Research: Systemic amyloidosis

Systemic amyloidosis is a group of protein misfolding diseases that is caused by the formation of amyloid fibrils and their deposition in multiple organs. We are currently working on systemic AA amyloidosis and AL amyloidosis that are associated with fibrils derived from serum amyloid A protein or immunoglobulin light chains.

Photo shows systematic amyloidosis


Selected references:

Kollmer M, Meinhardt K, Haupt C, Liberta F, Wulff M, Linder J, Handl L, Heinrich L, Loos C, Schmidt M, Syrovets T, Simmet T, Westermark P, Westermark GT, Horn U, Schmidt V, Walther P, Fändrich M
Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits.
Proc. Natl. Acad. Sci. U.S.A. 2016, 113, 5604-5609

Annamalai K, Gührs KH, Koehler R, Schmidt M, Michel H, Loos C, Gaffney PM, Sigurdson CJ, Hegenbart U, Schönland S, Fändrich M
Polymorphism of amyloid fibrils in vivo.
Angewandte Chemie Int. Ed. 2016, 55, 4822-4825

Westermark GT, Fändrich M, Westermark P
AA Amyloidosis: Pathogenesis and Targeted Therapy.
Annu. Rev. Pathol. Mech. Dis. 2015, 10, 321-344

Gellermann GP, Appel TR, Tannert A, Radestock A, Hortschansky  P, Schroeckh V, Leisner C, Lütkepohl T, Shtrasburg S, Röcken C, Pras M, Linke RP, Diekmann S, Fändrich M
Raft lipids as common components of human extracellular amyloid fibrils.
Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 6297-6302

Contact

Prof. Dr. Marcus Fändrich
Tel: +49-(0)731/50 32750
Fax: +49-(0)731/50 32759
E-Mail: marcus.faendrich
Helmholtzstraße 8/1
Room number 1.55