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  • 151.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Engberg, Anna E.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Rosengren-Holmberg, Jenny P.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Chen, H
    University of Pennsylvania.
    Lambris, JD
    University of Pennsylvania.
    Nicholls, Ian A.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Blood protein-polymer adsorption fingerprinting: Implications for understanding hemoocompatibility and for biomaterial design.2011Ingår i: Journal of Biomedical Materials Research. Part A, ISSN 1549-3296, E-ISSN 1552-4965, Vol. 97A, nr 1, s. 74-84Artikel i tidskrift (Refereegranskat)
  • 152.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Fromell, Karin
    Uppsala University.
    Hilborn, Jöns
    Uppsala University.
    Nilsson, Bo
    Uppsala University.
    The innate immune response: A key factor in biocompatibility2016Ingår i: Bioresorbable Polymers for Biomedical Applications: From Fundamentals to Translational Medicine / [ed] Giuseppe Perale & Jöns Hilborn, Elsevier, 2016, s. 85-94Kapitel i bok, del av antologi (Refereegranskat)
  • 153.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala university, Sweden.
    Fromell, Karin
    Uppsala university, Sweden.
    Hilborn, Jöns
    Uppsala university, Sweden.
    Nilsson, Bo
    Uppsala university, Sweden.
    The innate immunity response: A key factor in biocompatibility2017Ingår i: Bioresorbable polymers for biomedical applications: From fundamentals to translational medicine / [ed] Guiseppe Perale & Jöns Hilborn, Woodhead Publishing Limited, 2017, 1, s. 85-94Kapitel i bok, del av antologi (Refereegranskat)
  • 154.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala university, Sweden.
    Fromell, Karin
    Uppsala university, Sweden.
    Mohlin, Camilla
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Teramura, Yuji
    Uppsala university, Sweden;Univ Tokyo, Japan.
    Nilsson, Bo
    Uppsala university, Sweden.
    A human whole-blood model to study the activation of innate immunity system triggered by nanoparticles as a demonstrator for toxicity2019Ingår i: Science and Technology of Advanced Materials, ISSN 1468-6996, E-ISSN 1878-5514, Vol. 20, nr 1, s. 688-698Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    In this review article, we focus on activation of the soluble components of the innate immune system triggered by nonbiological compounds and stress variances in activation due to the difference in size between nanoparticles (NPs) and larger particles or bulk material of the same chemical and physical composition. We then discuss the impact of the so-called protein corona which is formed on the surface of NPs when they come in contact with blood or other body fluids. For example, NPs which bind inert proteins, proteins which are prone to activate the contact system (e.g., factor XII), which may lead to clotting and fibrin formation or the complement system (e.g., IgG or C3), which may result in inflammation and vascular damage. Furthermore, we describe a whole blood model which we have developed to monitor activation and interaction between different components of innate immunity: blood protein cascade systems, platelets, leukocytes, cytokine generation, which are induced by NPs. Finally, we describe our own studies on innate immunity system activation induced by three fundamentally different species of NPs (two types of engineered NPs and diesel NPs) as demonstrator of the utility of an initial determination of the composition of the protein corona formed on NPs exposed to ethylenediaminetetraacetic acid (EDTA) plasma and subsequent analysis in our whole blood model. [GRAPHICS] .

  • 155.
    Nilsson Ekdahl, Kristina
    et al.
    Uppsala University.
    Henningsson, A. J
    Ryhov County Hospital.
    Sandholm, Kerstin
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Forsberg, Pia
    Linköping University.
    Ernerudh, Jan
    Linköping University.
    Ekerfelt, Christina
    Linköping University.
    Immunity in borreliosis with special emphasis on the role of complement2007Ingår i: Advances in Experimental Medicine and Biology, ISSN 0065-2598, E-ISSN 2214-8019, Vol. 598, s. 198-213Artikel i tidskrift (Refereegranskat)
  • 156.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Hong, Jaan
    Uppsala University.
    Hamad, Osama
    Uppsala University.
    Larsson, Rolf
    Uppsala University.
    Nilsson, Bo
    Uppsala University.
    Evaluation of the blood compatibility of materials, cells and tissues: Basic concepts, test models and practical guidelines2013Ingår i: Complement Therapeutics / [ed] J.D. Lambris, V.M. Holers & D. Ricklin, Springer, 2013, s. 257-270Kapitel i bok, del av antologi (Refereegranskat)
    Abstract [en]

    Medicine today uses a wide range of biomaterials, most of which make contact with blood permanently or transiently upon implantation. Contact between blood and nonbiological materials or cells or tissue of nonhematologic origin initiates activation of the cascade systems (complement, contact activation/coagulation) of the blood, which induces platelet and leukocyte activation.

    Although substantial progress regarding biocompatibility has been made, many materials and medical treatment procedures are still associated with severe side effects. Therefore, there is a great need for adequate models and guidelines for evaluating the blood compatibility of biomaterials. Due to the substantial amount of cross talk between the different cascade systems and cell populations in the blood, it is advisable to use an intact system for evaluation.

    Here, we describe three such in vitro models for the evaluation of the biocompatibility of materials and therapeutic cells and tissues. The use of different anticoagulants and specific inhibitors in order to be able to dissect interactions between the different cascade systems and cells of the blood is discussed. In addition, we describe two clinically relevant medical treatment modalities, the integration of titanium implants and transplantation of islets of Langerhans to patients with type 1 diabetes, whose mechanisms of action we have addressed using these in vitro models.

  • 157.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Huang, Shan
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Nilsson, Bo
    Uppsala University.
    Teramura, Yuji
    Uppsala University;The University of Tokyo, Japan.
    Complement inhibition in biomaterial- and biosurface-induced thromboinflammation2016Ingår i: Seminars in Immunology, ISSN 1044-5323, E-ISSN 1096-3618, Vol. 28, nr 3, s. 268-277Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Therapeutic medicine today includes a vast number of procedures involving the use of biomaterials, transplantation of therapeutic cells or cell clusters, as well as of solid organs. These treatment modalities are obviously of great benefit to the patient, but also present a great challenge to the innate immune system, since they involve direct exposure of non-biological materials, cells of non-hematological origin as well as endothelial cells, damaged by ischemia-perfusion in solid organs to proteins and cells in the blood. The result of such an exposure may be an inappropriate activation of the complement and contact/kallikrein systems, which produce mediators capable of triggering the platelets and PMNs and monocytes, which can ultimately result in thrombotic and inflammatory (i.e., a thrombo-inflammatory) response to the treatment modality. In this concept review, we give an overview of the mechanisms of recognition within the innate immunity system, with the aim to identify suitable points for intervention. Finally, we discuss emerging and promising techniques for surface modification of biomaterials and cells with specific inhibitors in order to diminish thromboinflammation and improve clinical outcome.

