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  • 101.
    Lindblom, Rickard P. F.
    et al.
    Karolinska Institutet;Univ Uppsala Hosp;Karolinska Univ Hosp.
    Berg, Alexander
    Karolinska Institutet.
    Ström, Mikael
    Karolinska Institutet.
    Aeinehband, Shahin
    Karolinska Institutet.
    Dominguez, Cecilia A.
    Karolinska Institutet.
    Al Nimer, Faiez
    Karolinska Institutet.
    Abdelmagid, Nada
    Karolinska Institutet.
    Heinig, Matthias
    Max Delbruck Ctr Mol Med, Germany.
    Zelano, Johan
    Karolinska Institutet.
    Harnesk, Karin
    Karolinska Institutet.
    Hubner, Norbert
    Max Delbruck Ctr Mol Med, Germany.
    Nilsson, Bo
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Uppsala University.
    Diez, Margarita
    Karolinska Institutet.
    Cullheim, Staffan
    Karolinska Institutet.
    Piehl, Fredrik
    Karolinska Institutet.
    Complement receptor 2 is up regulated in the spinal cord following nerve root injury and modulates the spinal cord response2015Ingår i: Journal of Neuroinflammation, ISSN 1742-2094, E-ISSN 1742-2094, Vol. 12, artikel-id 192Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Background: Activation of the complement system has been implicated in both acute and chronic states of neurodegeneration. However, a detailed understanding of this complex network of interacting components is still lacking. Methods: Large-scale global expression profiling in a rat F2(DAxPVG) intercross identified a strong cis-regulatory influence on the local expression of complement receptor 2 (Cr2) in the spinal cord after ventral root avulsion (VRA). Expression of Cr2 in the spinal cord was studied in a separate cohort of DA and PVG rats at different time-points after VRA, and also following sciatic nerve transection (SNT) in the same strains. Consequently, Cr2(-/-) mice and Wt controls were used to further explore the role of Cr2 in the spinal cord following SNT. The in vivo experiments were complemented by astrocyte and microglia cell cultures. Results: Expression of Cr2 in naive spinal cord was low but strongly up regulated at 5-7 days after both VRA and SNT. Levels of Cr2 expression, as well as astrocyte activation, was higher in PVG rats than DA rats following both VRA and SNT. Subsequent in vitro studies proposed astrocytes as the main source of Cr2 expression. A functional role for Cr2 is suggested by the finding that transgenic mice lacking Cr2 displayed increased loss of synaptic nerve terminals following nerve injury. We also detected increased levels of soluble CR2 (sCR2) in the cerebrospinal fluid of rats following VRA. Conclusions: These results demonstrate that local expression of Cr2 in the central nervous system is part of the axotomy reaction and is suggested to modulate subsequent complement mediated effects.

  • 102. Lundgren, Brita A
    et al.
    Rorsman, Fredrik
    Portela-Gomes, G
    Grimelius, Lars
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Nilsson, Bo
    Ekwall, Olof
    Identification of complement C3 as an autoantigen in inflammatory bowel disease2010Ingår i: Journal of Gastroenterology and Hepatology, ISSN 0815-9319, E-ISSN 1440-1746, Vol. 2, nr 4, s. 429-436Artikel i tidskrift (Refereegranskat)
  • 103. Mangsbo, Sara
    et al.
    Sanchez, Javier
    Anger, Kerstin
    Lambris, John
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Loskog, Angelica
    Nilsson, Bo
    Tötterman, Thomas
    Complement activation by CpG in a human whole blood loop system: mechanisms and immunomodulatory effects2009Ingår i: Journal of Immunology, ISSN 0022-1767, E-ISSN 1550-6606, Vol. 183, nr 10, s. 6724-6732Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Phosphorothioate oligodeoxynucleotides can activate complement, and experimental murine studies have revealed differential effects upon simultaneous TLR stimulation and complement activation compared with either event alone. We set out to investigate the immune stimulatory effects of CpG 2006 in fresh non-anticoagulated human blood with or without presence of active complement. We also sought to elucidate the mechanism behind complement activation upon stimulation with phosphorothioate CpG 2006. In a human blood loop system, both backbone and sequence-specific effects by CpG were counteracted by selective inhibition of C3. Furthermore, DNA backbone-mediated CD40 and CD83 expression on monocytes and sequence-specific IL-6 and TNF production were reduced by complement inhibition. CpG-induced complement activation occurred via either the classical or the alternative pathway and deposits of both IgM and properdin, two activators of complement, were detected on CpG after incubation with EDTA plasma. Quartz crystal microbalance with dissipation monitoring demonstrated alternative pathway convertase build-up onto CpG as a likely pathway to initiate and sustain complement activation. Specific inhibition of C3 suppressed CpG 2006 uptake into monocytes indicating that C3 fragments are involved in CpG internalization. The interplay between complement and TLR9 signaling demonstrated herein warrants further investigation.

  • 104. Markiewski, M.M
    et al.
    Nilsson, Bo
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Mollnes, T E
    Lambris, J D
    Complement and Coagulation: Strangers or Partners in Crime?2007Ingår i: Trends in Immunology, Vol. 28, nr 4, s. 184-192Artikel i tidskrift (Refereegranskat)
  • 105. Mathsson, L
    et al.
    Tejde, A
    Carlson, K
    Höglund, M
    Nilsson, Bo
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Rönnelid, J
    Cryoglobulin-induced cytokine production via Fc-gamma-RIIa: inverse effects of complement blockade on the production of TNF-alfa and IL-10. Implications for the growth of malignant B-cell clones2005Ingår i: British journal of haematology, Vol. 129, nr 6, s. 830-838Artikel i tidskrift (Refereegranskat)
  • 106. Moberg, L
    et al.
    Johansson, H
    Luknius, A
    Berne, C
    Foss, A
    Källen, R
    Østraat, O
    Salmela, K
    Tibell, A
    Tufveson, G
    Elgue, G
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Larsson, R
    Korsgren, O
    Nilsson, Bo
    Expression and secretion of tissue factor in the islets of Langerhans: A likely explanation for the development of thrombotic reactions in clinical islet transplantation (IBMIR) in vitro2002Ingår i: Lancet, Vol. 360, s. 2039-2045Artikel i tidskrift (Refereegranskat)
  • 107.
    Mohebnasab, Maedeh
    et al.
    Univ Penn, USA.
    Eriksson, Oskar
    Uppsala University, Sweden.
    Persson, Barbro
    Uppsala University, Sweden.
    Sandholm, Kerstin
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Mohlin, Camilla
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Huber-Lang, Markus
    Univ Hosp Ulm, Germany.
    Keating, Brendan J.
    Univ Penn, USA.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University, Sweden.
    Nilsson, Bo
    Uppsala University, Sweden.
    Current and Future Approaches for Monitoring Responses to Anti-complement Therapeutics2019Ingår i: Frontiers in Immunology, ISSN 1664-3224, E-ISSN 1664-3224, Vol. 10, s. 1-13, artikel-id 2539Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Aberrations in complement system functions have been identified as either direct or indirect pathophysiological mechanisms in many diseases and pathological conditions, such as infections, autoimmune diseases, inflammation, malignancies, and allogeneic transplantation. Currently available techniques to study complement include quantification of (a) individual complement components, (b) complement activation products, and (c) molecular mechanisms/function. An emerging area of major interest in translational studies aims to study and monitor patients on complement regulatory drugs for efficacy as well as adverse events. This area is progressing rapidly with several anti-complement therapeutics under development, in clinical trials, or already in clinical use. In this review, we summarized the appropriate indications, techniques, and interpretations of basic complement analyses, exemplified by a number of clinical disorders.

