The Shapes of Z-alpha(1)-Antitrypsin Polymers in Solution Support the C-Terminal Domain-Swap Mechanism of Polymerization
(2014) In Biophysical Journal 107(8). p.1905-1912- Abstract
- Emphysema and liver cirrhosis can be caused by the Z mutation (Glu342Lys) in the serine protease inhibitor alpha 1-antitrypsin (alpha 1AT), which is found in more than 4% of the Northern European population. Homozygotes experience deficiency in the lung concomitantly with a massive accumulation of polymers within hepatocytes, causing their destruction. Recently, it was proposed that Z-alpha 1AT polymerizes by a C-terminal domain swap. In this study, small-angle x-ray scattering (SAXS) was used to characterize Z-alpha 1AT polymers in solution. The data show that the Z-alpha 1AT trimer, tetramer, and pentamer all form ring-like structures in strong support of a common domain-swap polymerization mechanism that can lead to self-terminating... (More)
- Emphysema and liver cirrhosis can be caused by the Z mutation (Glu342Lys) in the serine protease inhibitor alpha 1-antitrypsin (alpha 1AT), which is found in more than 4% of the Northern European population. Homozygotes experience deficiency in the lung concomitantly with a massive accumulation of polymers within hepatocytes, causing their destruction. Recently, it was proposed that Z-alpha 1AT polymerizes by a C-terminal domain swap. In this study, small-angle x-ray scattering (SAXS) was used to characterize Z-alpha 1AT polymers in solution. The data show that the Z-alpha 1AT trimer, tetramer, and pentamer all form ring-like structures in strong support of a common domain-swap polymerization mechanism that can lead to self-terminating polymers. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/4780778
- author
- Behrens, Manja LU ; Sendall, Timothy J. ; Pedersen, Jan S. ; Kjeldgaard, Morten ; Huntington, James A. and Jensen, Jan K.
- organization
- publishing date
- 2014
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biophysical Journal
- volume
- 107
- issue
- 8
- pages
- 1905 - 1912
- publisher
- Cell Press
- external identifiers
-
- wos:000343682700016
- pmid:25418171
- scopus:84908231015
- pmid:25418171
- ISSN
- 1542-0086
- DOI
- 10.1016/j.bpj.2014.08.030
- language
- English
- LU publication?
- yes
- id
- 4b078246-b01e-486b-9446-eef8be37a00d (old id 4780778)
- date added to LUP
- 2016-04-01 10:58:29
- date last changed
- 2025-04-04 15:12:20
@article{4b078246-b01e-486b-9446-eef8be37a00d,
abstract = {{Emphysema and liver cirrhosis can be caused by the Z mutation (Glu342Lys) in the serine protease inhibitor alpha 1-antitrypsin (alpha 1AT), which is found in more than 4% of the Northern European population. Homozygotes experience deficiency in the lung concomitantly with a massive accumulation of polymers within hepatocytes, causing their destruction. Recently, it was proposed that Z-alpha 1AT polymerizes by a C-terminal domain swap. In this study, small-angle x-ray scattering (SAXS) was used to characterize Z-alpha 1AT polymers in solution. The data show that the Z-alpha 1AT trimer, tetramer, and pentamer all form ring-like structures in strong support of a common domain-swap polymerization mechanism that can lead to self-terminating polymers.}},
author = {{Behrens, Manja and Sendall, Timothy J. and Pedersen, Jan S. and Kjeldgaard, Morten and Huntington, James A. and Jensen, Jan K.}},
issn = {{1542-0086}},
language = {{eng}},
number = {{8}},
pages = {{1905--1912}},
publisher = {{Cell Press}},
series = {{Biophysical Journal}},
title = {{The Shapes of Z-alpha(1)-Antitrypsin Polymers in Solution Support the C-Terminal Domain-Swap Mechanism of Polymerization}},
url = {{http://dx.doi.org/10.1016/j.bpj.2014.08.030}},
doi = {{10.1016/j.bpj.2014.08.030}},
volume = {{107}},
year = {{2014}},
}