Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.

H Eriksson; Mogens Holst Nissen

Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.

Department of Immunology and Microbiology

3 Citations (Scopus)

Abstract

Apart from cleaving C1s, we demonstrate for the first time that: 1) at concentrations found in serum, the activated forms of the complement components C1r in addition to C1s can cleave the heavy chain of MHC class I antigens, 2) the cleavage by C1r and C1s is seemingly dependent upon a native configuration of the MHC class I antigen, since heat denaturation of the HLA antigens reduce the cleavage. The proteolytic fragments following C1 cleavage were characterized by precipitation with Con A-Sepharose, anti-MHC class I and anti-beta 2-microglobulin antibodies. The proteolysis of the alpha-chain of MHC class I was shown to take place between the alpha 2- and alpha 3- domains as estimated by the Con A-Sepharose precipitation pattern on SDS-PAGE. The alpha 1/alpha 2 fragment was still shown to interact with beta 2-microglobulin as shown by immunoprecipitation.

Original language	English
Journal	Biochemical and Biophysical Research Communications
Volume	187
Issue number	2
Pages (from-to)	832-8
Number of pages	6
ISSN	0006-291X
Publication status	Published - 1992

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@article{94e84a60ba3411ddae57000ea68e967b,

title = "Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.",

abstract = "Apart from cleaving C1s, we demonstrate for the first time that: 1) at concentrations found in serum, the activated forms of the complement components C1r in addition to C1s can cleave the heavy chain of MHC class I antigens, 2) the cleavage by C1r and C1s is seemingly dependent upon a native configuration of the MHC class I antigen, since heat denaturation of the HLA antigens reduce the cleavage. The proteolytic fragments following C1 cleavage were characterized by precipitation with Con A-Sepharose, anti-MHC class I and anti-beta 2-microglobulin antibodies. The proteolysis of the alpha-chain of MHC class I was shown to take place between the alpha 2- and alpha 3- domains as estimated by the Con A-Sepharose precipitation pattern on SDS-PAGE. The alpha 1/alpha 2 fragment was still shown to interact with beta 2-microglobulin as shown by immunoprecipitation.",

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

note = "Keywords: Antibodies, Monoclonal; Cell Line; Complement C1r; Complement C1s; Electrophoresis, Polyacrylamide Gel; Glycosylation; Heat; Histocompatibility Antigens Class I; Humans; Immunosorbent Techniques; Molecular Weight; Peptide Fragments; Protein Conformation; Protein Denaturation; Structure-Activity Relationship",

year = "1992",

language = "English",

volume = "187",

pages = "832--8",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Elsevier",

number = "2",

}

TY - JOUR

T1 - Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.

AU - Eriksson, H

AU - Nissen, Mogens Holst

N1 - Keywords: Antibodies, Monoclonal; Cell Line; Complement C1r; Complement C1s; Electrophoresis, Polyacrylamide Gel; Glycosylation; Heat; Histocompatibility Antigens Class I; Humans; Immunosorbent Techniques; Molecular Weight; Peptide Fragments; Protein Conformation; Protein Denaturation; Structure-Activity Relationship

PY - 1992

Y1 - 1992

N2 - Apart from cleaving C1s, we demonstrate for the first time that: 1) at concentrations found in serum, the activated forms of the complement components C1r in addition to C1s can cleave the heavy chain of MHC class I antigens, 2) the cleavage by C1r and C1s is seemingly dependent upon a native configuration of the MHC class I antigen, since heat denaturation of the HLA antigens reduce the cleavage. The proteolytic fragments following C1 cleavage were characterized by precipitation with Con A-Sepharose, anti-MHC class I and anti-beta 2-microglobulin antibodies. The proteolysis of the alpha-chain of MHC class I was shown to take place between the alpha 2- and alpha 3- domains as estimated by the Con A-Sepharose precipitation pattern on SDS-PAGE. The alpha 1/alpha 2 fragment was still shown to interact with beta 2-microglobulin as shown by immunoprecipitation.

AB - Apart from cleaving C1s, we demonstrate for the first time that: 1) at concentrations found in serum, the activated forms of the complement components C1r in addition to C1s can cleave the heavy chain of MHC class I antigens, 2) the cleavage by C1r and C1s is seemingly dependent upon a native configuration of the MHC class I antigen, since heat denaturation of the HLA antigens reduce the cleavage. The proteolytic fragments following C1 cleavage were characterized by precipitation with Con A-Sepharose, anti-MHC class I and anti-beta 2-microglobulin antibodies. The proteolysis of the alpha-chain of MHC class I was shown to take place between the alpha 2- and alpha 3- domains as estimated by the Con A-Sepharose precipitation pattern on SDS-PAGE. The alpha 1/alpha 2 fragment was still shown to interact with beta 2-microglobulin as shown by immunoprecipitation.

M3 - Journal article

C2 - 1530639

SN - 0006-291X

VL - 187

SP - 832

EP - 838

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 2

ER -

Complement component C1r mediated cleavage of the heavy chain of the major histocompatibility class I antigens.

Abstract

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