  • 108.
    Mohlin, Camilla
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Johansson, Kjell
    Örebro University.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Complement factor involvement during experimental AMD2015Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 67, nr 1, s. 163-163Artikel i tidskrift (Övrigt vetenskapligt)
  • 109.
    Mohlin, Camilla
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Petrus-Reurer, S.
    Karolinska Institutet;Karolinska Univ Hosp.
    Lanner, F.
    Karolinska Institutet;Karolinska Univ Hosp.
    Sandholm, Kerstin
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Kvanta, A.
    Karolinska Institutet.
    Nilsson, B.
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Complement system proteins in human embryonic stem cell-derived retinal pigment epithelial cells co-cultured with or without porcine retina2017Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 89, s. 162-163Artikel i tidskrift (Övrigt vetenskapligt)
  • 110.
    Mohlin, Camilla
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Petrus-Reurer, Sandra
    Karolinska Institutet;Karolinska University Hospital.
    Lanner, Fredrik
    Karolinska Institutet;Karolinska University Hospital.
    Sandholm, Kerstin
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Nilsson, Per H.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Univ Oslo, Norway.
    Nilsson, Bo
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Is the polarized secretion of complement factor H of importance in age-related macular degeneration?2018Ingår i: Investigative Ophthalmology and Visual Science, ISSN 0146-0404, E-ISSN 1552-5783, Vol. 59, nr 9Artikel i tidskrift (Övrigt vetenskapligt)
  • 111.
    Mohlin, Camilla
    et al.
    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).
    Kvanta, Anders
    Karolinska institutet.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala university.
    Johansson, Kjell
    Örebro university.
    A model to study complement involvement in experimental retinal degeneration.2018Ingår i: Upsala Journal of Medical Sciences, ISSN 0300-9734, E-ISSN 2000-1967, Vol. 123, nr 1, s. 28-42Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    BACKGROUND: The complement system (CS) plays a role in the pathogenesis of a number of ocular diseases, including diabetic retinopathy (DR), glaucoma, uveitis, and age-related macular degeneration (AMD). Given that many of the complex eye-related degenerative diseases have limited treatment opportunities, we aimed to mimic the in vivo retinal degenerative process by developing a relevant co-culture system.

    METHOD AND MATERIALS: The adult porcine retina was co-cultured with the spontaneously arising human retinal pigment epithelial cells-19 (ARPE-19).

    RESULTS: Inflammatory activity was found after culture and included migrating microglial cells, gliosis, cell death, and CS activation (demonstrated by a minor increase in the secreted anaphylotoxin C3a in co-culture). CS components, including C1q, C3, C4, soluble C5b-9, and the C5a receptor, were expressed in the retina and/or ARPE cells after culture. C1q, C3, and CS regulators such as C4 binding protein (C4BP), factor H (CFH), and factor I (CFI) were secreted after culture.

    DISCUSSION: Thus, our research indicates that this co-culturing system may be useful for investigations of the CS and its involvement in experimental neurodegenerative diseases.

  • 112.
    Mohlin, Camilla
    et al.
    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).
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University, Sweden.
    Nilsson, Bo
    Uppsala University, Sweden.
    The link between morphology and complement in ocular disease2017Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 89, s. 84-99Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    The complement system is a vital component of the immune-priveliged human eye that is always active at a low-grade level, preventing harmful intraocular injuries caused by accumulation of turnover products and controlling pathogens to preserve eye homeostasis and vision. The complement system is a double-edged sword that is essential for protection but may also become harmful and contribute to eye pathology. Here, we review the evidence for the involvement of complement system dysregulation in age-related macular degeneration, glaucoma, uveitis, and neuromyelitis optica, highlighting the relationship between morphogical changes and complement system protein expression and regulation in these diseases. The potential benefits of complement inhibition in age-related macular degeneration, glaucoma, uveitis, and neuromyelitis optica are abundant, as are those of further research to improve our understanding of complement-mediated injury in these diseases.

