Inhibition of C9 polymerization within the SC5b-9 complex of complement by S-protein

E. R. Podack, K. T. Preissner, H. J. Muller-Eberhard

Research output: Contribution to journalArticle

79 Citations (Scopus)

Abstract

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 106 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 Å length and 30 to 250 Å 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.

Original languageEnglish
Pages (from-to)89-96
Number of pages8
JournalActa Pathologica Microbiologica et Immunologica Scandinavica - Supplementum
Volume92
Issue number284
StatePublished - Jan 1 1984
Externally publishedYes

Fingerprint

Protein S
Polymerization
Complement System Proteins
Complement Membrane Attack Complex
Gold Colloid
Proteins
Zymosan
Avidin
Electrophoresis
Molecular Weight
Gels
complement C9 polymer
Electrons
Membranes
Serum
complement C5b-7 complex

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Inhibition of C9 polymerization within the SC5b-9 complex of complement by S-protein. / Podack, E. R.; Preissner, K. T.; Muller-Eberhard, H. J.

In: Acta Pathologica Microbiologica et Immunologica Scandinavica - Supplementum, Vol. 92, No. 284, 01.01.1984, p. 89-96.

Research output: Contribution to journalArticle

@article{74c852a1c7e0459d95f2cb2f49a904a2,
title = "Inhibition of C9 polymerization within the SC5b-9 complex of complement by S-protein",
abstract = "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 106 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 {\AA} length and 30 to 250 {\AA} 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.",
author = "Podack, {E. R.} and Preissner, {K. T.} and Muller-Eberhard, {H. J.}",
year = "1984",
month = "1",
day = "1",
language = "English",
volume = "92",
pages = "89--96",
journal = "APMIS. Supplementum",
issn = "0108-0210",
publisher = "Wiley-Blackwell",
number = "284",

}

TY - JOUR

T1 - Inhibition of C9 polymerization within the SC5b-9 complex of complement by S-protein

AU - Podack, E. R.

AU - Preissner, K. T.

AU - Muller-Eberhard, H. J.

PY - 1984/1/1

Y1 - 1984/1/1

N2 - 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 106 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 Å length and 30 to 250 Å 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.

AB - 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 106 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 Å length and 30 to 250 Å 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.

UR - http://www.scopus.com/inward/record.url?scp=0021273740&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0021273740&partnerID=8YFLogxK

M3 - Article

C2 - 6587746

AN - SCOPUS:0021273740

VL - 92

SP - 89

EP - 96

JO - APMIS. Supplementum

JF - APMIS. Supplementum

SN - 0108-0210

IS - 284

ER -