared to other platelet alpha-granule proteins such as VEGF and endostatin.

    Materials and methods: Human isolated platelets were incubated with thrombin (0.5 U/ml), PAR1-activating peptide (AP) (0.4-30 mu M) or PAR4-AP (1.5-300 mu M) for up to 24 hours. ELISA, western blot and fluorescence microscopy were used to measure secretion, contents and localization of PAI-1, VEGF and endostatin. Results: Our results show that PAI-1 and VEGF might be co-localized and that endostatin does not co-localize with either PAI-1 or VEGF. PAI-1 and VEGF show a similar secretion pattern, being more sensitive to low grade PAR1 activation, but secretion was also observed with higher concentrations of PAR4-APs. PAI-1 is secreted in an active form. PAI-1 mRNA was found in platelets, and elevated levels of PAI-1 were detected after 24 hours incubation of platelets.

    Conclusions: PAI-1 and VEGF, but not endostatin, might be stored in the same alpha-granule in human platelets. PAI-1 and VEGF also show a similar secretion pattern, being more sensitive to PAR1 than to PAR4 activation, but the secretion is not exclusively selective. Our results also show that platelet PAI-1 is increased if incubated for 24 hours, both with addition of PAR1-activating peptide and without activation, which could indicate de novo synthesis.

  • 8.
    Peng, Xiang
    et al.
    Department of Nephrology, Qingyuan City Hospital of Jinan University, Guangdong, China; Department of Medical and Health Sciences, Linköping University, Linköping, Sweden.
    Ramström, Sofia
    Department of Experimental and Clinical Medicine, Linköping University, Linköping, Sweden.
    Kurz, Tino
    Department of Medical and Health Sciences, Linköping University, Linköping, Sweden.
    Grenegård, Magnus
    Örebro University, School of Medicine, Örebro University, Sweden. Department of Medical and Health Sciences, Linköping University, Linköping, Sweden; .
    Segelmark, Mårten
    Department of Medical and Health Sciences, Linköping University, Linköping, Sweden.
    The neutrophil serine protease PR3 induces shape change of platelets via the Rho/Rho kinase and Ca2+ signaling pathways2014In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 134, no 2, p. 418-425Article in journal (Refereed)
    Abstract [en]

    Introduction: Proteinase 3 (PR3) is released from neutrophil azurophilic granules and exerts complex effects on the inflammatory process. PR3 catalyzes the degradation of a number of macromolecules, but the consequences on blood cells are less well defined. In the present study, the effect of PR3 on human platelets was thoroughly investigated.

    Methods: The experiments were performed on washed platelets freshly isolated from blood donated by healthy human volunteers. Platelets shape change and aggregation was measured on a Chrono-Log aggregometer. The phosphorylated form of MYPT1 was visualized by immunostaining. Platelet activation was further evaluated by flow cytometry.

    Results: PR3 induced platelet shape change but not aggregation. Flow cytometry analysis showed that PR3 induced no P-selectin expression or binding of fibrinogen to the platelets, and it did not change the activation in response to PAR1- or PAR4-activating peptides or to thrombin. Furthermore, Fura-2 measurement and immuno-blotting analysis, respectively, revealed that PR3 stimulated small intracellular Ca2+ mobilization and Thr696-specific phosphorylation of the myosin phosphatase target subunit 1 (MYPT1). Separate treatment of platelets with the Rho/Rho kinase inhibitor Y-27632 and the intracellular Ca2+ chelator BAPTA/AM reduced the shape change induced by PR3 whereas concurrent treatment completely inhibited it.

    Conclusion: The data shows that the neutrophil protease PR3 is a direct modulator of human platelets and causes shape change through activation of the Rho/Rho kinase and Ca2+ signaling pathways. This finding highlights an additional mechanism in the complex interplay between neutrophils and platelets.

