tailieunhanh - Báo cáo khoa học: Aspects on human amyloid forms and their fibril polypeptides

Amyloid is anin vivo fibrillar substance containing a fibril protein and several additional molecules. Presently, 25 proteins have been reported as main fibril components. Why just a few proteins form amyloidin vivo is still insufficiently understood. Many fibril proteins appear as fragments of larger precursors and for some types it is not clear whether fragmentation comes before or after fibrillation. | iFEBS Journal MINIREVIEW Aspects on human amyloid forms and their fibril polypeptides Per Westermark Department of Genetics and Pathology Rudbeck Laboratory Uppsala University Sweden Keywords amyloid deposition prion protein folding seeding Correspondence P. Westermark Department of Genetics and Pathology Rudbeck Laboratory Uppsala University SE-751 85 Uppsala Sweden Fax 46 18 552739 Tel 46 18 6113849 E-mail Received 16 August 2005 accepted 18 October 2005 doi Amyloid is an in vivo fibrillar substance containing a fibril protein and several additional molecules. Presently 25 proteins have been reported as main fibril components. Why just a few proteins form amyloid in vivo is still insufficiently understood. Many fibril proteins appear as fragments of larger precursors and for some types it is not clear whether fragmentation comes before or after fibrillation. The self-assembly by amyloid proteins can be speeded up by seeding with preformed fibrils. In mice systemic amyloidoses are transmissible by a seeding mechanism. Whether this prionlike mechanism occurs in humans is not known but can definitely not be ruled out. Deposition of aggregated specific polypeptides as amyloid has attracted much attention during the last years. Amyloidosis has long been known as a group of diseases with widely spread often pronounced deposits in vital organs thereby being immediately life-threatening. The existence of small amyloid deposits limited to certain organs or tissues has also been known for some time although their amyloid nature was not immediately accepted. These localized amyloid forms were regarded as innocent bystanders or by-products of disease rather than being involved in their pathogenesis. This view has changed radically during the last decade. Now small amyloid deposits or more probably oligomeric preamyloid aggregates of specific amyloid fibril proteins are believed to be important in the pathogenesis .

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