Proteolysis of the heavy chain of major histocompatibility complex class I antigens by complement component C1s.

H Eriksson; Mogens Holst Nissen

Proteolysis of the heavy chain of major histocompatibility complex class I antigens by complement component C1s.

H Eriksson, Mogens Holst Nissen

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

31 Citationer (Scopus)

Abstract

Udgivelsesdato: 1990-Feb-9

Originalsprog	Engelsk
Tidsskrift	BBA General Subjects
Vol/bind	1037
Udgave nummer	2
Sider (fra-til)	209-15
Antal sider	6
ISSN	0304-4165
Status	Udgivet - 1990

Bibliografisk note

Keywords: Animals; Binding Sites; Chromatography, Affinity; Complement C1s; Epitopes; H-2 Antigens; Histocompatibility Antigens Class I; Humans; Major Histocompatibility Complex; Mice; Molecular Weight; Rats

Citationsformater

@article{1d3af8e0ba3511ddae57000ea68e967b,

title = "Proteolysis of the heavy chain of major histocompatibility complex class I antigens by complement component C1s.",

abstract = "The major histocompatibility complex (MHC) class I antigens contain a light chain, beta 2-microglobulin, non-covalently associated to the transmembrane heavy alpha-chain carrying the allotypic determinants. Since the C1q complement component is known to associate with beta 2-microglobulin, and we recently found that activated C1s complement was capable of cleaving beta 2-microglobulin, we decided to investigate the proteolytic activity of C1 complement towards the heavy chain of class I antigens. Our results demonstrate that human C1s complement cleaves the heavy chain of human class I antigens into at least two fragments, with apparent molecular weights of 22,000 and 24,000 g/mol on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), under both reducing and non-reducing conditions. The cleavage of the heavy chain is inhibited by the presence of C1 esterase inhibitor. The molecular weights of the fragments are in agreement with the cleavage located in the area between the disulphide loops of the alpha 2-and alpha 3-domains of the heavy chain. In addition human C1s complement is able to cleave H-2 antigens from mouse in a similar fashion but not rat MHC class I antigen or mouse MHC class II antigen (I-Ad). Mouse MHC class I antigen-specific determinants could also be detected in supernatant from mouse spleen cells incubated with C1r and C1s. These results indicate the presence in the body fluids of a non-membrane-bound soluble form of the alpha 1-and alpha 2-domains which represent the binding site for antigenic peptides.",

author = "H Eriksson and Nissen, {Mogens Holst}",

note = "Keywords: Animals; Binding Sites; Chromatography, Affinity; Complement C1s; Epitopes; H-2 Antigens; Histocompatibility Antigens Class I; Humans; Major Histocompatibility Complex; Mice; Molecular Weight; Rats",

year = "1990",

language = "English",

volume = "1037",

pages = "209--15",

journal = "BBA General Subjects",

issn = "0304-4165",

publisher = "Elsevier",

number = "2",

}

TY - JOUR

T1 - Proteolysis of the heavy chain of major histocompatibility complex class I antigens by complement component C1s.

AU - Eriksson, H

AU - Nissen, Mogens Holst

N1 - Keywords: Animals; Binding Sites; Chromatography, Affinity; Complement C1s; Epitopes; H-2 Antigens; Histocompatibility Antigens Class I; Humans; Major Histocompatibility Complex; Mice; Molecular Weight; Rats

PY - 1990

Y1 - 1990

N2 - The major histocompatibility complex (MHC) class I antigens contain a light chain, beta 2-microglobulin, non-covalently associated to the transmembrane heavy alpha-chain carrying the allotypic determinants. Since the C1q complement component is known to associate with beta 2-microglobulin, and we recently found that activated C1s complement was capable of cleaving beta 2-microglobulin, we decided to investigate the proteolytic activity of C1 complement towards the heavy chain of class I antigens. Our results demonstrate that human C1s complement cleaves the heavy chain of human class I antigens into at least two fragments, with apparent molecular weights of 22,000 and 24,000 g/mol on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), under both reducing and non-reducing conditions. The cleavage of the heavy chain is inhibited by the presence of C1 esterase inhibitor. The molecular weights of the fragments are in agreement with the cleavage located in the area between the disulphide loops of the alpha 2-and alpha 3-domains of the heavy chain. In addition human C1s complement is able to cleave H-2 antigens from mouse in a similar fashion but not rat MHC class I antigen or mouse MHC class II antigen (I-Ad). Mouse MHC class I antigen-specific determinants could also be detected in supernatant from mouse spleen cells incubated with C1r and C1s. These results indicate the presence in the body fluids of a non-membrane-bound soluble form of the alpha 1-and alpha 2-domains which represent the binding site for antigenic peptides.

AB - The major histocompatibility complex (MHC) class I antigens contain a light chain, beta 2-microglobulin, non-covalently associated to the transmembrane heavy alpha-chain carrying the allotypic determinants. Since the C1q complement component is known to associate with beta 2-microglobulin, and we recently found that activated C1s complement was capable of cleaving beta 2-microglobulin, we decided to investigate the proteolytic activity of C1 complement towards the heavy chain of class I antigens. Our results demonstrate that human C1s complement cleaves the heavy chain of human class I antigens into at least two fragments, with apparent molecular weights of 22,000 and 24,000 g/mol on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE), under both reducing and non-reducing conditions. The cleavage of the heavy chain is inhibited by the presence of C1 esterase inhibitor. The molecular weights of the fragments are in agreement with the cleavage located in the area between the disulphide loops of the alpha 2-and alpha 3-domains of the heavy chain. In addition human C1s complement is able to cleave H-2 antigens from mouse in a similar fashion but not rat MHC class I antigen or mouse MHC class II antigen (I-Ad). Mouse MHC class I antigen-specific determinants could also be detected in supernatant from mouse spleen cells incubated with C1r and C1s. These results indicate the presence in the body fluids of a non-membrane-bound soluble form of the alpha 1-and alpha 2-domains which represent the binding site for antigenic peptides.

M3 - Journal article

C2 - 1689590

SN - 0304-4165

VL - 1037

SP - 209

EP - 215

JO - BBA General Subjects

JF - BBA General Subjects

IS - 2

ER -