TAILIEUCHUNG - Báo cáo khoa học: Interaction of human stefin B in the prefibrillar oligomeric form with membranes Correlation with cellular toxicity

Protein aggregation is central to most neurodegenerative diseases, as shown by familial case studies and by animal models. A modified ‘amyloid cas-cade’ hypothesis for Alzheimer’s disease states that prefibrillar oligomers, also called amyloid-b-derived diffusible ligands or globular oligomers, are the responsible toxic agent. It has been proposed that these oligomeric spe-cies, as shown for amyloid-b, b2 -microglobulin or prion fragments, exert toxicity by forming pores in membranes, initiating a cascade of detrimental events for the cell. . | iFEBS Journal Interaction of human stefin B in the prefibrillar oligomeric form with membranes Correlation with cellular toxicity Gregor Anderluh1 Ion Gutierrez-Aguirre1 Sabina Rabzelj2 Slavko Ceru2 Natasa Kopitar-Jerala2 Peter Macek1 Vito Turk2 and Eva Zerovnik2 1 Department of Biology BiotechnicalFaculty University of Ljubljana Slovenia 2 Department of Biochemistry and Molecular Biology Jozef Stefan Institute Ljubljana Slovenia Keywords amyloid toxins conformationaldisease cystatins lipid binding prefibrillar oligomers Correspondence E. Zerovnik Department of Biochemistry and Molecular Biology JoZef Stefan Institute Jamova 39 1000 Ljubljana Slovenia Fax 386 477 3984 E-mail Received 21 February 2005 revised 6 April 2005 accepted 12 April 2005 doi Protein aggregation is central to most neurodegenerative diseases as shown by familial case studies and by animal models. A modified amyloid cascade hypothesis for Alzheimer s disease states that prefibrillar oligomers also called amyloid-b-derived diffusible ligands or globular oligomers are the responsible toxic agent. It has been proposed that these oligomeric species as shown for amyloid-b b2-microglobulin or prion fragments exert toxicity by forming pores in membranes initiating a cascade of detrimental events for the cell. Interaction of granular aggregates and globular oligomers of an amyloidogenic protein human stefin B with model lipid membranes and monolayers was studied. Prefibrillar oligomers aggregates of stefin B are shown to cause concentration-dependent membrane leaking in contrast to the homologous stefin A. Prefibrillar oligomers aggregates of stefin B also increase the surface pressure at an air-water interface . they have amphipathic character and are surface seeking. In addition they show stronger interaction with 1 2-dioleoyl-sn-glycero-3-phosphocholine and 1 2-dioleoyl-sn-glycero-3- phospho-rac- 1-glycerol monolayers than native stefin A or .

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