  • 158.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Lambris, JD
    Elwing, H
    Ricklin, D
    Nilsson, Per H.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Teramura, Y
    Nicholls, Ian A.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Nilsson, Bo
    Innate immunity activation on biomaterial surfaces: A mechanistic model and coping strategies2011Ingår i: Advanced Drug Delivery Reviews, ISSN 0169-409X, E-ISSN 1872-8294, Vol. 63, nr 12, s. 1042-1050Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    When an artificial biomaterial (e.g., a stent or implantable pump) is exposed to blood, plasma proteins immediately adhere to the surface, creating a new interface between the biomaterial and the blood. The recognition proteins within the complement and contact activation/coagulation cascade systems of the blood will be bound to, or inserted into, this protein film and generate different mediators that will activate polymorphonuclear leukocytes and monocytes, as well as platelets. Under clinical conditions, the ultimate outcome of these processes may be thrombotic and inflammatory reactions, and consequently the composition and conformation of the proteins in the initial layer formed on the surface will to a large extent determine the outcome of a treatment involving the biomaterial, affecting both the functionality of the material and the patient's life quality. This review presents models of biomaterial-induced activation processes and describes various strategies to attenuate potential adverse reactions by conjugating bioactive molecules to surfaces or by introducing nanostructures.

  • 159.
    Nilsson Ekdahl, Kristina
    et al.
    University Hospital, Uppsala.
    Lööf, L
    Ahrenstedt, Örjan
    Nilsson, U R
    Nilsson, Bo
    Defective elimination of C3b/iC3b-coated autologous erythrocytes in patients with primary biliary cirrhosis, alcoholic cirrhosis, and ulcerative colitis1997Ingår i: The journal of laboratory and clinical medicine, Vol. 130, s. 285-292Artikel i tidskrift (Refereegranskat)
  • 160.
    Nilsson Ekdahl, Kristina
    et al.
    Department of Clinical Immunology and Transfusion Medicine, University Hospital, Uppsala.
    Lööf, L
    Nilsson, U R
    Nilsson, Bo
    An improved method to study complement receptor-mediated function of the fixed macrophage system in vivo1991Ingår i: Vox Sanguinis, ISSN 0042-9007, E-ISSN 1423-0410, Vol. 61, nr 1, s. 47-52Artikel i tidskrift (Refereegranskat)
    Abstract [en]

     A method to coat unsensitized erythrocytes with fragments of C3 and C4 using autologous serum, in order to study complement receptor-dependent function of the fixed macrophage system, is presented. After incubation with serum under optimal conditions, at least 90% of the cells had C3b/iC3b deposited on the surface, with an average of 20 × 103 molecules per cell. Elimination of the coated cells by the fixed macrophage system was studied in 12 normal subjects. With a dose of 4.5 × 108 red cells injected, 75% of the cells were eliminated with a half-life of approximately 2.4 ± 0.3 min (n = 7). In subjects receiving ten times more cells, there was a rapid decrease in the amount of C3-coated cells, reaching a nadir with 85% remaining for 4–6 min, after which there was a gradual release of cells for another 20 min (n = 5). In absolute numbers, 3 × 108 of labeled cells were eliminated regardless of the dose injected. The coating procedure presented here is simple, does not introduce heterologous blood components and makes it possible to control the amount and the degree of fragmentation of the C3 and C4 deposited on the erythrocyte surface. 

  • 161.
    Nilsson Ekdahl, Kristina
    et al.
    University Hospital, Uppsala.
    Lööf, L
    Nilsson, U R
    Nilsson, Bo
    Development of an immunoassay for the detection of minute amounts of IgG-coated erythrocytes in whole blood: Its application for the assessment of Fc-mediated clearance of anti-D-coated erythrocytes in vivo1989Ingår i: Vox Sanguinis, ISSN 0042-9007, E-ISSN 1423-0410, Vol. 57, nr 3, s. 188-192Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A rapid and sensitive immunoassay for the detection of minute quantities of IgG-coated erythrocytes in whole blood was developed. Washed red blood cells were incubated in two steps with anti-human IgG antiserum followed by 125I-labelled protein A. The assay was able to detect amounts of sensitized erythrocytes as small as 0.5 ml of packed erythrocytes in a total blood volume of 5 liters and hematocrit 40%. A linear relation between increasing amounts of IgG-coated red cells in whole blood and the binding of 125I-labelled protein A was obtained. We applied the technique on the assessment of the removal of IgG anti-D-coated erythrocytes from the circulation of test individuals. T1/2 for the elimination of approximately 4 ml packed red cells sensitized with 62 μg of anti-D in 14 normal subjects was 20±5 min (mean±SEM). A splenectomized person did not clear the injected cells from the circulation during the test period of 70 min. If a standard curve was constructed the total blood volume in the test subjects could be calculated. This value correlated well (r = 0.99) with the blood volume calculated from the height and weight of the test individuals. 

  • 162.
    Nilsson Ekdahl, Kristina
    et al.
    Department of Clinical Immunology and Transfusion Medicine, University Hospital, Uppsala.
    Lööf, L
    Nyberg, A
    Nilsson, U R
    Nilsson, Bo
    Defective Fc receptor-mediated clearance in patients with primary biliary cirrhosis1991Ingår i: Gastroenterology, ISSN 0016-5085, E-ISSN 1528-0012, Vol. 101, nr 4, s. 1076-1082Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Fc receptor-mediated clearance of immunoglobulin G-coated autologous erythrocytes was studied in patients with primary biliary cirrhosis (n = 14), alcoholic liver cirrhosis (n = 5) and healthy reference individuals (n = 14). The mean half-life of the sensitized erythrocytes was significantly prolonged in patients with primary biliary cirrhosis (85 +/- 25 minutes; P less than 0.001) compared with the corresponding value in patients with alcoholic cirrhosis (16 +/- 2 minutes) and healthy reference individuals (20 +/- 5 minutes), respectively. No correlation between clearance rate and age, liver histopathology, or serum levels of bilirubin, aminotransferases, immunoglobulin G, immunoglobulin A, and Clq binding or C3-containing immune complexes was found. The results presented here indicate a profound disturbance of Fc receptor-mediated immune clearance function in patients with primary biliary cirrhosis. 

