Folding related dimerization of human cystatin C
(1996) In Journal of Biological Chemistry 271(3). p.1314-1321- Abstract
- With the aim to improve our understanding of the structural basis for protein self-association and aggregation, in particular in relationship to protein refolding and amyloid formation, folding-related processes for human cystatin C have been studied. Using NMR spectroscopy together with chromatographic and electrophoretic methods, a self-association process resulting in dimer formation for protein samples treated with denaturing agents as well as for samples subjected to low pH or high temperature conditions could be studied with amino acid resolution. In all three cases, the dimerization involves properly folded molecules and proceeds via the reactive site of the inhibitor, which leads to complete loss of its biological activity. This... (More)
- With the aim to improve our understanding of the structural basis for protein self-association and aggregation, in particular in relationship to protein refolding and amyloid formation, folding-related processes for human cystatin C have been studied. Using NMR spectroscopy together with chromatographic and electrophoretic methods, a self-association process resulting in dimer formation for protein samples treated with denaturing agents as well as for samples subjected to low pH or high temperature conditions could be studied with amino acid resolution. In all three cases, the dimerization involves properly folded molecules and proceeds via the reactive site of the inhibitor, which leads to complete loss of its biological activity. This dimerization process has potential relevance for amyloid formation by the brain hemorrhage-causing Leu-Gln variant of cystatin C. The results also indicate that cystatin C dimerization and inactivation may occur in acidified compartments in vivo, which could be relevant for the physiological regulation of cysteine proteinase activity. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1111055
- author
- Ekiel, Irena and Abrahamson, Magnus LU
- organization
- publishing date
- 1996
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 271
- issue
- 3
- pages
- 1314 - 1321
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- scopus:0030052426
- ISSN
- 1083-351X
- language
- English
- LU publication?
- yes
- id
- 4ff789a4-1810-40da-8e53-8775de8ae102 (old id 1111055)
- alternative location
- http://www.jbc.org/cgi/content/full/271/3/1314
- date added to LUP
- 2016-04-01 12:12:13
- date last changed
- 2022-02-03 19:01:27
@article{4ff789a4-1810-40da-8e53-8775de8ae102,
abstract = {{With the aim to improve our understanding of the structural basis for protein self-association and aggregation, in particular in relationship to protein refolding and amyloid formation, folding-related processes for human cystatin C have been studied. Using NMR spectroscopy together with chromatographic and electrophoretic methods, a self-association process resulting in dimer formation for protein samples treated with denaturing agents as well as for samples subjected to low pH or high temperature conditions could be studied with amino acid resolution. In all three cases, the dimerization involves properly folded molecules and proceeds via the reactive site of the inhibitor, which leads to complete loss of its biological activity. This dimerization process has potential relevance for amyloid formation by the brain hemorrhage-causing Leu-Gln variant of cystatin C. The results also indicate that cystatin C dimerization and inactivation may occur in acidified compartments in vivo, which could be relevant for the physiological regulation of cysteine proteinase activity.}},
author = {{Ekiel, Irena and Abrahamson, Magnus}},
issn = {{1083-351X}},
language = {{eng}},
number = {{3}},
pages = {{1314--1321}},
publisher = {{American Society for Biochemistry and Molecular Biology}},
series = {{Journal of Biological Chemistry}},
title = {{Folding related dimerization of human cystatin C}},
url = {{http://www.jbc.org/cgi/content/full/271/3/1314}},
volume = {{271}},
year = {{1996}},
}