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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1984-7-23
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pubmed:abstractText |
The effect of S-protein on the polymerization of C9 during assembly of the C5b-9 complex was examined. Utilizing SDS polyacrylamide gradient slab gel electrophoresis, tubular poly C9 was quantitated as SDS resistant protein of 1.1 to 1.3 X 10(6) molecular weight. Poly C9 formation occurred upon incubation of purified C5b-6, C7, C8 and C9 at molar ratios 1:1:1:12. Addition of purified S-protein to the protein mixture or to preassembled C5b-7 or C5b-8 blocked formation of poly C9 in a dose dependent fashion and gave rise to SC5b-9. SC5b-9 assembled from purified proteins or in zymosan-activated serum was visualized in the electron microscope as a wedge-shaped structure of 350 to 400 A length and 30 to 250 A width which lacked tubular poly C9 seen in images of the membrane attack complex (MAC). Using biotinyl-S-protein and colloidal gold particles coated with avidin, S-protein was located at the wide end of the wedge-like SC5b-9 complex. It is concluded that S-protein has a dual function in SC5b-9 assembly. It blocks the membrane site of C5b-7 and it inhibits C9 polymerization by SC5b-8. Accordingly, the main structural difference between SC5b-9 and the MAC is the lack of tubular poly C9.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Complement C9,
http://linkedlifedata.com/resource/pubmed/chemical/Complement Membrane Attack Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Complement System Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Polymers,
http://linkedlifedata.com/resource/pubmed/chemical/S-protein (control)
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pubmed:status |
MEDLINE
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pubmed:issn |
0108-0172
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
89-96
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pubmed:dateRevised |
2008-2-12
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pubmed:meshHeading |
pubmed-meshheading:6587746-Binding Sites,
pubmed-meshheading:6587746-Complement Activation,
pubmed-meshheading:6587746-Complement C9,
pubmed-meshheading:6587746-Complement Membrane Attack Complex,
pubmed-meshheading:6587746-Complement System Proteins,
pubmed-meshheading:6587746-Glycoproteins,
pubmed-meshheading:6587746-Humans,
pubmed-meshheading:6587746-Membrane Glycoproteins,
pubmed-meshheading:6587746-Molecular Weight,
pubmed-meshheading:6587746-Polymers,
pubmed-meshheading:6587746-Protein Conformation
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pubmed:year |
1984
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pubmed:articleTitle |
Inhibition of C9 polymerization within the SC5b-9 complex of complement by S-protein.
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pubmed:publicationType |
Journal Article,
Comparative Study,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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