The cysteine 34 residue of A1M/α₁-microglobulin is essential for protection of irradiated cell cultures and reduction of carbonyl groups

References

• Flower DR. The lipocalin protein family: structure and function. Biochem J 1996;318:1–14.
   PubMed Web of Science ®Google Scholar
• Åkerström B, Flower DR, Salier JP. Lipocalins: unity in diversity. Biochim Biophys Acta 2000;1482:1–8.
   PubMedGoogle Scholar
• Åkerström B, Borregaard N, Flower DR, Salier JP (eds.). Lipocalins: An Introduction. Georgetown, Texas: Landers Bioscience; 2006.
   Google Scholar
• Ganfornina MD, Sanchez D, Greene LH, Flower DR (eds.). The lipocalin protein family: protein sequence, structure and relationship to the calycin superfamily. Georgetown, Texas: Landers Bioscience; 2006.
   Google Scholar
• Ekström B, Berggård I. Human α1-microglobulin. Purification procedure, chemical and physiochemical properties. J Biol Chem 1977;252:8048–8057.
   PubMedGoogle Scholar
• Åkerström B, Lögdberg L (eds.). α₁-microglobulin. Georgetown, Texas: Landers Bioscience; 2006.
   Google Scholar
• Akerström B, Lögdberg L. An intriguing member of the lipocalin protein family: α1-microglobulin. Trends Biochem Sci 1990;15:240–243.
   PubMedGoogle Scholar
• Kaumeyer JF, Polazzi JO, Kotick MP. The mRNA for a proteinase inhibitor related to the HI-30 domain of inter- alpha-trypsin inhibitor also encodes α-1-microglobulin (protein HC). Nucleic Acids Res 1986;14:7839–7850.
   PubMedGoogle Scholar
• Lindqvist A, Bratt T, Altieri M, Kastern W, Åkerström B. Rat α1-microglobulin: co-expression in liver with the light chain of inter-alpha-trypsin inhibitor. Biochim Biophys Acta 1992;1130:63–67.
   PubMedGoogle Scholar
• Bratt T, Olsson H, Sjöberg EM, Jergil B, Åkerström B. Cleavage of the α1-microglobulin -bikunin precursor is localized to the Golgi apparatus of rat liver cells. Biochim Biophys Acta 1993;1157:147–154.
   PubMedGoogle Scholar
• Allhorn M, Klapyta A, Åkerström B. Redox properties of the lipocalin α1-microglobulin: reduction of cytochrome c, hemoglobin, and free iron. Free Radic Biol Med 2005;38:557–567.
   PubMed Web of Science ®Google Scholar
• Åkerström B, Maghzal GJ, Winterbourn CC, Kettle AJ. The lipocalin α1-microglobulin has radical scavenging activity. J Biol Chem 2007;282:31493–1503.
   PubMed Web of Science ®Google Scholar
• Olsson MG, Allhorn M, Bulow L, Hansson SR, Ley D, Olsson ML, et al. Pathological conditions involving extracellular hemoglobin: molecular mechanisms, clinical significance, and novel therapeutic opportunities for α(1)- microglobulin. Antioxid Redox Signal 2012; 17;813–846. Epub ahead of print.
   PubMed Web of Science ®Google Scholar
• Olsson MG, Olofsson T, Tapper H, Åkerström B. The lipocalin α1-microglobulin protects erythroid K562 cells against oxidative damage induced by heme and reactive oxygen species. Free Radic Res 2008;42:725–736.
   PubMed Web of Science ®Google Scholar
• Olsson MG, Allhorn M, Larsson J, Cederlund M, Lundqvist K, Schmidtchen A, et al. Up-Regulation of A1M/α1-microglobulin in skin by heme and reactive oxygen species gives protection from oxidative damage. PLoS One 2011;6:e27505.
   PubMed Web of Science ®Google Scholar
• May K, Rosenlöf L, Olsson MG, Centlow M, Mörgelin M, Larsson I, et al. Perfusion of human placenta with hemoglobin introduces preeclampsia-like injuries that are prevented by α1–microglobulin. Placenta 2011;32:323–332.
   PubMed Web of Science ®Google Scholar
• Olsson MG, Nilsson EJ, Rutardottir S, Paczesny J, Pallon J, Akerstrom B. Bystander cell death and stress response is inhibited by the radical scavenger α(1)-microglobulin in irradiated cell cultures. Radiat Res 2010;174:590–600.
   PubMed Web of Science ®Google Scholar
• Little JB, Azzam EI, de Toledo SM, Nagasawa H. Bystander effects: intercellular transmission of radiation damage signals. Radiat Prot Dosimetry 2002;991:159–162.
   Google Scholar
• Mothersill C, Seymour C. Radiation-induced bystander effects: past history and future directions. Radiat Res 2001;155: 759–767.