  • 113.
    Moll, Guido
    et al.
    Karolinska Institutet;Karolinska University Hospital Huddinge.
    Alm, Jessica J.
    Karolinska University Hospital Huddinge.
    Davies, Lindsay C.
    Cardiff University, UK.
    von Bahr, Lena
    Karolinska University Hospital Huddinge.
    Heldring, Nina
    Karolinska University Hospital Huddinge.
    Stenbeck-Funke, Lillemor
    Uppsala University.
    Hamad, Osama A.
    Uppsala University.
    Hinsch, Robin
    Karolinska University Hospital Huddinge.
    Ignatowicz, Lech
    Locke, Matthew
    Cardiff University, UK.
    Lönnies, Helena
    Karolinska Institutet;Karolinska University Hospital Huddinge.
    Lambris, John D.
    University of Pennsylvania School of Medicine, USA.
    Teramura, Yuji
    Uppsala University;The University of Tokyo, Japan.
    Nilsson Ekdahl, Kristina
    Uppsala University.
    Nilsson, Bo
    Uppsala University.
    Le Blanc, Katarina
    Karolinska Institutet;Karolinska University Hospital Huddinge.
    Do Cryopreserved Mesenchymal Stromal Cells Display Impaired Immunomodulatory and Therapeutic Properties?2014Ingår i: Stem Cells, ISSN 1066-5099, E-ISSN 1549-4918, Vol. 32, nr 9, s. 2430-2442Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    We have recently reported that therapeutic mesenchymal stromal cells (MSCs) have low engraftment and trigger the instant blood mediated inflammatory reaction (IBMIR) after systemic delivery to patients, resulting in compromised cell function. In order to optimize the product, we compared the immunomodulatory, blood regulatory, and therapeutic properties of freeze-thawed and freshly harvested cells. We found that freeze-thawed MSCs, as opposed to cells harvested from continuous cultures, have impaired immunomodulatory and blood regulatory properties. Freeze-thawed MSCs demonstrated reduced responsiveness to proinflammatory stimuli, an impaired production of anti-inflammatory mediators, increased triggering of the IBMIR, and a strong activation of the complement cascade compared to fresh cells. This resulted in twice the efficiency in lysis of thawed MSCs after 1 hour of serum exposure. We found a 50% and 80% reduction in viable cells with freshly detached as opposed to thawed in vitro cells, indicating a small benefit for fresh cells. In evaluation of clinical response, we report a trend that fresh cells, and cells of low passage, demonstrate improved clinical outcome. Patients treated with freshly harvested cells in low passage had a 100% response rate, twice the response rate of 50% observed in a comparable group of patients treated with freeze-thawed cells at higher passage. We conclude that cryobanked MSCs have reduced immunomodulatory and blood regulatory properties directly after thawing, resulting in faster complement-mediated elimination after blood exposure. These changes seem to be paired by differences in therapeutic efficacy in treatment of immune ailments after hematopoietic stem cell transplantation. Stem Cells 2014;32:2430–2442

  • 114. Moll, Guido
    et al.
    Jitschin, R
    von Bahr, Lena
    Rasmusson-Duprez, Ida
    Sundberg, Berit
    Lönnies, Lena
    Elgue, Graciela
    Nilsson Ekdahl, Kristina
    Department of Immunology, Genetics and Pathology, Rudbeck Laboratory, Uppsala University.
    Mougliakakos, D
    Lambris, John
    Ringden, O
    Le Blanc, Katarina
    Nilsson, Bo
    Mesenchymal Stromal Cells Engage Complement and Complement Receptor Bearing Innate Effector Cells to Modulate Immune Responses (Open Access)2011Ingår i: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 6, nr 7, s. e21703-Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Infusion of human third-party mesenchymal stromal cells (MSCs) appears to be a promising therapy for acute graft-versus-host disease (aGvHD). To date, little is known about how MSCs interact with the body's innate immune system after clinical infusion. This study shows, that exposure of MSCs to blood type ABO-matched human blood activates the complement system, which triggers complement-mediated lymphoid and myeloid effector cell activation in blood. We found deposition of complement component C3-derived fragments iC3b and C3dg on MSCs and fluid-phase generation of the chemotactic anaphylatoxins C3a and C5a. MSCs bound low amounts of immunoglobulins and lacked expression of complement regulatory proteins MCP (CD46) and DAF (CD55), but were protected from complement lysis via expression of protectin (CD59). Cell-surface-opsonization and anaphylatoxin-formation triggered complement receptor 3 (CD11b/CD18)-mediated effector cell activation in blood. The complement-activating properties of individual MSCs were furthermore correlated with their potency to inhibit PBMC-proliferation in vitro, and both effector cell activation and the immunosuppressive effect could be blocked either by using complement inhibitor Compstatin or by depletion of CD14/CD11b-high myeloid effector cells from mixed lymphocyte reactions. Our study demonstrates for the first time a major role of the complement system in governing the immunomodulatory activity of MSCs and elucidates how complement activation mediates the interaction with other immune cells.

  • 115. Moll, Guido
    et al.
    Rasmusson-Duprez, Ida
    von Bahr, Lena
    Conolly-Andersen, Ann-Marie
    Elgue, Graciela
    Funke, Lillemor
    Hamad, Osama
    Lönnies, Helena
    Magnusson, Peetra
    Sanchez, Javier
    Teramura, Yuji
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Ringden, Olof
    Korsgren, Olle
    Nilsson, Bo
    LeBlanc, Katarina
    Are therapeutic human mesenchymal stromal cells compatible with human blood?2012Ingår i: Stem Cells, ISSN 1066-5099, E-ISSN 1549-4918, Vol. 30, nr 7, s. 1565-1574Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Multipotent mesenchymal stromal cells (MSCs) are tested in numerous clinical trials. Questions have been raised concerning fate and function of these therapeutic cells after systemic infusion. We therefore asked whether culture-expanded human MSCs elicit an innate immune attack, termed instant blood-mediated inflammatory reaction (IBMIR), which has previously been shown to compromise the survival and function of systemically infused islet cells and hepatocytes. We found that MSCs expressed hemostatic regulators similar to those produced by endothelial cells but displayed higher amounts of prothrombotic tissue/stromal factors on their surface, which triggered the IBMIR after blood exposure, as characterized by formation of blood activation markers. This process was dependent on the cell dose, the choice of MSC donor, and particularly the cell-passage number. Short-term expanded MSCs triggered only weak blood responses in vitro, whereas extended culture and coculture with activated lymphocytes increased their prothrombotic properties. After systemic infusion to patients, we found increased formation of blood activation markers, but no formation of hyperfibrinolysis marker D-dimer or acute-phase reactants with the currently applied dose of 1.0–3.0 × 106 cells per kilogram. Culture-expanded MSCs trigger the IBMIR in vitro and in vivo. Induction of IBMIR is dose-dependent and increases after prolonged ex vivo expansion. Currently applied doses of low-passage clinical-grade MSCs elicit only minor systemic effects, but higher cell doses and particularly higher passage cells should be handled with care. This deleterious reaction can compromise the survival, engraftment, and function of these therapeutic cells.

