Abstract:
:alpha 1-Antitrypsin (alpha 1-AT) accumulates in the rough endoplasmic reticulum through a mechanism of polymerization. Polymerization is favored by the incorrect tertiary structure of the alpha 1-AT caused by a point mutation at position 342 of the protein. Accumulation of alpha 1-AT in the liver cells (and in hepatocytes and colangiocytes) is not sufficient per se to explain the liver disease that is manifested in a minority of PiZ subjects and thus, a trigger factor must be hypothesized. A virus (hepatitis C virus or some other kind of virus not identified as yet) is among the most probable trigger factors. In Z subjects (among the general population), relevant liver disease is probably a more rare event than thought in the past and most of these subjects escape major liver disease. Usually, liver disease is not a significant problem in patients with COPD.
journal_name
Chestjournal_title
Chestauthors
Massi Gdoi
10.1378/chest.110.6_supplement.251ssubject
Has Abstractpub_date
1996-12-01 00:00:00pages
251S-255Sissue
6 Suppleissn
0012-3692issn
1931-3543pii
S0012-3692(15)43425-7journal_volume
110pub_type
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