Stabilization of amyloidogenic β2m by MHCI assembly 1 Class I Major Histocomapatibility Complex: the Trojan horse for secretion of amyloidogenic β2-microglobulin

نویسندگان

  • Levon Halabelian
  • Stefano Ricagno
  • Sofia Giorgetti
  • Carlo Santambrogio
  • Alberto Barbiroli
  • Sara Pellegrino
  • Adnane Achour
  • Rita Grandori
  • Loredana Marchese
  • Sara Raimondi
  • P. Patrizia Mangione
  • Raya Al-Shawi
  • Paul Simons
  • Ivana Speck
  • Monica Stoppini
  • Vittorio Bellotti
چکیده

From the 1 Dipartimento di Bioscienze, Università di Milano, Via Celoria 26, 20133 Milano, Italy, the 2 Department of Molecular Medicine, Institute of Biochemistry “A. Castellani”, Via Taramelli 3/b, 27100 Pavia, Italy, the 3 Department of Biotechnology and Biosciences, University of Milano-Bicocca, Piazza della Scienza 2, 20126 Milan, Italy, the 4 Section of Biochemistry, Dipartimento di Scienze Molecolari Agroalimentari, University of Milan, 20133 Milan, Italy, the 5 Dipartimento di Scienze Farmaceutichesez. Chimica generale e organica "A. Marchesini", Università degli Studi di Milano, 20133 Milan, Italy, the 6 Center for Infectious Medicine (CIM), Department of Medicine, Karolinska University Hospital Huddinge, Karolinska Institutet, Stockholm, Sweden, the 7 Wolfson Drug Discovery Unit, Centre for Amyloidosis and Acute Phase Proteins, University College London, London NW3 2PF, UK, the 8 Dipartimento di Scienze Mediche e Biologiche, Università di Udine, 33100 Udine, Italy,and the 9 Centre for Biomedical Science, Division of Medicine, University College London, London NW3 2PF, UK.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Class I Major Histocompatibility Complex, the Trojan Horse for Secretion of Amyloidogenic β2-Microglobulin*

To form extracellular aggregates, amyloidogenic proteins bypass the intracellular quality control, which normally targets unfolded/aggregated polypeptides. Human D76N β2-microglobulin (β2m) variant is the prototype of unstable and amyloidogenic protein that forms abundant extracellular fibrillar deposits. Here we focus on the role of the class I major histocompatibility complex (MHCI) in the in...

متن کامل

Influence of heparin molecular size on the induction of C-terminal unfolding in β2-microglobulin

Dialysis-related amyloidosis (DRA) is characterized by accumulation of amyloid β2-microglobulin (β2m) in the interstitial matrix. Matrix substances such as heparin have reportedly been strongly implicated in the pathogenesis of dialysis-related amyloidosis. In clinical setting of hemodialysis, two types of heparin, i.e., high and low molecular heparin (H.M.H. and L.M.H.) have been routinely use...

متن کامل

Influence of heparin molecular size on the induction of C- terminal unfolding in β2-microglobulin

Dialysis-related amyloidosis (DRA) is characterized by accumulation of amyloid β2- microglobulin (β2m) in the interstitial matrix. Matrix substances such as heparin have reportedly been strongly implicated in the pathogenesis of dialysis-related amyloidosis. In clinical setting of hemodialysis, two types of heparin, i.e., high and low molecular heparin (H.M.H. and L.M.H.) have been routinely us...

متن کامل

β2-microglobulin gene mutation is not a common mechanism of HLA class I total loss in human tumors

Major histocompatibility (MHC) class I molecules play an important role in cell recognition against virus-infected and tumor cells. Their main function is to present peptides derived from intracellular proteins to cytotoxic T-lymphocytes (CTL). The correct assembly of MHC class I peptide complexes is required for the stable expression of HLA class I [l]. This assembly occurs in the endoplasmic ...

متن کامل

Structural and Thermodynamic Characteristics of Amyloidogenic Intermediates of β-2-Microglobulin

β-2-microglobulin (β2m) self-aggregates to form amyloid fibril in renal patients taking long-term dialysis treatment. Despite the extensive structural and mutation studies carried out so far, the molecular details on the factors that dictate amyloidogenic potential of β2m remain elusive. Here we report molecular dynamics simulations followed by the solvation thermodynamic analyses on the wild-t...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2013