  • 9.
    Walker, A. J.
    et al.
    Div Epidemiol & Publ Hlth, City Hosp Nottingham, Univ Nottingham, Nottingham, England; NIHR Biomed Res Unit, Nottingham Digest Dis Ctr, Nottingham, England .
    Grainge, M. J.
    Div Epidemiol & Publ Hlth, City Hosp Nottingham, Univ Nottingham, Nottingham, England; NIHR Biomed Res Unit, Nottingham Digest Dis Ctr, Nottingham, England .
    Card, T. R.
    Div Epidemiol & Publ Hlth, City Hosp Nottingham, Univ Nottingham, Nottingham, England; NIHR Biomed Res Unit, Nottingham Digest Dis Ctr, Nottingham, England .
    West, J.
    Div Epidemiol & Publ Hlth, City Hosp Nottingham, Univ Nottingham, Nottingham, England; NIHR Biomed Res Unit, Nottingham Digest Dis Ctr, Nottingham, England .
    Ranta, S.
    Childhood Canc Res Unit, Karolinska Inst, Stockholm, Sweden.
    Ludvigsson, Jonas F.
    Örebro University, School of Health and Medical Sciences, Örebro University, Sweden. Dept Med Epidemiol & Biostat, Karolinska Inst, Stockholm, Sweden; Dept Pediat, Örebro Univ Hosp, Univ Örebro, Örebro, Sweden.
    Venous thromboembolism in children with cancer: a population-based cohort study2014In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 133, p. S189-S189Article in journal (Other academic)
  • 10.
    Walker, Alex J.
    et al.
    Div Epidemiol & Publ Hlth, City Hosp Nottingham, Univ Nottingham, Nottingham, England; Nottingham Digestive Diseases Centre, National Institute for Health Research (NIHR) Biomed Res Unit, Nottingham, England.
    Grainge, Matthew J.
    Div Epidemiol & Publ Hlth, City Hosp Nottingham, Univ Nottingham, Nottingham, England; Nottingham Digestive Diseases Centre, National Institute for Health Research (NIHR) Biomed Res Unit, Nottingham, England.
    Card, Tim R.
    Div Epidemiol & Publ Hlth, City Hosp Nottingham, Univ Nottingham, Nottingham, England; Nottingham Digestive Diseases Centre, National Institute for Health Research (NIHR) Biomed Res Unit, Nottingham, England.
    West, Joe
    Div Epidemiol & Publ Hlth, City Hosp Nottingham, Univ Nottingham, Nottingham, England; Nottingham Digestive Diseases Centre, National Institute for Health Research (NIHR) Biomed Res Unit, Nottingham, England.
    Ranta, Susanna
    Childhood Canc Res Unit, Karolinska Inst, Stockholm, Sweden.
    Ludvigsson, Jonas F.
    Örebro University Hospital. Department of Medical Epidemiology and Biostatistics, Karolinska Institutet Sockholm, Sweden; Department of Pediatrics, Örebro University Hospital, Örebro University, Örebro, Sweden.
    Venous thromboembolism in children with cancer: A population-based cohort study2014In: Thrombosis Research, ISSN 0049-3848, E-ISSN 1879-2472, Vol. 133, no 3, p. 340-344Article in journal (Refereed)
    Abstract [en]

    Introduction: Cancer is a known risk factor for venous thromboembolism (VTE) in adults, but population-based data in children are scarce.

    Materials and methods: We conducted a cohort study utilising linkage of the Clinical Practice Research Database (primary care), Hospital Episodes Statistics (secondary care), UK Cancer Registry data and Office for National Statistics cause of death data. From these databases, we selected 498 children with cancer diagnosed between 1997 and 2006 and 20,810 controls without cancer. We calculated VTE incidence rates in children with cancer vs. controls, and hazard ratios (HRs) using Cox regression.

    Results: We identified four VTE events in children with cancer compared with four events in the larger control population corresponding to absolute risks of 1.52 and 0.06 per 1000 person-years respectively. The four children with VTE and cancer were diagnosed with hematological, bone or non-specified cancer. Childhood cancer was hence associated with a highly increased risk of VTE (HR adjusted for age and sex: 28.3; 95% CI = 7.0-114.5).

    Conclusions: Children with cancer are at increased relative risk of VTE compared to those without cancer. Physicians could consider thromboprophylaxis in children with cancer to reduce their excess risk of VTE however the absolute risk is extremely small and the benefit gained therefore would need to be balanced against the risk invoked of implementing such a strategy.

    Novelty & Impact Statements: While there is a reasonable level of knowledge about the risk of VTE in adult populations, it is not well known whether this risk is reflected in paediatric patients. We found a substantial increase in risk of VTE in children with cancer compared to a child population without cancer. While this finding is important, the absolute risk of VTE is still low and must be balanced with the risks of anticoagulation. (C) 2014 The Authors. Published by Elsevier Ltd. All rights reserved.

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