  • 116.
    Nicholls, Ian A.
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Karlsson, Björn C. G.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Andersson, Håkan S.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Golker, Kerstin
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Henschel, Henning
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Olsson, Gustaf D.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    O'Mahony, John
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Orozovic, Kanita
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Rosengren, Annika M.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Rosengren-Holmberg, Jenny P.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Shoravi, Siamak
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Wiklander, Jesper G.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Wikman, Susanne
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Biomimetic Polymer Design2009Konferensbidrag (Refereegranskat)
  • 117.
    Nicholls, Ian A.
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Moledcular Imprints2009Patent (Övrig (populärvetenskap, debatt, mm))
  • 118. Nilsson, B
    et al.
    Grossberger, D
    Nilsson Ekdahl, Kristina
    University Hospital, Uppsala.
    Riegert, P
    Becherer, J D
    Nilsson, U R
    Conformational differences between surface-bound and fluid-phase C3. Epitope mapping by cDNA expression1992Ingår i: Biochemical journal, Vol. 282, s. 715-721Artikel i tidskrift (Refereegranskat)
  • 119. Nilsson, B
    et al.
    Hong, J
    Larsson, R
    Elgue, G
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Sahu, A
    Lambris, J D
    Compstatin inhibits complement and cellular activation in whole blood in models for extracorpereal circulation1998Ingår i: Blood, Vol. 92, s. 1661-1667Artikel i tidskrift (Refereegranskat)
  • 120. Nilsson, B
    et al.
    Nilsson Ekdahl, Kristina
    Uppsala university.
    Components of the alternative pathway1988Ingår i: The Complement System / [ed] K. Rother & G. Till, Springer, 1988, 1, s. 23-49Kapitel i bok, del av antologi (Övrigt vetenskapligt)
  • 121. Nilsson, Bo
    et al.
    Andersson, Jonas
    Neff, Jeniffer
    Caldwell, Karin
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Elutable Surface coatings2005Patent (Övrig (populärvetenskap, debatt, mm))
  • 122.
    Nilsson, Bo
    et al.
    Uppsala University.
    Asif, Sana
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Manell, Elin
    Swedish University of Agricultural Sciences.
    Biglarnia, Alireza
    Skåne University Hospital.
    Jensen-Waern, Marianne
    Swedish University of Agricultural Sciences.
    Teramura, Yuji
    Uppsala University;Univ Tokyo, Japan.
    A protective role of complement regulators linked to a PEG phospholipid construct in reducing ischemic reperfusion injury in transplantation2017Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 89, s. 208-208Artikel i tidskrift (Övrigt vetenskapligt)
  • 123.
    Nilsson, Bo
    et al.
    Uppsala University.
    Hamad, Osama
    Uppsala University.
    Ahlström, Håkan
    Uppsala University.
    Kullberg, Joel
    Uppsala University.
    Johansson, Lars
    Uppsala University.
    Lindhagen, Lars
    Uppsala University.
    Haenni, Arvo
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Uppsala University.
    Lind, Lars
    Uppsala University.
    C3 and C4 are strongly related to adipose tissue variables and cardiovascular risk factors2014Ingår i: European Journal of Clinical Investigation, ISSN 0014-2972, E-ISSN 1365-2362, Vol. 44, nr 6, s. 587-596Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Background In several reports, C3 and C4 have been linked to diabetes and cardiovascular disease (CVD). Here, we investigate this link and the degree of C3 activation in elderly individuals. Methods In this study, C3 and C4 and the activation fragment C3a-desArg were analysed in 1016 subjects aged 70, in which blood pressure, lipid variables and fasting blood glucose were assessed. Results C3 levels were related to all the investigated classical cardiovascular risk factors and the metabolic syndrome (BMI, waist circumference, fat distribution, blood pressure, blood glucose levels, TG) except total cholesterol and LDL cholesterol in a highly significant fashion (Spearman up to 0,5; P<0.0001). C4 and C3a-desArg were associated in the same fashion but less significantly, while the ratios C4/C3 or C3a-desArg/C3 were not, indicating thatthe association was not directly related to complement activation. The levels C3 and to a lesser degree C4 and C3a-desArg were associated particularly with CRP, but also with E-selectin and ICAM-1. In addition, C3 and C4 levels were shown to decline significantly in 15 female subjects enrolled in a weight-reduction programme over 4 months. Conclusion A strong relation between C3, C4 and C3a-desArg levels, adipose tissue and risk factors of CVD was established. The data support that theadipose tissue produces complement components and generates initiators of inflammation, such as C3a and C5a, able to trigger a cyto/chemokine response, in proportion to the amount of adipose tissue. This corroborates the concept that complement contributes to the low-grade inflammation associated with obesity.

  • 124. Nilsson, Bo
    et al.
    Korsgren, Olle
    Lambris, John
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    Can cells and biomaterials in therapeutic medicine be shielded from innate immune recognition2010Ingår i: Trends in immunology, ISSN 1471-4906, E-ISSN 1471-4981, Vol. 31, nr 1, s. 32-38Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Biomaterials (e.g. polymers, metals, or ceramics), cell and cell cluster (e.g. pancreatic islets) transplantation are beginning to offer novel treatment modalities for some otherwise intractable diseases. The innate immune system is involved in incompatibility reactions that occur when biomaterials or cells are introduced into the blood circulation. In particular, the complement, coagulation and contact systems are involved in the recognition of biomaterials and cells, eliciting activation of platelets and leukocytes. Such treatments are associated with anaphylactoid and thrombotic reactions, inflammation, and rejection of biomaterials and cells, leading to treatment failures and adverse reactions. We discuss here the new technologies that are being developed to shield the biomaterial and cell surfaces from recognition by the innate immune system.

  • 125.
    Nilsson, Bo
    et al.
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV. Uppsala University.
    Complement Diagnostics: Concepts, Indications, and Practical Guidelines2012Ingår i: Clinical & Developmental Immunology, ISSN 1740-2522, E-ISSN 1740-2530, artikel-id 962702Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Aberrations in the complement system have been shown to be direct or indirect pathophysiological mechanisms in a number of diseases and pathological conditions such as autoimmune disease, infections, cancer, allogeneic and xenogeneic transplantation, and inflammation. Complement analyses have been performed on these conditions in both prospective and retrospective studies and significant differences have been found between groups of patients, but in many diseases, it has not been possible to make predictions for individual patients because of the lack of sensitivity and specificity of many of the assays used. The basic indications for serological diagnostic complement analysis today may be divided into three major categories: (a) acquired and inherited complement deficiencies; (b) disorders with complement activation; (c) inherited and acquired C1INH deficiencies. Here, we summarize indications, techniques, and interpretations for basic complement analyses and present an algorithm, which we follow in our routine laboratory.

