Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s.

Mogens Holst Nissen; P Roepstorff; L Thim; B Dunbar; J E Fothergill

Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s.

Mogens Holst Nissen, P Roepstorff, L Thim, B Dunbar, J E Fothergill

Department of Immunology and Microbiology

43 Citations (Scopus)

Abstract

We have now demonstrated that activated complement component C1s cleaves beta 2-microglobulin at the position identical to that at which beta 2-microglobulin is cleaved in serum of patients suffering from lung cancer. The main cleavage is in the disulphide loop C-terminal to Lys-58, generating a modified form of beta 2-microglobulin with a two-chain structure. The C-terminal Lys-58 in the A chain is highly susceptible to removal by a carboxypeptidase-B-like activity causing the formation of des-Lys58-beta 2-microglobulin. This is the first demonstration of a noncomplement protein substrate for the proteolytic activity of C1s. The C1s-induced cleavage of beta 2-microglobulin can be inhibited in the presence of C1 esterase inhibitor, demonstrating a regulatory function of C1 esterase inhibitor in the C1s-induced cleavage of beta 2-microglobulin.

Original language	English
Journal	European Journal of Biochemistry
Volume	189
Issue number	2
Pages (from-to)	423-9
Number of pages	6
ISSN	0014-2956
Publication status	Published - 1990

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@article{06e978a0ba3511ddae57000ea68e967b,

title = "Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s.",

abstract = "We have now demonstrated that activated complement component C1s cleaves beta 2-microglobulin at the position identical to that at which beta 2-microglobulin is cleaved in serum of patients suffering from lung cancer. The main cleavage is in the disulphide loop C-terminal to Lys-58, generating a modified form of beta 2-microglobulin with a two-chain structure. The C-terminal Lys-58 in the A chain is highly susceptible to removal by a carboxypeptidase-B-like activity causing the formation of des-Lys58-beta 2-microglobulin. This is the first demonstration of a noncomplement protein substrate for the proteolytic activity of C1s. The C1s-induced cleavage of beta 2-microglobulin can be inhibited in the presence of C1 esterase inhibitor, demonstrating a regulatory function of C1 esterase inhibitor in the C1s-induced cleavage of beta 2-microglobulin.",

author = "Nissen, {Mogens Holst} and P Roepstorff and L Thim and B Dunbar and Fothergill, {J E}",

note = "Keywords: Amino Acid Sequence; Complement C1r; Complement C1s; Electrophoresis, Polyacrylamide Gel; Humans; Lysine; Mass Spectrometry; Molecular Sequence Data; Molecular Weight; Peptide Fragments; Substrate Specificity; beta 2-Microglobulin",

year = "1990",

language = "English",

volume = "189",

pages = "423--9",

journal = "FEBS Journal",

issn = "1742-464X",

publisher = "Springer Verlag",

number = "2",

}

TY - JOUR

T1 - Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s.

AU - Nissen, Mogens Holst

AU - Roepstorff, P

AU - Thim, L

AU - Dunbar, B

AU - Fothergill, J E

N1 - Keywords: Amino Acid Sequence; Complement C1r; Complement C1s; Electrophoresis, Polyacrylamide Gel; Humans; Lysine; Mass Spectrometry; Molecular Sequence Data; Molecular Weight; Peptide Fragments; Substrate Specificity; beta 2-Microglobulin

PY - 1990

Y1 - 1990

N2 - We have now demonstrated that activated complement component C1s cleaves beta 2-microglobulin at the position identical to that at which beta 2-microglobulin is cleaved in serum of patients suffering from lung cancer. The main cleavage is in the disulphide loop C-terminal to Lys-58, generating a modified form of beta 2-microglobulin with a two-chain structure. The C-terminal Lys-58 in the A chain is highly susceptible to removal by a carboxypeptidase-B-like activity causing the formation of des-Lys58-beta 2-microglobulin. This is the first demonstration of a noncomplement protein substrate for the proteolytic activity of C1s. The C1s-induced cleavage of beta 2-microglobulin can be inhibited in the presence of C1 esterase inhibitor, demonstrating a regulatory function of C1 esterase inhibitor in the C1s-induced cleavage of beta 2-microglobulin.

AB - We have now demonstrated that activated complement component C1s cleaves beta 2-microglobulin at the position identical to that at which beta 2-microglobulin is cleaved in serum of patients suffering from lung cancer. The main cleavage is in the disulphide loop C-terminal to Lys-58, generating a modified form of beta 2-microglobulin with a two-chain structure. The C-terminal Lys-58 in the A chain is highly susceptible to removal by a carboxypeptidase-B-like activity causing the formation of des-Lys58-beta 2-microglobulin. This is the first demonstration of a noncomplement protein substrate for the proteolytic activity of C1s. The C1s-induced cleavage of beta 2-microglobulin can be inhibited in the presence of C1 esterase inhibitor, demonstrating a regulatory function of C1 esterase inhibitor in the C1s-induced cleavage of beta 2-microglobulin.

M3 - Journal article

C2 - 2110898

SN - 1742-464X

VL - 189

SP - 423

EP - 429

JO - FEBS Journal

JF - FEBS Journal

IS - 2

ER -

Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s.

Abstract

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