  • 163.
    Nilsson Ekdahl, Kristina
    et al.
    Biomedical Centre, Uppsala.
    Michaëlsson, G
    Gerdén, B
    Lööf, L
    Nilsson, B
    Impairments in complement receptor- and Fc receptor-mediated functions in psoriasis1995Ingår i: Archives of dermatological research, Vol. 287, s. 225-230Artikel i tidskrift (Refereegranskat)
  • 164.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala university, Sweden.
    Mohlin, Camilla
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Adler, Anna
    Uppsala university, Sweden.
    Aman, Amanda
    Uppsala university, Sweden.
    Manivel, Vivek Anand
    Uppsala university, Sweden.
    Sandholm, Kerstin
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Huber-Lang, Markus
    Univ Hosp Ulm, Germany.
    Fromell, Karin
    Uppsala university, Sweden.
    Nilsson, Bo
    Uppsala university, Sweden.
    Is generation of C-3(H2O) necessary for activation of the alternative pathway in real life?2019Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 114, s. 353-361Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    In the alternative pathway (AP) an amplification loop is formed, which is strictly controlled by various fluid-phase and cell-bound regulators resulting in a state of homeostasis. Generation of the "C3b-like" C3(H2O) has been described as essential for AP activation, since it conveniently explains how the initial fluid-phase AP convertase of the amplification loop is generated. Also, the AP has a status of being an unspecific pathway despite thorough regulation at different surfaces. During complement attack in pathological conditions and inflammation, large amounts of C3b are formed by the classical/lectin pathway (CP/LP) convertases. After the discovery of LP's recognition molecules and its tight interaction with the AP, it is increasingly likely that the AP acts in vivo mainly as a powerful amplification mechanism of complement activation that is triggered by previously generated C3b molecules initiated by the binding of specific recognition molecules. Also in many pathological conditions caused by a dysregulated AP amplification loop such as paroxysmal nocturnal hemoglobulinuria (PNH) and atypical hemolytic uremic syndrome (aHUS), C3b is available due to minute LP and CP activation and/or generated by non-complement proteases. Therefore, C3(H2O) generation in vivo may be less important for AP activation during specific attack or dysregulated homeostasis, but may be an important ligand for C3 receptors in cell-cell interactions and a source of C3 for the intracellular complement reservoir.

  • 165.
    Nilsson Ekdahl, Kristina
    et al.
    Uppsala university, Sweden.
    Nilsson, Bo
    Uppsala university, Sweden.
    Hemodialys, inflammation och det naturliga immunsystemet2018Ingår i: Vaskulär Medicin, ISSN 2000-3188, Vol. 34, nr 3, s. 17-21Artikel, forskningsöversikt (Övrigt vetenskapligt)
    Abstract [sv]

    Hemodialys är en livräddande behandling vid kronisk njursvikt, men dialyspatienter har också en kraftigt ökad risk för kardiovaskulär sjukdom. Dialys utgör en enorm utmaning för kroppens naturliga immunsystem (”innate immunity”) eftersom patientens blod under behandlingen kommer i direkt kontakt med kroppsfrämmande ytor såsom i membran, slangar, och pumpar mm. Då sker aktivering av blodets olika protein-system: främst komplementsystemet, kontakt/kallikreinsystemet och koagulationsystemet, vilket initialt leder till en lokal inflammation i anslutning till materialytan i dialyskretsen, men också generering av inflammatoriska mediatorer, till exempel anafylatoxiner och bradykinin. Dessa substanser transporteras sedan med blodet till patienten tillsammans med aktiverade leukocyter och trombocyter som aktiverar endotelet i patientens kardiovaskulära system, som då kan förlora sina normala anti-inflammatoriska och anti-trombotiska funktioner. Sammantaget resulterar detta i en kronisk inflammation som kan leda till atherogenes och arterioskleros. Möjliga strategier att dämpa dessa reaktioner inkluderar val av antikoagulantia med högre specificitet än de typer av heparin som används idag, samt ytmodifiering av de material som ingår i dialyskretsen.

  • 166.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson, Bo
    Increased affinity between CR1 and C3b phosphorylated by a casein kinase released by activated human platelets2001Ingår i: European journal of immunology, Vol. 31, s. 1047-1054Artikel i tidskrift (Refereegranskat)
  • 167.
    Nilsson Ekdahl, Kristina
    et al.
    University Hospital, Uppsala.
    Nilsson, Bo
    Phosphorylation of complement component C3 after synthesis in U937 cells by a putative protein kinase CK2, which is regulated by CD11b: Evidence that membrane-bound proteases preferentially cleave phosphorylated C31997Ingår i: Biochemical journal, Vol. 328, s. 625-633Artikel i tidskrift (Refereegranskat)
  • 168.
    Nilsson Ekdahl, Kristina
    et al.
    Uppsala University.
    Nilsson, Bo
    Uppsala University.
    Phosphorylation of complement component C3 and C3 fragments by a human platelet protein kinase. Inhibition of factor I mediated cleavage of C3b1995Ingår i: Journal of immunology, Vol. 154, s. 6502-6509Artikel i tidskrift (Refereegranskat)
  • 169.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen. University Hospital, Uppsala.
    Nilsson, Bo
    Phosphorylation of plasma proteins with emphasis on complement component C31999Ingår i: Molecular immunology, Vol. 36 (4-5), s. 233-240Artikel i tidskrift (Refereegranskat)
  • 170.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson, Bo
    Profound alterations in C3 functions caused by phosphorylation by a casein kinase released by activated human platelets with special reference to thiol ester function1999Ingår i: Journal of immunology, Vol. 162, s. 7426-7433Artikel i tidskrift (Refereegranskat)
  • 171.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson, Bo
    Andersson, Jonas
    Neff, Jeniffer
    Caldwell, Karin
    Surface coating comprising bioactive compound2004Patent (Övrig (populärvetenskap, debatt, mm))
  • 172.
    Nilsson Ekdahl, Kristina
    et al.
    University Hospital, Uppsala.
    Nilsson, Bo
    Gölander, C G
    Elwing, H
    Lassen, B
    Nilsson, U R
    Complement activation on radio frequency plasma modified polystyrene surfaces1993Ingår i: Journal of colloid and interface science, Vol. 158, s. 121-128Artikel i tidskrift (Refereegranskat)
  • 173.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson, Bo
    Storm, K E
    Nilsson, U R
    Techniques to study functional properties of IgG preparations for parenteral use1992Ingår i: Life science advances, Vol. 11, s. 221-227Artikel i tidskrift (Refereegranskat)
  • 174.
    Nilsson Ekdahl, Kristina
    et al.
    Department of Clinical Immunology and Transfusion Medicine, University Hospital, Uppsala.
    Nilsson, U R
    Nilsson, Bo
    Inhibition of factor I by diisopropylfluorophosphate. Evidence of conformational changes in factor I induced by C3b and additional studies on the specificity of factor I1990Ingår i: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 144, nr 11, s. 4269-4274Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The factor I-mediated cleavage of C3b, using factor H as a cofactor was completely inhibited by diisopropylfluorophosphate (DFP) when factor I and C3b were incubated with DFP before the addition of factor H. Inhibition, although to a lesser degree, was observed when factor H was present during DFP-exposure. No inhibition in factor I activity was seen when factor I and H were incubated with DFP either alone or together. It was also demonstrated that the 38-kDa subunit of factor I bound radiolabeled DFP when factor I and C3b together were exposed to DFP. These observations suggest that factor I interacts with C3b in a manner that exposes its catalytic site to DFP, an interaction that is independent of factor H. The inhibitory effect by DFP on factor I led us to further investigate the factor I cleavage products of iC3b, inasmuch as previous reports were ambiguous as to whether digestion occurs in the presence of DFP. Digestion of C3b bound to activated thiol Sepharose (ATS-C3b) in the presence of factor H at low pH and ionic strength and in serum by complement activation produced C3d,g- like fragments with apparent molecular mass of 41 and 43 kDa. These fragments were shown to have three different N-terminal and two different C-terminal ends. The major fragments had N-terminal sequences starting with Glu933, as shown by sequence determination. Traces of fragments extending beyond this point were also found, shown by Western blot analysis using a panel of mAb previously shown to bind to epitopes exposed within a region of C3 spanning residues 929 to 943, as well as a shorter fragment starting with Glu938. When digestion of C3b is carried out in the presence of DFP, the factor I level necessary for digestion is elevated and may explain how the first two cleavages producing iC3b but not the following giving C3d,g, can occur. The finding of several factor I cleavage sites in the C3d,g region of C3 demonstrates that factor I has a broad specificity, mainly for arginyl bonds. It has also been shown to digest a lysyl bond exposed in ATS- bound C3b. 