  • 126. Nilsson, Bo
    et al.
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Components of the alternative pathway1998Ingår i: The complement system / [ed] Klaus Rother, Gerd O Till, Gertrud Maria Hänsch, Springer, 1998, 2, s. 23-49Kapitel i bok, del av antologi (Refereegranskat)
    Abstract [en]

    Its key role in life preserving functions such as host defense against infections or inflammatory reactions has put the serum complement system at the forefront of biomedical research in both the laboratory and the clinic. This book describes the basic regulation of the complement systems, presenting its biological functions, the target cell receptors for such functions and their interactions with ligands to induce specific cellular responses. The biological functions are also discussed in the context of more complex conditions, for example in host defense, chronic inflammatory disease, graft rejection as well as in adverse reactions to drugs or to artificial surfaces. The book offers the present state-of-the-art compiled by leading experts in the field. Extensive literature citations offer easy access to those interested in more detail.

  • 127. Nilsson, Bo
    et al.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV.
    The tick-over theory revisited: Is C3 a contact-activated protein?2012Ingår i: Immunobiology, ISSN 0171-2985, E-ISSN 1878-3279, Vol. 217, nr 11, s. 1106-1110Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    The tick-over theory was first introduced in the 1970s to explain the presence of the initial C3b molecules, which are able to trigger complement activation by the alternative pathway in human plasma under physiological conditions. After the identification of the thioester, the predominant hypothesis has been that this bond is hydrolyzed at a slow but constant rate by nucleophilic attack by H2O, leading to the generation of C3(H2O). Here we put forward the hypothesis that the rate of hydrolysis of C3 to C3(H2O) may be greatly accelerated by the interaction between C3 and a number of biological and artificial interfaces, including gas bubbles, biomaterial surfaces and different lipid surfaces and complexes. We therefore propose that C3 should preferentially be regarded as a contact activated protein rather than a target for passive, random hydrolysis in the fluid phase. (C) 2012 Elsevier GmbH. All rights reserved.

  • 128. Nilsson, Bo
    et al.
    Nilsson Ekdahl, Kristina
    Department of Clinical Immunology and Transfusion Medicine, University Hospital, Uppsala.
    Avila, D
    Nilsson, U R
    Lambris, J D
    Neoantigens in complement component C3 as detected by monoclonal antibodies. Mapping of the recognized epitopes by synthetic peptides1990Ingår i: Biochemical Journal, ISSN 0264-6021, E-ISSN 1470-8728, Vol. 268, nr 1, s. 55-61Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The different fragments of the third complement component, C3, generated upon complement activation/inactivation have the ability to bind to several other complement components and receptors as well as to proteins of foreign origin. These multiple reactivities of C3 fragments are associated with a series of conformational changes occurring in the C3 molecule during its degradation. The conformations acquired by the different C3 fragments are also associated with the exposure of neoantigenic epitopes that are specific for (a) particular fragment(s). In order to study these epitopes and thus the conformational changes occurring in C3, monoclonal antibodies (mAbs) recognizing such epitopes were produced in Balb/c mice after immunization with denatured human C3. Two of the three antibodies (7D84.1 and 7D264.6) presented in this study recognized predominantly surface-bound iC3b, and one mAb (7D323.1) recognized both surface-bound and fluid-phase iC3b. Although none of the mAbs recognized any other fluid-phase C3 fragment, all three antibodies detected micro-titre-plate-fixed C3b and iC3b, but not C3c or C3d. In addition to the reaction with human C3, mAb 7D323.1 also bound to micro-titre-plate-fixed rabbit C3. The epitopes recognized by the three mAbs were further localized by using synthetic peptides that were designed on the basis of the differential binding of the mAbs to the C3 fragments. All three antibodies reacted with C3-(924-965)-peptide, which represents the region of C3 between the kallikrein-cleavage site (923-924) and the elastase-cleavage site (965-966). On the basis of the binding of the mAbs to five different overlapping peptides spanning the region between residues 924 and 965 of the human C3 sequence, and the sequence similarity between human C3 and rabbit C3 within this area, the epitopes recognized by these antibodies are mapped. The contribution of the individual amino acid residues in the formation of the epitopes is discussed. 

  • 129.
    Nilsson, Bo
    et al.
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Uppsala University.
    Kemper, Claudia
    King's College London, UK.
    Mollnes, Tom Eirik
    Nordland Hospital, Norway;University of Tromsø, Norway.
    Preface. 15th European Meeting on Complement in Human Disease 2015, Uppsala, Sweden.2015Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 67, nr 1, s. 1-2Artikel i tidskrift (Övrigt vetenskapligt)
  • 130.
    Nilsson, Bo
    et al.
    Uppsala University.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakultetsnämnden för naturvetenskap och teknik, Institutionen för naturvetenskap, NV. Uppsala University.
    Korsgren, Olle
    Uppsala University.
    Control of IBMIR (Instant Blood-Mediated Inflammatory Reaction) to improve islets of Langerhans engraftement2011Ingår i: Current Opinion in Organ Transplantation, ISSN 1087-2418, E-ISSN 1531-7013, Vol. 16, nr 6, s. 620-626Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Purpose of review Transplantation of islets of Langerhans is an emerging treatment procedure for patients with severe type 1 diabetes, but despite recent progress the procedure is associated with massive tissue loss caused by an inflammatory reaction termed instant blood-mediated inflammatory reaction (IBMIR). This reactioninvolves activation of the complement and coagulation cascades, ultimately resulting in clot formation and infiltration of leukocytes into the islets, which leadsto disruption of islet integrity and islet destruction. Recent findings In this review we discuss basic mechanisms underlying the IBMIR and emerging strategies for therapeutic regulation of the IBMIR. These include the use ofselective inhibitors of the coagulation and complement systems, different procedures to coat the surface of the islets as well as the development ofcomposite islet-endothelial cell grafts. Summary The IBMIR is a major cause of tissue loss in clinical islet transplantation, and most likely in other cell therapies in which cells are exposed to blood. Thus, it is an obvious target for therapeutic intervention. Due to its complexity, it is necessary to use different strategies to control the IBMIR.

