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Aspects on human amyloid forms and their fibril polypeptides
Author(s) -
Westermark Per
Publication year - 2005
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2005.05024.x
Subject(s) - fibril , amyloid fibril , amyloid (mycology) , chemistry , biophysics , in vivo , protein aggregation , amyloid disease , microbiology and biotechnology , biochemistry , amyloid β , biology , medicine , pathology , inorganic chemistry , disease
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 prion‐like mechanism occurs in humans is not known, but can definitely not be ruled out.