  • 175.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Norberg, D
    Sturfelt, G
    Nilsson, U. R
    Nilsson, Bo
    A rapid, inexpensive, and easy-to-perform haemolytic complement assay using serum of buffer-changed EDTA-plasma: Its use for differential diagnosis and follow-up of patients with systemic lupus erythematosus2007Ingår i: Clinical and Vaccine Immunology, ISSN 1556-6811, E-ISSN 1556-679X, Vol. 14, nr 5, s. 549-555Artikel i tidskrift (Refereegranskat)
  • 176.
    Nilsson Ekdahl, Kristina
    et al.
    Department of Clinical Immunology and Transfusion Medicine, University Hospital, Uppsala.
    Pekna, M
    Nilsson, Bo
    Nilsson, U R
    Generation of iC3 on the interphase between blood and gas1992Ingår i: Scandinavian Journal of Immunology, ISSN 0300-9475, E-ISSN 1365-3083, Vol. 35, nr 1, s. 85-91Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Earlier studies have shown that C3 can be denatured when blood comes in contact with a polystyrene surface. This study was undertaken to sec if similar denaturation of C3 occurs at the gas plasma interface which is found in all kinds of oxygenator used during cardio-pulmonary operations. An in vitro system consisting of gas bubbling through human blood, serum or plasma was used. The generation of C3a, as an indicator of complement activation, and iC3 and iC3 fragments were monitored. Both C3a and iC3/iC3 fragments levels were increased during bubbling. In contrast to the C3a level, no reduction in iC3/iC3 fragments formation was seen in the presence of EDTA, indicating that il was independent of complement activation. The rate of iC3/iC3 fragments generation was unaffected by the composition of the gas (pure oxygen, pure nitrogen or air), suggesting that the denaturation of C3 indeed occurred at the serum gas interface. C3 and iC3/iC3 fragments were isolated from bubbled EDTA-chelated serum by PEG precipitation and chromatography on FPLC, using a Mono S column and detected by two ELISAs, specific for native C3 and iC3/iC3 fragments. After 240 min approximately 20% of the total amount of C3 consisted of intact iC3 and it was confirmed that this population bound to human erythrocytes. 

  • 177.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Persson, Barbro
    Uppsala University.
    Mohlin, Camilla
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Sandholm, Kerstin
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Skattum, Lillemor
    Lund University.
    Nilsson, Bo
    Uppsala University.
    Interpretation of Serological Complement Biomarkers in Disease2018Ingår i: Frontiers in Immunology, ISSN 1664-3224, E-ISSN 1664-3224, Vol. 9, artikel-id 2237Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Complement systemaberrations have been identified as pathophysiological mechanisms in a number of diseases and pathological conditions either directly or indirectly. Examples of such conditions include infections, inflammation, autoimmune disease, as well as allogeneic and xenogenic transplantation. Both prospective and retrospective studies have demonstrated significant complement-related differences between patient groups and controls. However, due to the low degree of specificity and sensitivity of some of the assays used, it is not always possible to make predictions regarding the complement status of individual patients. Today, there are three main indications for determination of a patient's complement status: (1) complement deficiencies (acquired or inherited); (2) disorders with aberrant complement activation; and (3) C1 inhibitor deficiencies (acquired or inherited). An additional indication is to monitor patients on complement-regulating drugs, an indication which may be expected to increase in the near future since there is now a number of such drugs either under development, already in clinical trials or in clinical use. Available techniques to study complement include quantification of: (1) individual components; (2) activation products, (3) function, and (4) autoantibodies to complement proteins. In this review, we summarize the appropriate indications, techniques, and interpretations of basic serological complement analyses, exemplified by a number of clinical disorders.

  • 178.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Ronquist, Gunnar
    University Hospital, Uppsala.
    Nilsson, Bo
    University Hospital, Uppsala.
    Babiker, Adil A
    University Hospital, Uppsala.
    Possible immunoprotective and angiogenesis-promoting roles for malignant cell-derived prostasomes: A new paradigm for prostatic cancer?2006Ingår i: Current Topics in Complement / [ed] John D. Lambris, Springer, 2006, Vol. 586, s. 107-119Kapitel i bok, del av antologi (Refereegranskat)
    Abstract [en]

    Understanding the protective mechanisms utilized by metastatic prostate cancer cells in order to avoid attack by complement or other parts of the innate immune system and to affect tumor angiogenesis and metastasis will help us to identify suitable targets for pharmaceutical intervention. We have shown that at least two different complement-attenuating mechanisms are at work in close proximity to prostasomes: transfer of CD59, which inhibits complement at the level of MAC insertion, and phosphorylation of C3 so as to make it resistant to (physiological) activation and thereby regulate complement at the convertase level. In addition, we have shown that both fibrinogen and vitronectin, which play critical roles in cell adhesion, are targets for prostasome-mediated phosphorylation. Given the broad specificity of the various PKs, it is most likely that other relevant substrates such as proteins involved in angiogenesis or different matrix proteins may be found. Finally, we have demonstrated that expression and function of different proteins capable of mediating these effects (CD59 and PKs, particularly PKA) are highly upregulated on prostasomes derived from malignant cell lines as compared to seminal prostasomes, suggesting that the malignant cell-associated prostasomes have a higher potential to interact with neighboring cells.

