Phone: +49 304 50536115
Overall research program
The overall research program of Dr Röcken’s research group is (a) the investigation of the pathology and pathogenesis of systemic amyloidoses and (b) the improvement of the diagnosis and classification of systemic amyloidoses in surgical pathology.
a) We are specifically interested in the putative significance of macrophages and proteases, e.g. cathepsins, matrix metalloproteases and ADAMs, in generating amyloid proteins and clearing amyloid deposits using in vivo (mouse-) and in vitro (cell culture-) models. In the long term we wish to assess the putative value of protease-inhibitors for the treatment and prevention of amyloidoses.
b) We aim to improve the diagnosis and classification of amyloid in surgical pathology and provide a referral center for German and European surgical pathologists, who send amyloid containing biopsy specimens for the classification of amyloid applying and improving histochemical, immunohistochemical, biochemical and molecular biological techniques.
Five key publications
1. Röcken C, Stix B, Brömme D, Ansorge S, Roessner A, Bühling F. A putative role for
cathepsin K in degradation of AA and AL amyloidosis. Am J Pathol 158:1029-1038,
2. Stix B, Kähne T, Sletten K, Raynes J, Roessner A, Röcken C. Proteolysis of AA
amyloid fibril proteins by matrix metalloproteinases-1, -2, and –3. Am J Pathol
3. Bohne S, Sletten K, Menard R, Bühling F, Vöckler S, Wrenger E, Roessner A, Röcken
C. Cleavage of AL amyloid proteins by Cathepsin B, K and L. J Pathol. 203:528-
4. Röcken C, Menard R, Bühling F, Vöckler S, Raynes J, Stix B, Krüger S, Roessner A,
Kähne T. Proteolysis of serum amyloid A and AA amyloid proteins by cysteine
proteases: cathepsin B generates AA amyloid proteins and cathepsin L might
prevent their formation. Ann Rheum Dis 64: 808-815, 2005
5. 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. 102: 6297–6302, 2005