  • 131. Nilsson, Bo
    et al.
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Mollnes, T E
    Lambris, J D
    The role of complement in biomaterial-induced inflammation2006Ingår i: Molecular immunology, Vol. 44, nr 1-3, s. 82-94Artikel i tidskrift (Refereegranskat)
  • 132. Nilsson, Bo
    et al.
    Nilsson Ekdahl, Kristina
    University Hospital, Uppsala.
    Sjöholm, A
    Nilsson, U R
    Sturfelt, G
    Detection and characterization of immunoconglutinins in patients with systemic lupus erythematosus (SLE): serial analysis in relation to disease course1992Ingår i: Clinical and experimental immunology, Vol. 90, s. 251-255Artikel i tidskrift (Refereegranskat)
  • 133. Nilsson, Bo
    et al.
    Nilsson Ekdahl, Kristina
    Department of Clinical Immunology and Transfusion Medicine, University Hospital, Uppsala.
    Svarvare, M
    Bjelle, A
    Nilsson, U R
    Purification and characterization of IgG immunoconglutinins from patients with systemic lupus erythematosus: Implications for a regulatory function1990Ingår i: Clinical and Experimental Immunology, ISSN 0009-9104, E-ISSN 1365-2249, Vol. 82, nr 2, s. 262-267Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The levels of IgG immunoconglutinins in plasma from patients with rheumatoid arthritis, systemic lupus erythematosus and primary biliary cirrhosis were monitored by ELISA. High levels of IgG immunoconglutinins were found mainly in plasma from patients with systemic lupus erythematosus. These immunoconglutinins bound to microtitre plate-fixed C3, C3b and C3c but poorly to C3d. This binding was inhibited by particle-bound C3b and iC3b but not by the corresponding soluble fragments. Furthermore, Western blot analysis revealed no immunoconglutinin-binding to reduced C3 peptides and no binding was shown to soluble C3 α and β chain by ELISA. IgG immunoconglutinins were purified from three plasma specimens by affinity chromatography on activated thiol sepharose ATS/C3 fragments. Two immunoconglutinin preparations that preferentially recognize ATS-C3b, inhibited C5-converlase function by 50–100% while one immunoconglutinin that recognized ATS-C3d,g had no effect. The two former immunoconglutinins also inhibited all three factor I cleavages in C3α chain but the latter inhibited only the third cleavage. None of the immunoconglutinins affected the binding of complement-coated anti-BSA/BSA complexes to CRI (CD 35) on human erythrocytes, but the two immunoconglutinins that inhibited all factor I cleavages also inhibited the factor I-induced release of anti-BSA/BSA complexes from CRI. The results show that immunoconglutinins recognize specific epitopes on bound C3 fragments and that they are able to modulate C3-mcdiated functions. 

  • 134. Nilsson, Bo
    et al.
    Nilsson Ekdahl, Kristina
    Department of Clinical Immunology and Transfusion Medicine, University Hospital, Uppsala.
    Svensson, K E
    Bjelle, A
    Nilsson, U R
    Distinctive expression of neoantigenic C3(D) epitopes on bound C3 following activation and binding to different target surfaces in normal and pathological human sera1989Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 26, nr 4, s. 383-390Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Binding of C3 to sheep erythrocytes in a serum-free milieu (EAC14oxy2, EAC142) has previously been shown to mimic the antigenic change that occurs upon denaturation of C3 in sodium dodecyl sulphate (SDS), whereby neoantigenic C3(D) epitopes are exposed. The present paper deals with C3 bound to various target surfaces which are known to modulate the functional properties of C3 in different ways. Bound C3 fragments on serum-treated human aggregated gammaglobulin, zymosan, rabbit and sheep erythrocytes, and on circulating immune complexes isolated from sera of patients with rheumatoid arthritis and systemic lupus erythematosus, were shown to be mainly in the iC3b form. By RIAs, employing polyclonal antibodies, the range of C3(D) antigenic epitopes of 125I-labelled SDS denatured C3 expressed by the particle-bound iC3b was monitored. The physiologically bound iC3b on all tested particles expressed wide ranges of C3(D) epitopes and each type of particle-bound C3 exposed its individual range. By competition ELISA specific C3(D)α epitopes were monitored, employing monoclonal antibodies. A distinct difference in the expression of these epitopes was observed in iC3b bound to various test particles in the presence of normal serum and in iC3b present on circulating immune complexes from pathological sera. Considering that the neoantigenic C3(D) epitopes have been shown to be associated with different functions of C3, the distinctive antigenic expression of each type of serum-treated particle might reflect different functional forms of the protein. 

  • 135.
    Nilsson, Bo
    et al.
    Uppsala University.
    Teramura, Yuji
    Uppsala University;University of Tokyo.
    Nilsson Ekdahl, Kristina
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    The role and regulation of complement activation as part of the thromboinflammation elicited in cell therapies2014Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 61, nr 2, s. 185-190Artikel, forskningsöversikt (Refereegranskat)
    Abstract [en]

    Cell therapies in which the cells come into direct contact with blood and other body fluids are emerging treatment procedures for patients with various diseases, such as diabetes mellitus, liver insufficiency, and graft-versus-host disease. However, despite recent progress, these procedures are associated with tissue loss caused by thromboinflammatory reactions. These deleterious reactions involve the activation of the complement and coagulation cascades and platelet and leukocyte activation, ultimately resulting in clot formation and damage to the implanted cells. In this concept review, we discuss the basic mechanisms underlying the thrombininflammatory process, with special reference to the engagement of complement and emerging strategies for the therapeutic regulation of these reactions that include the use of selective systemic inhibitors and various procedures to coat the surfaces of the cells. The coating procedures may also be applied to other treatment modalities in which similar mechanisms are involved, including whole organ transplantation, treatment with biomaterials in contact with blood, and extracorporeal procedures. (C) 2014 Published by Elsevier Ltd.

