期刊
BIOPHYSICAL JOURNAL
卷 107, 期 8, 页码 1905-1912出版社
CELL PRESS
DOI: 10.1016/j.bpj.2014.08.030
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资金
- Villum Kann Rasmussen foundation
- Lundbeck Foundation
- Danish Cancer Society
- Danish National Research Foundation
- Medical Research Council [MR/L017431/1] Funding Source: researchfish
- Novo Nordisk Fonden [NNF13OC0006627] Funding Source: researchfish
- MRC [MR/L017431/1] Funding Source: UKRI
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.
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