Hereditary Systemic Amyloidosis Due to Asp76Asn Variant β2-Microglobulin | Zendy

Sophie Valleix | Zendy; Julian D. Gillmore | Zendy; Frank Bridoux | Zendy; P. Patrizia Mangione | Zendy; Ahmet Doğan | Zendy; Brigitte Nédelec | Zendy; Mathieu Boimard | Zendy; Guy Touchard | Zendy; JeanMichel Goujon | Zendy; Corinne Lacombe | Zendy; Pierre Lozeron | Zendy; David Adams | Zendy; Catherine Lacroix | Zendy; Thierry Maisonobe | Zendy; Violaine PlantéBordeneuve | Zendy; Julie A. Vrana | Zendy; Jason D. Theis | Zendy; Sofia Giorgetti | Zendy; Riccardo Porcari | Zendy; Stéfano Ricagno | Zendy; Martino Bolognesi | Zendy; Monica Stoppini | Zendy; Marc Delpech | Zendy; Mark B. Pepys | Zendy; Philip N. Hawkins | Zendy; Vittorio Bellotti | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Hereditary Systemic Amyloidosis Due to Asp76Asn Variant β₂-Microglobulin

Author(s) -

Sophie Valleix,

Julian D. Gillmore,

Frank Bridoux,

P. Patrizia Mangione,

Ahmet Doğan,

Brigitte Nédelec,

Mathieu Boimard,

Guy Touchard,

JeanMichel Goujon,

Corinne Lacombe,

Pierre Lozeron,

David Adams,

Catherine Lacroix,

Thierry Maisonobe,

Violaine PlantéBordeneuve,

Julie A. Vrana,

Jason D. Theis,

Sofia Giorgetti,

Riccardo Porcari,

Stéfano Ricagno,

Martino Bolognesi,

Monica Stoppini,

Marc Delpech,

Mark B. Pepys,

Philip N. Hawkins,

Vittorio Bellotti

Publication year - 2012

Publication title -

new england journal of medicine

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 19.889

H-Index - 1030

eISSN - 1533-4406

pISSN - 0028-4793

DOI - 10.1056/nejmoa1201356

Subject(s) - beta 2 microglobulin , amyloidosis , fibrillogenesis , medicine , amyloid fibril , amyloid (mycology) , fibril , pathology , biochemistry , chemistry , disease , amyloid β

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research