  • 136.
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Biomedicinsk kemi2000Ingår i: Klinisk kemi, Vol. 5, s. 151-152Artikel i tidskrift (Övrig (populärvetenskap, debatt, mm))
  • 137.
    Nilsson Ekdahl, Kristina
    University of Uppsala.
    Further studies on the phosphorylation of rat liver fructose-1,6-bisphosphatase. Importance of the three-dimensional structure of a substrate to protein kinase A1992Ingår i: Journal of biochemistry, Vol. 112, s. 719-723Artikel i tidskrift (Refereegranskat)
  • 138.
    Nilsson Ekdahl, Kristina
    Department of Medical and Physiological Chemistry, University of Uppsala.
    In vitro phosphorylation of fructose-1,6-bisphosphatase from rabbit and pig liver with cyclic AMP-dependent protein kinase1988Ingår i: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 262, nr 1, s. 27-31Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Homogeneous preparations of fructose-1,6-bisphosphatase from mouse, man, rabbit, pig, and rat were tested as substrates for cyclic AMP-dependent protein kinase. Up to 1 mol of [32P]phosphate per mole enzyme subunit was incorporated into fructose-1,6-bisphosphatase from pig and rabbit liver, which should be compared with 2.6 mol of phosphate per mole enzyme subunit in the case of the rat liver enzyme. The phosphorylation of fructose-1,6-bisphosphatase from the livers of man and mouse was negligible. Phosphorylation of pig and rabbit fructose-1,6-bisphosphatase decreased the apparent Km for fructose-1,6-bisphosphate, but in contrast to the case of the rat liver enzyme it did not change the inhibition constants for AMP and fructose-2,6-bisphosphate. The Phosphorylation sites in rabbit and pig liver fructose-1,6-bisphosphatase were located close to the carboxyterminal of the polypeptide chains, since trypsin treatment of the phosphorylated enzyme quantitatively removed all of the protein-bound radioactivity without significantly altering the subunit molecular weight and with a maintained neutral pH Optimum. 

  • 139.
    Nilsson Ekdahl, Kristina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Magisterprogrammet i biomedicin2001Ingår i: Klinisk kemi, Vol. 1, s. 34-35Artikel i tidskrift (Övrig (populärvetenskap, debatt, mm))
  • 140.
    Nilsson Ekdahl, Kristina
    Department of Medical and Physiological Chemistry, Biomedical Center, University of Uppsala.
    Rat liver fructose-1,6-bisphosphatase: Identification of serine- 338 as a third major phosphorylation site for cyclic AMP-dependent protein kinase. Activity changes associated with multisite phosphorylation in vitro1987Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 262, s. 16699-16703Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Rat liver fructose-1,6-bisphosphatase was phosphorylated with [32P]ATP and the catalytic subunit of cyclic AMP-dependent protein kinase. After digestion with trypsin, two peptides were isolated containing 68 and 32% of the total radioactivity, respectively. The former was found to contain the sequence Ala-Lys-Ser(P)-Arg-Pro-Ser(P)-Leu-Pro. In this fragment, Ser-341, but not Ser-338, had earlier been reported to be a phosphorylation site. The other peptide contained phosphorylated Ser-356. It was demonstrated that all the protein-bound [32P]phosphate was distributed evenly between these three serines in the native enzyme regardless of the degree of phosphorylation. Preservation of the three-dimensional structure, however, was needed to obtain phosphorylation of Ser-356. Peptides containing each phosphorylatable serine residue were sequentially removed by digesting the enzyme with chymotrypsin which cleaved off Ser-356, denaturing it with urea, digesting it further with chymotrypsin, thus removing Ser-341, and finally treating it with trypsin which eliminated the rest of the radioactivity which was bound to Ser-338. Kinetic studies of fructose-1,6-bisphosphatase digested in this manner revealed that phosphorylation of Ser-338 decreased the apparent Km for fructose 1,6-bisphosphatase, whereas phosphorylation of Ser-341 decreased the inhibitory effect of AMP and fructose 2,6-bisphosphatase, Phosphorylation of Ser-356 did not affect these parameters. 

  • 141.
    Nilsson Ekdahl, Kristina
    Uppsala University.
    Studies on the regulation of rat liver pyruvate kinase and fructose 1,6-bisphosphatase1987Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
  • 142.
    Nilsson Ekdahl, Kristina
    Department of Medical and Physiological Chemistry, Biomedical Center, University of Uppsala.
    Studies on the regulation of rat liver pyruvate kinase and fructose-1,6-bisphosphatase1987Ingår i: Upsala journal of medical sciences, Vol. 92, nr 3, s. 217-232Artikel i tidskrift (Refereegranskat)
  • 143.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Bengtsson, A A
    Andersson, J
    Elgue, G
    Rönnblom, L
    Sturfelt, G
    Nilsson, Bo
    Thrombotic disease in systemic lupus erythematosus is associated with a maintained systemic platelet activation2004Ingår i: British journal of haematology, Vol. 125 (1), s. 74-78Artikel i tidskrift (Refereegranskat)
  • 144.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Blomberg, Carolina
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Henningsson Johnsson, Anna
    Dahle, Charlotte
    Håkansson, Irene
    Sandholm, Kerstin
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Ernerudh, Jan
    Systemic and Intrathecal Complement Activation in Multiple Sclerosis and Guillan-Barré Syndrome2009Ingår i: Molecular Immunology, ISSN 0161-5890, E-ISSN 1872-9142, Vol. 46, nr 14, s. 2848-2848Artikel i tidskrift (Refereegranskat)
  • 145.
    Nilsson Ekdahl, Kristina
    et al.
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB). Uppsala University.
    Davoodpour, Padideh
    Uppsala University.
    Ekstrand-Hammarström, Barbro
    Swedish Defence Research Agency, Umeå.
    Fromell, Karin
    Uppsala University.
    Hamad, Osama A
    Uppsala University.
    Hong, Jaan
    Uppsala University.
    Bucht, Anders
    Swedish Defence Research Agency, Umeå;Umeå University.
    Mohlin, Camilla
    Linnéuniversitetet, Fakulteten för Hälso- och livsvetenskap (FHL), Institutionen för kemi och biomedicin (KOB).
    Seisenbaeva, Gulaim A
    Swedish University of Agricultural Sciences (SLU).
    Kessler, Vadim G
    Swedish University of Agricultural Sciences (SLU).
    Nilsson, Bo
    Uppsala University.
    Contact (kallikrein/kinin) system activation in whole human blood induced by low concentrations of α-Fe2O3 nanoparticles2018Ingår i: Nanomedicine: Nanotechnology, Biology and Medicine, ISSN 1549-9634, E-ISSN 1549-9642, Vol. 14, nr 3, s. 735-744Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Iron-oxide nanoparticles (NPs) generated by environmental events are likely to represent health problems. α-Fe2O3 NPs were synthesized, characterized and tested in a model for toxicity utilizing human whole blood without added anticoagulant. MALDI-TOF of the corona was performed and activation markers for plasma cascade systems (complement, contact and coagulation systems), platelet consumption and release of growth factors, MPO, and chemokine/cytokines from blood cells were analyzed. The coronas formed on the pristine α-Fe2O3 NPs contained contact system proteins and they induced massive activation of the contact (kinin/kallikrein) system, as well as thrombin generation, platelet activation, and release of two pro-angiogeneic growth factors: platelet-derived growth factor and vascular endothelial growth factor, whereas complement activation was unaffected. The α-Fe2O3 NPs exhibited a noticeable toxicity, with kinin/kallikreinactivation, which may be associated with hypotension and long-term angiogenesis in vivo, with implications for cancer, arteriosclerosis and pulmonary disease.

