Membranolysis by the ninth component of human complement.

Details

Serval ID
serval:BIB_A655D8BD2F1A
Type
Article: article from journal or magazin.
Collection
Publications
Title
Membranolysis by the ninth component of human complement.
Journal
Biochemical and Biophysical Research Communications
Author(s)
Tschopp J., Podack E.R.
ISSN
0006-291X (Print)
ISSN-L
0006-291X
Publication state
Published
Issued date
1981
Volume
100
Number
3
Pages
1409-1414
Language
english
Abstract
The lytic property of isolated C9 was shown by using heat (48°C) to induce polymerization of C9, which was then exposed to egg lecithin vesicles containing carboxyfluorescein. In this environment, C9 penetrated the vesicles and released the marker. C5b-9 and C5b-8 also released carboxyfluorescein at 48°C, as did C5b-7 to a lesser extent. However, neither isolated C5b-6, C7, C8 nor albumin caused such release. At 30°C, the C9 remained in the monomeric form and could not lyse the vesicles.
C9 polymers formed at 48°C were ring-shaped with an internal diameter of approximately 100 Å and an outer diameter of approximately 180 Å. These rings of C9 polymers strikingly resembled the ultrastructures formed by the membrane attack complex of complement, viewed from the top.
Our results indicate that polymeric C9 causes the membranolysis of phospholipid vesicles and, hence, that C9 alone is a cytotoxic molecule.
Keywords
Complement C9/metabolism, Complement System Proteins/metabolism, Fluoresceins, Humans, Liposomes, Macromolecular Substances, Microscopy, Electron, Phosphatidylcholines
Pubmed
Web of science
Create date
24/01/2008 15:19
Last modification date
20/08/2019 15:11
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