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  • 1. Almandoz-Gil, Leire
    et al.
    Welander, Hedvig
    Ihse, Elisabet
    Khoonsari, Payam Emami
    Musunuri, Sravani
    Lendel, Christofer
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Applied Physical Chemistry.
    Sigvardson, Jessica
    Karlsson, Mikael
    Ingelsson, Martin
    Kultima, Kim
    Bergstrom, Joakim
    Low molar excess of 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote oligomerization of alpha-synuclein through different pathways2017In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 110, p. 421-431Article in journal (Refereed)
    Abstract [en]

    Aggregated alpha-synuclein is the main component of Lewy bodies, intraneuronal inclusions found in brains with Parkinson's disease and dementia with Lewy bodies. A body of evidence implicates oxidative stress in the pathogenesis of these diseases. For example, a large excess (30: 1, aldehyde: protein) of the lipid peroxidation end products 4-oxo-2-nonenal (ONE) or 4-hydroxy-2-nonenal (HNE) can induce alpha-synuclein oligomer formation. The objective of the study was to investigate the effect of these reactive aldehydes on alpha-synuclein at a lower molar excess (3: 1) at both physiological (7.4) and acidic (5.4) pH. As observed by size-exclusion chromatography, ONE rapidly induced the formation of alpha-synuclein oligomers at both pH values, but the effect was less pronounced under the acidic condition. In contrast, only a small proportion of alpha-synuclein oligomers were formed with low excess HNE-treatment at physiological pH and no oligomers at all under the acidic condition. With prolonged incubation times (up to 96 h), more alpha-synuclein was oligomerized at physiological pH for both ONE and HNE. As determined by Western blot, ONE-oligomers were more SDS-stable and to a higher-degree cross-linked as compared to the HNE-induced oligomers. However, as shown by their greater sensitivity to proteinase K treatment, ONE-oligomers, exhibited a less compact structure than HNE-oligomers. As indicated by mass spectrometry, ONE modified most Lys residues, whereas HNE primarily modified the His50 residue and fewer Lys residues, albeit to a higher degree than ONE. Taken together, our data show that the aldehydes ONE and HNE can modify alpha-synuclein and induce oligomerization, even at low molar excess, but to a higher degree at physiological pH and seemingly through different pathways.

  • 2.
    Almandoz-Gil, Leire
    et al.
    Uppsala Univ, Dept Publ Hlth & Caring Sci, Mol Geriatr, SE-75185 Uppsala, Sweden..
    Welander, Hedvig
    Uppsala Univ, Dept Publ Hlth & Caring Sci, Mol Geriatr, SE-75185 Uppsala, Sweden..
    Ihse, Elisabeth
    Uppsala Univ, Dept Publ Hlth & Caring Sci, Mol Geriatr, SE-75185 Uppsala, Sweden..
    Khoonsari, Payam Emami
    Uppsala Univ, Dept Med Sci, SE-75185 Uppsala, Sweden..
    Musunuri, Sravani
    Uppsala Univ, Dept Med Sci, SE-75185 Uppsala, Sweden..
    Lendel, Christofer
    KTH, School of Engineering Sciences in Chemistry, Biotechnology and Health (CBH), Chemistry.
    Sigvardson, Jessica
    BioArctic AB, Warfvinges Vag 35, SE-11251 Stockholm, Sweden..
    Karlsson, Mikael
    Uppsala Univ, Dept Engn Sci, SE-75121 Uppsala, Sweden..
    Ingelsson, Martin
    Uppsala Univ, Dept Publ Hlth & Caring Sci, Mol Geriatr, SE-75185 Uppsala, Sweden..
    Kultima, Kim
    Uppsala Univ, Dept Med Sci, SE-75185 Uppsala, Sweden..
    Bergstrom, Joakim
    Uppsala Univ, Dept Publ Hlth & Caring Sci, Mol Geriatr, SE-75185 Uppsala, Sweden..
    Low molar excess of 4-oxo-2-nonenal and 4-hydroxy-2-nonenal promote oligomerization of alpha-synuclein through different pathways (vol 110, pg 421, 2017)2018In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 117, p. 258-258Article in journal (Refereed)
  • 3. Veneskoski, Marja
    et al.
    Turunen, S. Pauliina
    University of Oulu, 90014 Oulu, Finland.
    Kummu, Outi
    Nissinen, Antti
    Rannikko, Sirpa
    Levonen, Anna-Liisa
    Hörkkö, Sohvi
    Specific recognition of malondialdehyde and malondialdehyde acetaldehyde adducts on oxidized LDL and apoptotic cells by complement anaphylatoxin C3a.2011In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 51, no 4, p. 834-43Article in journal (Refereed)
    Abstract [en]

    Oxidatively modified low-density lipoproteins (Ox-LDL) and complement anaphylatoxins C3a and C5a are colocalized in atherosclerotic lesions. Anaphylatoxin C3a also binds and breaks bacterial lipid membranes and phosphatidylcholine liposomes. The role of oxidized lipid adducts in C3a binding to Ox-LDL and apoptotic cells was investigated. Recombinant human C3a bound specifically to low-density lipoprotein and bovine serum albumin modified with malondialdehyde (MDA) and malondialdehyde acetaldehyde (MAA) in chemiluminescence immunoassays. No binding was observed to native proteins, LDL oxidized with copper ions (CuOx-LDL), or phosphocholine. C3a binding to MAA-LDL was inhibited by two monoclonal antibodies specific for MAA-LDL. On agarose gel electrophoresis, C3a comigrated with MDA-LDL and MAA-LDL, but not with native LDL or CuOx-LDL. C3a bound to apoptotic cells in flow cytometry. C3a opsonized MAA-LDL and was taken up by J774A.1 macrophages in immunofluorescence analysis. Complement-activated human serum samples (n=30) showed increased C3a binding to MAA-LDL (P<0.001) and MDA-LDL (P<0.001) compared to nonactivated samples. The amount of C3a bound to MAA-LDL was associated with total complement activity, C3a desArg concentration, and IgG antibody levels to MAA-LDL. Proteins containing MDA adducts or MAA adducts may bind C3a in vivo and contribute to inflammatory processes involving activation of the complement system in atherosclerosis.

  • 4.
    Welander, Hedvig
    et al.
    Uppsala Universitet.
    Wiberg, Henning
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Applied Physical Chemistry.
    Emmer, Åsa
    KTH, School of Chemical Science and Engineering (CHE), Chemistry, Applied Physical Chemistry.
    Lannfelt, Lars
    Uppsala Universitet.
    Ingelsson, Martin
    Uppsala Universitet.
    Bergström, Joakim
    Uppsala Universitet.
    Histidine 50 is a crucial residue for alpha-synuclein aggregation induced by lipid peroxidation-derived aldehydes2012In: Free Radical Biology & Medicine, ISSN 0891-5849, E-ISSN 1873-4596, Vol. 53, no Suppl 1, p. S248-S249Article in journal (Refereed)
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