  • 146.
    Nilsson Ekdahl, Kristina
    et al.
    Department of Medical and Physiological Chemistv, University of Uppsala, Box 575, S-75123 Uppsala, Sweden.
    Ekman, P
    Fructose-1,6-bisphosphatase from rat liver. A comparison of the kinetics of the unphosphorylated enzyme and the enzyme phosphorylated by cyclic AMP-dependent protein kinase.1985Ingår i: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 260, s. 14173-14179Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    A purification procedure for rat hepatic fructose-1,6-bisphosphatase, described earlier, has been improved, resulting in an enzyme preparation with a neutral pH optimum and with both phosphorylatable serine residues present. The subunit Mr was 40,000. Phosphorylation in vitro with cyclic AMP-dependent protein kinase resulted in the incorporation of 1.4 mol of phosphate/mol of subunit and led to an almost 2-fold decrease in apparent Km for fructose-1,6-bisphosphate. In contrast to yeast fructose-1,6-bisphosphatase, fructose-2,6-bisphosphate had no effect on the rate of phosphorylation or dephosphorylation of the intact enzyme. The effects of the composition of the assay medium, with regard to buffering substance and Mg2+ concentration, on the apparent Km values of phosphorylated and unphosphorylated enzyme were investigated. The kinetics of phosphorylated and unphosphorylated fructose-1,6-bisphosphatase were studied with special reference to the inhibitory effects of adenine nucleotides and fructose-2,6-bisphosphate. Unphosphorylated fructose-1,6-bisphosphatase was more susceptible to inhibition by both AMP and fructose 2,6-bisphosphate than phosphorylated enzyme, at high and low substrate concentrations. Both ATP and ADP had a similar effect on the two enzyme forms, ADP being the more potent inhibitor. Finally, the combined effect of several inhibitors at physiological concentrations was studied. Under conditions resembling the gluconeogenic state, phosphorylated fructose-1,6-bisphosphatase was found to have twice the activity of the unphosphorylated enzyme. 

  • 147.
    Nilsson Ekdahl, Kristina
    et al.
    UNIV UPPSALA, CTR BIOMED, DEPT CIENCIAS BIOL, S-75123 UPPSALA, SWEDEN .
    Ekman, P
    Hepatic L-type pyruvate kinase: Separation of unphosphorylated, phosphorylated and proteolytically modified in vivo forms1984Ingår i: Journal of Biochemistry (Tokyo), ISSN 0021-924X, E-ISSN 1756-2651, Vol. 95, nr 4, s. 917-924Artikel i tidskrift (Refereegranskat)
  • 148.
    Nilsson Ekdahl, Kristina
    et al.
    Department of Medical and Physiological Chemistry, Biomedical Center, University of Uppsala .
    Ekman, Pia
    Department of Medical and Physiological Chemistry, Biomedical Center, University of Uppsala.
    Effects of epinephrine, glucagon and insulin on the activity and degree of phosphorylation of fructose-1,6-bisphosphatase in cultured hepatocytes1987Ingår i: Biochimica et Biophysica Acta. Molecular Cell Research, ISSN 0167-4889, E-ISSN 1879-2596, Vol. 929, s. 318-326Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    The effects of epinephrine, glucagon and insulin on the activity and degree of phosphorylation of fructose-1,6-bisphosphatase in isolated hepatocytes maintained in cell culture for 24 h were investigated. Epinephrine caused a rapid decrease in the apparent Km monitored as the activity ratio between the activity at 12.5 and 83 μM fructose-1,6-bisphosphate, reaching a maximum after 5 min. Glucagon caused a slower and less pronounced activation, and insulin caused an equally slow increase in Km. The effect of epinephrine and glucagon was completely reciprocated by insulin and the action of insulin was totally erased by the other two. Glucagon stimulated the incorporation of [32P]phosphate into fructose-1,6-bisphosphatase from about 2.5 to 4.2 mol/mol enzyme and epinephrine to 3.5 mol/mol. The effect of the two hormones acting together was cumulative. Insulin brought about a decrease in the degree of phosphorylation to 2.0 mol/mol. The effect of epinephrine was shown to be caused by the β-receptors, since it was completely blocked by propanolol (a β-antagonist) and remained unaffected by the presence of phentolamine (an α-antagonist). 

  • 149.
    Nilsson Ekdahl, Kristina
    et al.
    University of Uppsala.
    Ekman, Pia
    University of Uppsala.
    The effect of fructose-2,6-bisphosphate and AMP on the activity of phosphorylated and unphosphorylated fructose-1,6 bisphosphatase from rat liver1984Ingår i: FEBS letters, Vol. 167, nr 2, s. 203-209Artikel i tidskrift (Refereegranskat)
    Abstract [en]

    Rat liver fructose-1,6-bisphosphatase was partially phosphorylated in vitro and separated into unphosphorylated and fully phosphorylated enzyme. The effects of fructose 2,6-bisphosphate and AMP on these two enzyme forms were examined. Unphosphorylated fructose-1,6-bisphosphatase was more easily inhibited by both effectors. Fructose 2,6-bisphosphate affected both K0.5 and Vmax, while the main effect of AMP was to lower Vmax. Fructose 2,6-bisphosphate and AMP together acted synergistically to decrease the activity of fructose-1,6-bisphosphatase, and since unphosphorylated and phosphorylated enzyme forms are affected differently, this might be a way to amplify the effect of phosphorylation. 

  • 150.
    Nilsson Ekdahl, Kristina
    et al.
    Högskolan i Kalmar, Naturvetenskapliga institutionen.
    Elgue, G
    Nilsson, Bo
    Phosphorylation of coagulation factor XI by a casein kinase released by activated human platelets increases its susceptibility to activation by factor XIIa and thrombin1999Ingår i: Thrombosis and haemostasis, Vol. 82, s. 1283-1289Artikel i tidskrift (Refereegranskat)
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