Cross-linking of ubiquitin, HSP27, parkin, and α-synuclein by γ-glutamyl-ε-lysine bonds in Alzheimer’s neurofibrillary tangles ZOLTÁN NEMES * ,1 , B. DEVREESE † , P. M. STEINERT ‡ , J. VAN BEEUMEN † and L. FÉSÜS § Departments of * Psychiatry and § Biochemistry and Molecular Biology and Signaling and Apoptosis Research Group, Hungarian Academy of Sciences, Research Center for Molecular Medicine, University of Debrecen, Debrecen, Hungary; † Laboratory of Protein Biochemistry and Protein Engineering, Ghent University, Gent, Belgium; and ‡ Laboratory of Skin Biology, NIAMS, NIH, Bethesda, Maryland, USA 1 Correspondence: Department of Psychiatry, University of Debrecen Medical and Health Sciences Center, Nagyerdei krt. 98. H-4012 Debrecen, Hungary. E-mail: znemes@dote.hu <h3>SPECIFIC AIMS</h3> 1) To analyze the frequency of the γ-glutamyl-ε-lysine (GGEL) cross-linkages in Alzheimer’s disease (AD) brain tissue and isolate disease-related cross-linked protein aggregates to determine the density of GGEL cross-links in those. AD specimen were compared with age-matched nondemented and younger non-neurological controls. 2) To identify the proteins and specific amino acid residues involved in GGEL cross-linking and estimate their relative contribution to the total of cross-links in intraneuronal protein aggregates. <h3>PRINCIPAL FINDINGS</h3> <h3>1. Frequency of GGEL cross-links in AD cortex is higher than in controls</h3> We
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Cross-linking of ubiquitin, HSP27, parkin, and α-synuclein by γ-glutamyl-ε-lysine bonds in Alzheimers neurofibrillary tangles
NEMES, ZOLTÁN; DEVREESE, B.; STEINERT, P. M.; VAN BEEUMEN, J.; FÉSÜS, L.
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, Volume 18 (10): 1135
Fed of American Socs for Experimental Biology – Jul 1, 2004
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