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

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Standard

Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s. / Nissen, Mogens Holst; Roepstorff, P; Thim, L; Dunbar, B; Fothergill, J E.

I: European Journal of Biochemistry, Bind 189, Nr. 2, 1990, s. 423-9.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Nissen, MH, Roepstorff, P, Thim, L, Dunbar, B & Fothergill, JE 1990, 'Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s.', European Journal of Biochemistry, bind 189, nr. 2, s. 423-9.

APA

Nissen, M. H., Roepstorff, P., Thim, L., Dunbar, B., & Fothergill, J. E. (1990). Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s. European Journal of Biochemistry, 189(2), 423-9.

Vancouver

Nissen MH, Roepstorff P, Thim L, Dunbar B, Fothergill JE. Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s. European Journal of Biochemistry. 1990;189(2):423-9.

Author

Nissen, Mogens Holst ; Roepstorff, P ; Thim, L ; Dunbar, B ; Fothergill, J E. / Limited proteolysis of beta 2-microglobulin at Lys-58 by complement component C1s. I: European Journal of Biochemistry. 1990 ; Bind 189, Nr. 2. s. 423-9.

Bibtex

@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",

}

RIS

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

VL - 189

SP - 423

EP - 429

JO - FEBS Journal

JF - FEBS Journal

SN - 1742-464X

IS - 2

ER -

ID: 8746747