Hereditary systemic amyloidosis due to Asp76Asn variant β2-microglobulin
| Autor: | Jean-Michel Goujon, Mathieu Boimard, Corinne Lacombe, Violaine Planté-Bordeneuve, Philip N. Hawkins, Monica Stoppini, Julie A. Vrana, Mark B. Pepys, Guy Touchard, Vittorio Bellotti, Riccardo Porcari, Thierry Maisonobe, Franck Bridoux, Sophie Valleix, Julian D. Gillmore, Ahmet Dogan, Martino Bolognesi, Jason D. Theis, Pierre Lozeron, Sofia Giorgetti, Marc Delpech, Catherine Lacroix, Stefano Ricagno, David H. Adams, Brigitte Nedelec, Palma Mangione |
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| Přispěvatelé: | Laboratoire de Biochimie et Génétique Moléculaire, Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Université Paris Descartes - Paris 5 (UPD5), Contrôle de la Réponse Immune B et des Lymphoproliférations (CRIBL), Centre National de la Recherche Scientifique (CNRS)-Université de Limoges (UNILIM)-Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST FR CNRS 3503), Service de néphrologie - hémodialyse et transplantation rénale, Centre hospitalier universitaire de Poitiers (CHU Poitiers), Laboratoire d'anatomopathologie, Université de Limoges (UNILIM)-Génomique, Environnement, Immunité, Santé, Thérapeutique (GEIST FR CNRS 3503)-Centre National de la Recherche Scientifique (CNRS), Assistance publique - Hôpitaux de Paris (AP-HP)-Université Paris Descartes - Paris 5 ( UPD5 ), Contrôle de la Réponse Immune B et des Lymphoproliférations ( CRIBL ), Centre National de la Recherche Scientifique ( CNRS ) -Université de Limoges ( UNILIM ) -Génomique, Environnement, Immunité, Santé, Thérapeutique ( GEIST FR CNRS 3503 ), Université de Poitiers-Centre hospitalier universitaire de Poitiers ( CHU Poitiers ), Ischémie - Reperfusion en transplatation rénale, Université de Poitiers-Institut National de la Santé et de la Recherche Médicale ( INSERM ), Centre hospitalier universitaire de Poitiers ( CHU Poitiers ), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Université Paris Descartes - Paris 5 (UPD5) |
| Jazyk: | angličtina |
| Rok vydání: | 2012 |
| Předmět: |
Male
MESH: Hydrogen-Ion Concentration Proteome MESH: Protein Structure Quaternary MESH : beta 2-Microglobulin MESH : Diarrhea MESH: Monitoring Physiologic 0302 clinical medicine [ SDV.IMM ] Life Sciences [q-bio]/Immunology MESH : Female Genes Dominant 0303 health sciences MESH: Middle Aged biology Amyloidosis MESH: Infant Newborn Fibrillogenesis MESH : Genes Dominant General Medicine Middle Aged MESH : Amyloidosis Familial Pedigree MESH: Glass MESH: Proteome MESH: Diarrhea Sjogren's Syndrome MESH : Glass [SDV.IMM]Life Sciences [q-bio]/Immunology Female Protein folding MESH: beta 2-Microglobulin MESH : Scalp Amyloidosis Familial Diarrhea medicine.medical_specialty Amyloid MESH: Pedigree MESH : Male MESH : Proteome MESH : Infant Newborn Fibril MESH: Scalp 03 medical and health sciences MESH : Hydrogen-Ion Concentration MESH : Protein Structure Quaternary Internal medicine medicine Humans MESH : Middle Aged MESH: Fetal Blood Protein Structure Quaternary 030304 developmental biology MESH : Fetal Blood MESH: Humans Beta-2 microglobulin business.industry MESH : Humans MESH : Monitoring Physiologic MESH: Electrodes medicine.disease MESH: Amyloidosis Familial In vitro MESH: Male Transthyretin Endocrinology MESH: Sjogren's Syndrome MESH : Pedigree biology.protein MESH : Sjogren's Syndrome beta 2-Microglobulin business MESH: Genes Dominant MESH: Female 030217 neurology & neurosurgery MESH : Electrodes |
| Zdroj: | New England Journal of Medicine New England Journal of Medicine, Massachusetts Medical Society, 2012, 366 (24), pp.2276-83. ⟨10.1056/NEJMoa1201356⟩ New England Journal of Medicine, Massachusetts Medical Society, 2012, 366 (24), pp.2276-83. 〈10.1056/NEJMoa1201356〉 |
| ISSN: | 0028-4793 1533-4406 |
| DOI: | 10.1056/NEJMoa1201356⟩ |
| Popis: | International audience; We describe a kindred with slowly progressive gastrointestinal symptoms and autonomic neuropathy caused by autosomal dominant, hereditary systemic amyloidosis. The amyloid consists of Asp76Asn variant β(2)-microglobulin. Unlike patients with dialysis-related amyloidosis caused by sustained high plasma concentrations of wild-type β(2)-microglobulin, the affected members of this kindred had normal renal function and normal circulating β(2)-microglobulin values. The Asp76Asn β(2)-microglobulin variant was thermodynamically unstable and remarkably fibrillogenic in vitro under physiological conditions. Previous studies of β(2)-microglobulin aggregation have not shown such amyloidogenicity for single-residue substitutions. Comprehensive biophysical characterization of the β(2)-microglobulin variant, including its 1.40-Å, three-dimensional structure, should allow further elucidation of fibrillogenesis and protein misfolding. |
| Databáze: | OpenAIRE |
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