The heparin binding domain of S-protein/vitronectin binds to complement components C7, C8, and C9 and perforin from cytolytic T-cells and inhibits their lytic activities

Details

Serval ID
serval:BIB_CC6879DD2B0F
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
The heparin binding domain of S-protein/vitronectin binds to complement components C7, C8, and C9 and perforin from cytolytic T-cells and inhibits their lytic activities
Journal
Biochemistry
Author(s)
Tschopp  J., Masson  D., Schafer  S., Peitsch  M., Preissner  K. T.
ISSN
0006-2960 (Print)
Publication state
Published
Issued date
05/1988
Volume
27
Number
11
Pages
4103-9
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: May 31
Abstract
S-Protein/vitronectin is a serum glycoprotein that inhibits the lytic activity of the membrane attack complex of complement, i.e., of the complex including the proteins C5b, C6, C7, C8, and C9n. We show that intact S-protein/vitronectin or its cyanogen bromide generated fragments also inhibit the hemolysis mediated by perforin from cytotoxic T-cells at 45 and 11 microM, respectively. The glycosaminoglycan binding site of S-protein/vitronectin is responsible for the inhibition, since a synthetic peptide corresponding to a part of this highly basic domain (amino acid residues 348-360) inhibits complement- as well as perforin-mediated cytolysis. In the case of C9, the synthetic peptide binds to the acidic residues occurring in its N-terminal cysteine-rich domain (residues 101-111). Antibodies raised against this particular segment react 25-fold better with the polymerized form of C9 as compared with its monomeric form, indicating that this site becomes exposed only upon the hydrophilic-amphiphilic transition of C9. Since the cysteine-rich domain of C9 has been shown to be highly conserved in C6, C7, and C8 as well as in perforin, the inhibition of the lytic activities of these molecules by S-protein/vitronectin or by peptides corresponding to its heparin binding site may be explained by a similar mechanism.
Keywords
Animals Antibodies, Monoclonal/diagnostic use Binding, Competitive Chromatography, Affinity Complement C7/metabolism Complement C8/metabolism Complement C9/metabolism Complement System Proteins/*metabolism Electrophoresis, Polyacrylamide Gel Glycoproteins/*metabolism Hemolysis Heparin/*metabolism Immunochemistry Membrane Glycoproteins/*metabolism Membrane Proteins/*metabolism Peptides/metabolism Pore Forming Cytotoxic Proteins Sheep T-Lymphocytes, Cytotoxic/*metabolism Vitronectin
Pubmed
Web of science
Create date
24/01/2008 15:19
Last modification date
20/08/2019 15:47
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