   PubMed Web of Science ®Google Scholar
• Prise KM, Folkard M, Michael BD. A review of the bystander effect and its implications for low-dose exposure. Radiat Prot Dosimetry 2003;104:347–355.
   PubMed Web of Science ®Google Scholar
• Azzam EI, de Toledo SM, Little JB. Oxidative metabolism, gap junctions and the ionizing radiation-induced bystander effect. Oncogene 2003;22:7050–7057.
   PubMed Web of Science ®Google Scholar
• Lyng FM, Seymour CB, Mothersill C. Production of a signal by irradiated cells which leads to a response in unirradiated cells characteristic of initiation of apoptosis. Br J Cancer 2000;83:1223–1230.
   PubMed Web of Science ®Google Scholar
• Lyng FM, Seymour CB, Mothersill C. Initiation of apoptosis in cells exposed to medium from the progeny of irradiated cells: a possible mechanism for bystander-induced genomic instability? Radiat Res 2002;157:365–370.
   PubMed Web of Science ®Google Scholar
• Villoutreix BO, Åkerström B, Lindqvist A. Structural model of human α1-microglobulin: proposed scheme for the interaction with the Gla domain of anticoagulant protein C. Blood Coagul Fibrinolysis 2000;11:261–275.
   PubMedGoogle Scholar
• Meining W, Skerra A. The crystal structure of human alpha(1)-microglobulin reveals a potential haem-binding site. Biochem J 2012;445:175–182.
   PubMedGoogle Scholar
• Kwasek A, Osmark P, Allhorn M, Lindqvist A, Åkerström B, Wasylewski Z. Production of recombinant human α1- microglobulin and mutant forms involved in chromophore formation. Protein Expr Purif 2007;53:145–152.
   PubMedGoogle Scholar
• Åkerström B, Bratt T, Enghild JJ. Formation of the alpha1-microglobulin chromophore in mammalian and insect cells: a novel post-translational mechanism? FEBS Lett 1995; 362:50–54.
   PubMedGoogle Scholar
• Greenwood FC, Hunter WM, Glover JS. The preparation of I-131-Labelled human growth hormone of high specific radioactivity. Biochem J 1963;89:114–123.
   PubMed Web of Science ®Google Scholar
• Plesner T, Norgaard-Pedersen B, Boenisch T. Radioimmunoassay of β2-microglobulin. Scand J Clin Lab Invest 1975;35: 729–735.
   PubMed Web of Science ®Google Scholar
• Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970;227:680–685.
   PubMed Web of Science ®Google Scholar
• Buss H, Chan TP, Sluis KB, Domigan NM, Winterbourn CC. Protein carbonyl measurement by a sensitive ELISA method. Free Radic Biol Med 1997;23:361–366.
   PubMed Web of Science ®Google Scholar
• Takagi T, Takagi K, Kawai T. Complete amino acid sequence of human α1-microglobulin. Biochem Biophys Res Commun 1981;98:997–1001.
   PubMedGoogle Scholar
• Amoresano A, Minchiotti L, Cosulich ME, Campagnoli M, Pucci P, Andolfo A, et al. Structural characterization of the oligosaccharide chains of human α1-microglobulin from urine and amniotic fluid. Eur J Biochem 2000;267: 2105–2112.
   PubMedGoogle Scholar
• Newcomer ME, Ong DE. Purification and crystallization of a retinoic acid-binding protein from rat epididymis. Identity with the major androgen-dependent epididymal proteins. J Biol Chem 1990;265:12876–12879.
   PubMedGoogle Scholar
• Miller NJ, Rice-Evans CA. Factors influencing the antioxidant activity determined by the ABTS + radical cation assay. Free Radic Res 1997;26:195–199.
   PubMed Web of Science ®Google Scholar
• Fournier T, Medjoubi NN, Porquet D. Alpha-1-acid glycoprotein. Biochim Biophys Acta 2000;1482:157–171.
   PubMed Web of Science ®Google Scholar
• Fernandez-Luna JL, Leyva-Cobian F, Mollinedo F. Identification of the protein HC receptor. FEBS Lett 1988;236: 471–474.
   PubMedGoogle Scholar
• Wester L, Michaelsson E, Holmdahl R, Olofsson T, Akerstrom B. Receptor for alpha1-microglobulin on T lymphocytes: inhibition of antigen-induced interleukin-2 production. Scand J Immunol 1998;48:1–7.
   PubMed Web of Science ®Google Scholar
• Sala A, Campagnoli M, Perani E, Romano A, Labo S, Monzani E, et al. Human α1-microglobulin is covalently bound to kynurenine-derived chromophores. J Biol Chem 2004;279:51033–51041.
   PubMedGoogle Scholar
• Berggård T, Cohen A, Persson P, Lindqvist A, Cedervall T, Silow M, et al. Alpha1-microglobulin chromophores are located to three lysine residues semiburied in the lipocalin pocket and associated with a novel lipophilic compound. Protein Sci 1999;8:2611–2620.
   PubMedGoogle Scholar