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J Biol Chem. 2015 Oct 30;290(44):26430-6. doi: 10.1074/jbc.R115.653097. Epub 2015 Sep 9.

Specific chaperones and regulatory domains in control of amyloid formation.

Author information

1
From the Department of Chemistry, University of Oxford, South Parks Road, Oxford OX1 5QY, United Kingdom.
2
the Department of Neurobiology, Care Sciences and Society (NVS), Center for Alzheimer Research, Karolinska Institutet - Novum, 141 57 Huddinge, Sweden, the Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, The Biomedical Centre, Box 575, 751 23 Uppsala, Sweden.
3
the Department of Neurobiology, Care Sciences and Society (NVS), Center for Alzheimer Research, Karolinska Institutet - Novum, 141 57 Huddinge, Sweden.
4
the Department of Medical Biochemistry and Biophysics (MBB), Karolinska Institutet, SE-171 77 Stockholm, Sweden, and Hans.Jornvall@ki.se.
5
the Department of Neurobiology, Care Sciences and Society (NVS), Center for Alzheimer Research, Karolinska Institutet - Novum, 141 57 Huddinge, Sweden, the Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, The Biomedical Centre, Box 575, 751 23 Uppsala, Sweden, the Institute of Mathematics and Natural Sciences, Tallinn University, Narva mnt 25, 101 20 Tallinn, Estonia Janne.Johansson@ki.se.

Abstract

Many proteins can form amyloid-like fibrils in vitro, but only about 30 amyloids are linked to disease, whereas some proteins form physiological amyloid-like assemblies. This raises questions of how the formation of toxic protein species during amyloidogenesis is prevented or contained in vivo. Intrinsic chaperoning or regulatory factors can control the aggregation in different protein systems, thereby preventing unwanted aggregation and enabling the biological use of amyloidogenic proteins. The molecular actions of these chaperones and regulators provide clues to the prevention of amyloid disease, as well as to the harnessing of amyloidogenic proteins in medicine and biotechnology.

KEYWORDS:

BRICHOS; lung surfactant; molecular chaperone; pH regulation; prion; protein domain; protein structure; spider silk protein

PMID:
26354437
PMCID:
PMC4646301
DOI:
10.1074/jbc.R115.653097
[Indexed for MEDLINE]
Free PMC Article

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