    The fact that substantial differences are found in protein expression profiles between physiological and pathological prostasomes may be relevant in the search for suitable clinical markers to identify patients with primary prostate cancer who are at risk for developing metastases. In addition, possible targets for therapeutic intervention may include GPI-anchored proteins and specific PKs present at high concentrations in close proximity to metastases. If the overexpression of RCAs and PKs on metastatic prostate cancer cells can be controlled or counteracted, these modifications could possibly also be used to potientate other types of immunotherapy.

  • 179.
    Nilsson Ekdahl, Kristina
    et al.
    University Hospital, Uppsala.
    Rönnblom, L
    University Hospital, Uppsala.
    Sturfeldt, G
    University Hospital, Lund.
    Nilsson, Bo
    University Hospital, Uppsala.
    Increased phosphate content in complement component C3, fibrinogen, vitronectin and other plasma proteins in SLE. Covariations with platelet activation and possible association with thrombosis1997Ingår i: Arthritis and rheumatism, Vol. 40, s. 2178-2186Artikel i tidskrift (Refereegranskat)
  • 180.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Soveri, Inga
    Uppsala University.
    Hilborn, Jons
    Uppsala University.
    Fellström, Bengt
    Uppsala University.
    Nilsson, Bo
    Uppsala University.
    Cardiovascular disease in haemodialysis: role of the intravascular innate immune system2017Ingår i: Nature Reviews Nephrology, ISSN 1759-5061, E-ISSN 1759-507X, Vol. 13, nr 5, s. 285-296Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Haemodialysis is a life-saving renal replacement modality for end-stage renal disease, but this therapy also represents a major challenge to the intravascular innate immune system, which is comprised of the complement, contact and coagulation systems. Chronic inflammation is strongly associated with cardiovascular disease (CVD) in patients on haemodialysis. Biomaterial-induced contact activation of proteins within the plasma cascade systems occurs during haemodialysis and initially leads to local generation of inflammatory mediators on the biomaterial surface. The inflammation is spread by soluble activation products and mediators that are generated during haemodialysis and transported in the extracorporeal circuit back into the patient together with activated leukocytes and platelets. The combined effect is activation of the endothelium of the cardiovascular system, which loses its anti-thrombotic and anti-inflammatory properties, leading to atherogenesis and arteriosclerosis. This concept suggests that maximum suppression of the intravascular innate immune system is needed to minimize the risk of CVD in patients on haemodialysis. A potential approach to achieve this goal is to treat patients with broad-specificity systemic drugs that target more than one of the intravascular cascade systems. Alternatively, 'stealth' biomaterials that cause minimal cascade system activation could be used in haemodialysis circuits.

  • 181.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala university.
    Teramura, Yuji
    Univ Tokyo, Japan.
    Asif, Sana
    Uppsala university.
    Jonsson, Nina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Magnusson, Peetra
    Uppsala university.
    Nilsson, Bo
    Uppsala university.
    Thromboinflammation in therapeutic medicine2015Ingår i: Immune Responses to Biosurfaces / [ed] Lambris J., Ekdahl K., Ricklin D., Nilsson B., Springer, 2015, Vol. 865, s. 3-17Konferensbidrag (Refereegranskat)
    Abstract [en]

    Thromboinflammation is primarily triggered by the humoral innate immune system, which mainly consists of the cascade systems of the blood, i.e., the complement, contact/coagulation and fibrinolytic systems. Activation of these systems subsequently induces activation of endothelial cells, leukocytes and platelets, finally resulting in thrombotic and inflammatory reactions. Such reactions are triggered by a number of medical procedures, e.g., treatment with biomaterials or drug delivery devices as well as in transplantation with cells, cell clusters or whole vascularized organs. Here, we (1) describe basic mechanisms for thromboinflammation; (2) review thromboinflammatory reactions in therapeutic medicine; and (3) discuss emerging strategies to dampen thromboinflammation.

  • 182.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Teramura, Yuji
    Uppsala University;Univ Tokyo, Japan.
    Asir, Sana
    Uppsala University.
    Manell, Elin
    Swedish University of Agricultural Sciences.
    Biglarnia, Alireza
    Skåne Univ Hosp.
    Jensen-Waern, Marianne
    Swedish University of Agricultural Sciences.
    Nilsson, Bo
    Uppsala University.
    Protective role of PEG conjugated phospholipid in reducing ischemic reperfusion injury in two allogeneic pig kidney transplant models2016Ingår i: Immunobiology, ISSN 0171-2985, E-ISSN 1878-3279, Vol. 221, nr 10, s. 1184-1184Artikel i tidskrift (Övrigt vetenskapligt)
  • 183.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Teramura, Yuji
    Uppsala University;Univ Tokyo, Japan.
    Hamad, Osama A.
    Uppsala University.
    Asif, Sana
    Uppsala University.
    Duehrkop, Claudia
    Uppsala University.
    Fromell, Karin
    Uppsala University.
    Gustafson, Elisabet
    Uppsala University Hospital.
    Hong, Jaan
    Uppsala University.
    Kozarcanin, Huda
    Uppsala University.
    Magnusson, Peetra U.
    Uppsala University.
    Huber-Lang, Markus
    University of Ulm, Germany.
    Garred, Peter
    Univ Copenhagen, Denmark.
    Nilsson, Bo
    Uppsala University.
    Dangerous liaisons: complement, coagulation, and kallikrein/kinin cross-talk act as a linchpin in the events leading to thromboinflammation2016Ingår i: Immunological Reviews, ISSN 0105-2896, E-ISSN 1600-065X, Vol. 274, nr 1, s. 245-269Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Innate immunity is fundamental to our defense against microorganisms. Physiologically, the intravascular innate immune system acts as a purging system that identifies and removes foreign substances leading to thromboinflammatory responses, tissue remodeling, and repair. It is also a key contributor to the adverse effects observed in many diseases and therapies involving biomaterials and therapeutic cells/organs. The intravascular innate immune system consists of the cascade systems of the blood (the complement, contact, coagulation, and fibrinolytic systems), the blood cells (polymorphonuclear cells, monocytes, platelets), and the endothelial cell lining of the vessels. Activation of the intravascular innate immune system in vivo leads to thromboinflammation that can be activated by several of the system's pathways and that initiates repair after tissue damage and leads to adverse reactions in several disorders and treatment modalities. In this review, we summarize the current knowledge in the field and discuss the obstacles that exist in order to study the cross-talk between the components of the intravascular innate immune system. These include the use of purified in vitro systems, animal models and various types of anticoagulants. In order to avoid some of these obstacles we have developed specialized human whole blood models that allow investigation of the cross-talk between the various cascade systems and the blood cells. We in particular stress that platelets are involved in these interactions and that the lectin pathway of the complement system is an emerging part of innate immunity that interacts with the contact/coagulation system. Understanding the resulting thromboinflammation will allow development of new therapeutic modalities.

  • 184.
    Nilsson, Per H.
    et al.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Engberg, Anna E.
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Bäck, Jennie
    Div. Clinical Immunology, Rudbeck Laboratory, University Hospital, Uppsala.
    Faxälv, Lars
    Department of Clinical Chemistry, Laboratory Medicine, University Hospital, Linköping.
    Lindahl, Tomas
    Department of Clinical Chemistry, Laboratory Medicine, University Hospital, Linköping.
    Nilsson, Bo
    Div. Clinical Immunology, Rudbeck Laboratory, University Hospital, Uppsala.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    The creation of an antithrombotic surface by apyrase immobilization2010Ingår i: Biomaterials, ISSN 0142-9612, E-ISSN 1878-5905, Vol. 31, nr 16, s. 4484-4491Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Blood incompatibility reactions caused by surfaces often involve platelet activation and subsequent platelet-initiated activation of the coagulation and complement cascades. The goal of this study was to immobilize apyrase on a biomaterial surface in order to develop an enzymatically active surface that would have the capacity to inhibit platelet activation by degrading ADP. We were able to immobilize apyrase on a polystyrene surface with preservation of the enzymatic activity. We then analyzed the hemocompatibility of the apyrase surface and of control surfaces by incubation with platelet-rich plasma (PRP) or whole blood. Monitoring of markers of platelet, coagulation, and complement activation and staining of the surfaces revealed decreased levels of platelet and coagulation activation parameters on the apyrase surface. The formation of antithrombin-thrombin and antithrombin-factor XIa complexes and the extent of platelet consumption were significantly lower on the apyrase surface than on any of the control surfaces. No significant differences were seen in complement activation (C3a levels). Staining of the apyrase surface revealed low platelet adherence and no formation of granulocyte platelet complexes. These results demonstrate that it is possible to create an antithrombotic surface targeting the ADP amplification of platelet activation by immobilizing apyrase.

  • 185.
    Nilsson, Per H.
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Magnusson, Peetra U
    Uppsala University.
    Qu, Hongchang
    University of Pennsylvania, USA.
    Iwata, Hiroo
    Kyoto University, Japan.
    Ricklin, Daniel
    University of Pennsylvania, USA.
    Hong, Jaan
    Uppsala University.
    Lambris, John D
    University of Pennsylvania, USA.
    Nilsson, Bo
    Uppsala University.
    Teramura, Yuji
    Uppsala University;Kyoto University, Japan.
    Autoregulation of thromboinflammation on biomaterial surfaces by a multicomponent therapeutic coating2013Ingår i: Biomaterials, ISSN 0142-9612, E-ISSN 1878-5905, Vol. 34, nr 4, s. 985-994Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Activation of the thrombotic and complement systems is the main recognition and effector mechanisms in the multiple adverse biological responses triggered when biomaterials or therapeutic cells come into blood contact. We have created a surface which is auto-protective to human innate immunity by combining three fundamentally different strategies, all developed by us previously, which have been shown to induce substantial, but incomplete hemocompatibility when used separately. In summary, we have conjugated a factor H-binding peptide; and an ADP-degrading enzyme; using a PEG linker on both material and cellular surfaces. When exposed to human whole blood, factor H was specifically recruited to the modified surfaces and inhibited complement attack. In addition, activation of platelets and coagulation was efficiently attenuated, by degrading ADP. Thus, by inhibiting thromboinflammation using a multicomponent approach, we have created a hybrid surface with the potential to greatly reduce incompatibility reactions involving biomaterials and transplantation.

  • 186. Nilsson, U R
    et al.
    Larm, O
    Storm, K E
    Nilsson, Bo
    Elwing, H
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Modification of the complement binding properties of polystyrene: Effects of end-point heparin attachment1993Ingår i: Scandinavian journal of immunology, Vol. 37, s. 349-354Artikel i tidskrift (Refereegranskat)
  • 187.
    Nilsson, UR
    et al.
    Uppsala University.
    Funke, Lillemor
    Uppsala University.
    Nilsson, Bo
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Two conformational forms of target bound iC3b which distinctively bind complement receptors 1 and 2 (CR1 and CR2) and two specific monoclonal antibodies.2010Ingår i: Upsala Journal of Medical Sciences, Supplement, ISSN 0300-9726Artikel i tidskrift (Övrigt vetenskapligt)
    Abstract [en]

    Introduction. The complement system is an essential part of the immune system of vertebrates. The central event of thecomplement activation cascade is the sequential proteolytic activation of C3, which is associated with profound alterations inthe molecule’s structure and conformation and is responsible for triggering most of the biological effects of complement.Material and methods. Here, we have studied the conformation of C3 fragments deposited onto an IgG-coated surface fromhuman serum during complement activation, using a set of unique monoclonal antibodies (mAbs) that are all specific for theC3dg portion of bound iC3b.Results. We were able to identify two conformational forms of target-bound iC3b: the first recognized by mAb 7D18.1, and thesecond by mAb 7D323.1. The first species of iC3b bound recombinant complement receptor 1 (CR1), while the second boundCR2. Since CR1 and CR2 are expressed by different subsets of leukocytes, this difference in receptor-binding capacity impliesthat there is a biological difference between the two forms of surface-bound iC3b.Conclusion. We propose that mAbs 7D18.1 and 7D323.1 can act as surrogate markers for CR1 and CR2, respectively, and thatthey may be useful tools for studying the immune complexes that are generated in various autoimmune diseases.

  • 188.
    Noiri, Makoto
    et al.
    Univ Tokyo, Japan.
    Asawa, Kenta
    Univ Tokyo, Japan.
    Okada, Naoya
    Univ Tokyo, Japan.
    Kodama, Tomonobu
    Jikei Univ Hosp, Japan.
    Murayama, Yuichi
    Jikei Univ Hosp, Japan.
    Inoue, Yuuki
    Univ Tokyo, Japan.
    Ishihara, Kazuhiko
    Univ Tokyo, Japan.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University, Sweden.
    Nilsson, Bo
    Uppsala University, Sweden.
    Teramura, Yuji
    Univ Tokyo, Japan;Uppsala University, Sweden.
    Modification of human MSC surface with oligopeptide-PEG-lipids for selective binding to activated endothelium2019Ingår i: Journal of Biomedical Materials Research. Part A, ISSN 1549-3296, E-ISSN 1552-4965, Vol. 107, nr 8, s. 1779-1792Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Promising cell therapies using mesenchymal stem cells (MSCs) is proposed for stroke patients. Therefore, we aimed to efficiently accumulate human MSC (hMSC) to damaged brain area to improve the therapeutic effect using poly(ethylene glycol) (PEG)-conjugated phospholipid (PEG-lipid) carrying an oligopeptide as a ligand, specific for E-selectin which is upregulated on activated endothelial cells under hypoxia-like stroke. Here we synthesized E-selectin-binding oligopeptide (ES-bp) conjugated with PEG spacer having different molecular weights from 1 to 40 kDa. We found that ES-bp can be immobilized onto the hMSC surface through PEG-lipid without influence on cell growth and differentiation into adipocytes and osteocytes, respectively. It is also possible to control the immobilization of ES-bp on hMSC surface (<10(8) ES-bp per cell). Immobilized ES-bp can be continuously immobilized at the outside of cell membrane when PEG-lipids with PEG 5 and 40 kDa were used. In addition, the modified hMSC can specifically attach onto E-selectin-immobilized surface as a model surface of activated endothelium in human blood, indicating the sufficient number of immobilized ES-bp onto hMSC. Thus, this technique is one of the candidates for hMSC accumulation to cerebral infarction area. (c) 2019 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 107A: 1779-1792, 2019.

  • 189. Norda, R
    et al.
    Knutson, F
    Berseus, O
    Åkerblom, O
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Stegmayr, B.G
    Nilsson, Bo
    Unexpected effects of donor gender on the storage of liquid plasma2007Ingår i: Vox Sanguinis, ISSN 0042-9007, E-ISSN 1423-0410, Vol. 93, nr 3, s. 223-228Artikel i tidskrift (Refereegranskat)
  • 190. Norda, Rut
    et al.
    Schött, U
    Berséus, Olof
    Åkerblom, Olof
    Nilsson, Bo
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Stegmayr, Bernd
    Knutson, Folke
    Complement activation products in liquid stored plasma and C3a-kinetics after transfusion of autologous plasma2012Ingår i: Vox Sanguinis, ISSN 0042-9007, E-ISSN 1423-0410, Vol. 102, nr 2, s. 125-133Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Background and Objectives  Keeping a small stock of liquid plasma readily available for transfusion is common practise in Sweden. We report data on complement activation markers in plasma components during storage in the liquid state and the kinetics of C3a-desArg after transfusion of autologous plasma with high content of C3a-desArg.

    Material and Methods  Plasma components were prepared by apheresis or from whole blood. C3 fragments (C3a-desArg, C3d,g, iC3), and soluble terminal complement complex (sC5b-9) were investigated. C3a-desArg kinetics was investigated in regular apheresis donors.

    Results  Apheresis plasma prepared by membrane centrifugation had significantly higher level of C3a-desArg, C3d,g and sC5b-9 from day 0 and low iC3, than plasma prepared by other methods. By storage day 7, C3a-desArg -levels were above the reference value in 88% of all components. After re-infusion of autologous plasma with high C3a-desArg content, there were rapid a1 and a2-distribution followed by a slower b-elimination phase.

    Conclusion  Plasma components prepared by different methods and stored in the liquid phase differ significantly in the amount and timing of complement activation. C3a-desArg present in plasma is rapidly eliminated after transfusion. Autologous plasma could be used to study complement kinetics in different clinical situations.

  • 191. Pekna, M
    et al.
    Nilsson, L
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson, U R
    Nilsson, Bo
    Evidence for iC3 generation during cardiopulmonary bypass as the result of blood-gas interaction1993Ingår i: Clinical and experimental immunology, Vol. 91, s. 404-409Artikel i tidskrift (Refereegranskat)
  • 192. Ramos, O F
    et al.
    Nilsson, Bo
    Nilsson Ekdahl, Kristina
    The Blood Centre, University Hospital, Uppsala.
    Eggertsen, G
    Yefenov, E
    Klein, E
    Elevated NK-mediated lysis of Raji and Daudi cells carrying fixed iC3b fragments1989Ingår i: Cellular Immunology, ISSN 0008-8749, E-ISSN 1090-2163, Vol. 119, nr 2, s. 459-469Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Raji and Daudi cells were opsonized with C3b, iC3b and C3d fragments by using purified complement components. The sensitivity of C3-opsonized cells to lysis mediated by low density blood lymphocytes was studied. Raji and Daudi cells carrying C3b or C3d fragments were lysed with similar efficiencies as the nonopsonized cells. The presence of iC3b on the target surface imposed elevated NK sensitivity. The iC3b-mediated enhancement of NK lysis was inhibited when iC3b fragments or rabbit anti-human C3 antibodies were included into the lytic assays. These results indicate that the iC3b fragments fixed on the targets bind to the CR3 on the lymphocytes. Results obtained in immobilized conjugate-lytic assays showed that iC3b-opsonized targets interact more readily with the lymphocytes. This was reflected by the elevated proportion of lymphocytes that were bound to the iC3b-carrying targets. The proportions of conjugates in which target damage occurred were similar with the control and with the iC3b-carrying cells. It seems therefore that opsonization of targets with iC3b leads to recruitment of effector lymphocytes due to contact with their CR3. However, once the effector-target contact is established, the triggering of lytic function does not seem to be influenced by the iC3b/CR3 bridge. 

  • 193.
    Ricklin, Daniel
    et al.
    Univ Penn, USA.
    Sfyroera, Georgia
    Univ Penn, USA.
    Reis, Edimara
    Univ Penn, USA.
    Chen, Hui
    Univ Penn, USA.
    Wu, Emilia
    Univ Minnesota, USA.
    Kaznessis, Yiannis
    Univ Minnesota, USA.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Nilsson, Bo
    Uppsala University.
    Lambris, John D.
    Univ Penn, USA.
    Rare loss-of-function mutation in C3 provides insight into molecular and pathophysiological determinants of alternative pathway activity2015Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 67, nr 1, s. 174-174Artikel i tidskrift (Övrigt vetenskapligt)
  • 194.
    Rosengren-Holmberg, Jenny P.
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Swedish Natl Forens Ctr, Sweden.
    Andersson, Jonas
    Univ Uppsala Hosp, Sweden.
    Smith, James R.
    Univ Portsmouth, UK.
    Alexander, Cameron
    Univ Nottingham, UK.
    Alexander, Morgan R.
    Univ Nottingham, UK.
    Tovar, Guenter
    Univ Stuttgart, Germany;Fraunhofer Inst Interfacial Engn & Biotechnol, Germany.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Univ Uppsala Hosp, Sweden.
    Nicholls, Ian A.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Heparin molecularly imprinted surfaces for the attenuation of complement activation in blood2015Ingår i: Biomaterials Science, ISSN 2047-4830, E-ISSN 2047-4849, Vol. 3, nr 8, s. 1208-1217Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Heparin-imprinted synthetic polymer surfaces with the ability to attenuate activation of both the complement and the coagulation system in whole blood were successfully produced. Imprinting was achieved using a template coated with heparin, a highly sulfated glycosaminoglycan known for its anticoagulant properties. The N,N'-diacryloylpiperazine-methacrylic acid copolymers were characterized using goniometry, AFM and XPS. The influence of the molecular imprinting process on morphology and template rebinding was demonstrated by radioligand binding assays. Surface hemocompatibility was evaluated using human whole blood without anticoagulants followed by measurement of complement activation markers C3a and sC5b-9 and platelet consumption as a surrogate coagulation activation marker. The observed low thrombogenicity of this copolymer combined with the attenuation of complement activation induced by the molecular imprint offer potential for the development of self-regulating surfaces with important potential clinical applications. We propose a mechanism for the observed phenomena based upon the recruitment of endogenous sulfated glycosaminoglycans with heparin-like activities.

  • 195.
    Rosengren-Holmberg, Jenny P.
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nicholls, Ian A.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Synthetic receptors for BSA and their application in a novel ELISA-assay2001Konferensbidrag (Refereegranskat)
  • 196.
    Rosengren-Holmberg, Jenny P.
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nicholls, Ian Alan
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Molecularly imprinted polymer synthetic receptors for bovine serum albumin2000Konferensbidrag (Refereegranskat)
  • 197.
    Rosengren-Holmberg, Jenny P.
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nicholls, Ian Alan
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    The development of quasi-2-dimensional synthetic receptors and their application in a novel ELISA-assay2000Konferensbidrag (Refereegranskat)
  • 198. Rönnelid, J
    et al.
    Gunnarsson, I
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson, Bo
    Correlation between anti-C1q and immune conglutinin levels, but not between levels of antibodies to the stucturally related autoantigens C1q and type II collagen in SLE or RA1997Ingår i: Journal of autoimmunity, Vol. 10, s. 415-423Artikel i tidskrift (Refereegranskat)
  • 199.
    Rönnelid, J
    et al.
    Uppsala University ; Karolinska Institute.
    Tejde, A
    Uppsala University.
    Mathsson, L
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Uppsala University.
    Nilsson, Bo
    Uppsala University.
    Immune complexes from SLE sera induce IL-10 production by a Fc-RII-dependent mechanism: A possible vicious circle maintaining B cell hyperactivity in SLE2003Ingår i: Annals of the Rheumatic Diseases, ISSN 0003-4967, E-ISSN 1468-2060, Vol. 62, s. 37-42Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Background: Raised interleukin (IL)6 and IL10 levels are thought to contribute to the pathogenesis of systemic lupus erythematosus (SLE) by enhancing autoantibody production and immune complex (IC) formation. These immune complexes can then stimulate cellular reactions through Fc and complement receptors.

    Objective: To investigate whether circulating SLE ICs stimulate type 2 cytokine production.

    Methods: Twenty serum samples from patients with active SLE were compared with sera from 18 healthy controls. Sera and polyethylene glycol (PEG) precipitates from sera were added to peripheral blood mononuclear cell (PBMC) cultures, and the production of IL10 and IL6 was investigated by enzyme linked immunospot assay (ELISPOT) and enzyme linked immunosorbent assay (ELISA). Fc gamma receptor (FcγR) antibodies were used in blocking experiments, and flow cytometry was used to assess the correlation between monocyte FcγR expression and IC-induced cytokine production.

    Results: Ten per cent dilutions of the SLE sera induced a significantly increased number of IL10-producing cells in comparison with control sera (median, 11.75 v 1.25 spot forming cells/50 000 PBMC; p<0.0001). PEG precipitates from SLE sera also induced significantly increased levels of IL10 (p=0.016) and IL6 (p=0.042) in comparison with control PEG precipitates. IL10 production induced by SLE PEG precipitates or by artificial ICs could be blocked by anti-FcγRII antibodies, and the FcγRII expression on CD14+ monocytes correlated with the IC-induced production of IL10 and IL6.

    Conclusions: SLE sera stimulate IL10 and IL6 production from PBMC, and this effect is at least partly explained by precipitable ICs acting through FcγRII. This effect provides a possible mechanism for the enhanced production of IL10 in SLE, whereby B cell activation, antibody production, IC stimulated monocytes/macrophages, and type 2 cytokines create a vicious cycle that may help to maintain B cell hyperactivity in SLE.

  • 200.
    Rönnelid, Johan
    et al.
    Uppsala Univ, Unit Clin Immunol, Uppsala, Sweden.
    Åhlin, Erik
    Uppsala Univ, Unit Clin Immunol, Uppsala, Sweden.
    Nilsson, Bo
    Uppsala Univ, Unit Clin Immunol, Uppsala, Sweden.
    Nilsson Ekdahl, Kristina
    Uppsala Univ, Unit Clin Immunol, Uppsala, Sweden.
    Mathsson, Linda
    Uppsala Univ, Unit Clin Immunol, Uppsala, Sweden.
    Immune complex-mediated cytokine production is regulated by classical complement activation both in vivo and in vitro2008Ingår i: Advances in experimental medicine and biology, Vol. 632, s. 187-201Artikel, forskningsöversikt (Övrigt vetenskapligt)
    Abstract [en]

    Immune complexes (IC) induce a number of cellular functions, including the enhancement of cytokine production from monocytes, macrophages and plasmacytoid dendritic cells. The range and the composition of cytokines induced by IC in vitro is influenced by the availability of an intact classical complement cascade during cell Culture, as we have showed in our studies on artificial IC and on cryoglobulins purified from patients with lymphoproliferative diseases. When IC purified from systemic lupus erythematosus sera were used to stimulate in vitro cytokine production, the amount of circulating IC and IC-induced cytokine levels depended both on in vivo classical complement function as well as on the occurrence of anti-SSA, but not on anti-dsDNA or any other autoantibodies. Collectively these findings illustrate that studies on IC-induced cytokine production in vitro requires stringent cell culture conditions with complete control and definition of access to an intact classical complement pathway in the cell cultures. If IC are formed in vivo, the results have to be interpreted in the context of classical complement activation in vivo as well as the occurrence of IC-associated autoantibodies at the time of serum sampling.

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