Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin

Standard

Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin. / Ben Nasr, A; Herwald, H; Sjöbring, U; Renné, T; Müller-Esterl, W; Björck, L.

in: BIOCHEM J, Jahrgang 326 ( Pt 3), 15.09.1997, S. 657-60.

Publikationen: SCORING: Beitrag in Fachzeitschrift/ZeitungSCORING: ZeitschriftenaufsatzForschungBegutachtung

Harvard

Ben Nasr, A, Herwald, H, Sjöbring, U, Renné, T, Müller-Esterl, W & Björck, L 1997, 'Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin', BIOCHEM J, Jg. 326 ( Pt 3), S. 657-60.

APA

Ben Nasr, A., Herwald, H., Sjöbring, U., Renné, T., Müller-Esterl, W., & Björck, L. (1997). Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin. BIOCHEM J, 326 ( Pt 3), 657-60.

Vancouver

Ben Nasr A, Herwald H, Sjöbring U, Renné T, Müller-Esterl W, Björck L. Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin. BIOCHEM J. 1997 Sep 15;326 ( Pt 3):657-60.

Bibtex

@article{bafd13a1703149e1b3056d9a4a216538,
title = "Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin",
abstract = "H-kininogen (high-molecular-mass kininogen, HK) is the precursor of the vasoactive peptide hormone bradykinin (BK). Previous work has demonstrated that HK binds to Streptococcus pyogenes through M-proteins, fibrous surface proteins and important virulence factors of these bacteria. Here we find that M-protein-expressing bacteria absorb HK from human plasma. The HK bound to the bacteria was found to be cleaved, and analysis of the degradation pattern suggested that the cleavage of HK at the bacterial surface is associated with the release of BK. Moreover, addition of activated plasma prekallikrein to bacteria preincubated with human plasma, resulted in BK release. This mechanism, by which a potent vasoactive and proinflammatory peptide is generated at the site of infection, should influence the host-parasite relationship during S. pyogenes infections.",
keywords = "Bradykinin, Humans, Kininogens, Protein Binding, Streptococcus pyogenes",
author = "{Ben Nasr}, A and H Herwald and U Sj{\"o}bring and T Renn{\'e} and W M{\"u}ller-Esterl and L Bj{\"o}rck",
year = "1997",
month = sep,
day = "15",
language = "English",
volume = "326 ( Pt 3)",
pages = "657--60",
journal = "BIOCHEM J",
issn = "0264-6021",
publisher = "PORTLAND PRESS LTD",

}

RIS

TY - JOUR

T1 - Absorption of kininogen from human plasma by Streptococcus pyogenes is followed by the release of bradykinin

AU - Ben Nasr, A

AU - Herwald, H

AU - Sjöbring, U

AU - Renné, T

AU - Müller-Esterl, W

AU - Björck, L

PY - 1997/9/15

Y1 - 1997/9/15

N2 - H-kininogen (high-molecular-mass kininogen, HK) is the precursor of the vasoactive peptide hormone bradykinin (BK). Previous work has demonstrated that HK binds to Streptococcus pyogenes through M-proteins, fibrous surface proteins and important virulence factors of these bacteria. Here we find that M-protein-expressing bacteria absorb HK from human plasma. The HK bound to the bacteria was found to be cleaved, and analysis of the degradation pattern suggested that the cleavage of HK at the bacterial surface is associated with the release of BK. Moreover, addition of activated plasma prekallikrein to bacteria preincubated with human plasma, resulted in BK release. This mechanism, by which a potent vasoactive and proinflammatory peptide is generated at the site of infection, should influence the host-parasite relationship during S. pyogenes infections.

AB - H-kininogen (high-molecular-mass kininogen, HK) is the precursor of the vasoactive peptide hormone bradykinin (BK). Previous work has demonstrated that HK binds to Streptococcus pyogenes through M-proteins, fibrous surface proteins and important virulence factors of these bacteria. Here we find that M-protein-expressing bacteria absorb HK from human plasma. The HK bound to the bacteria was found to be cleaved, and analysis of the degradation pattern suggested that the cleavage of HK at the bacterial surface is associated with the release of BK. Moreover, addition of activated plasma prekallikrein to bacteria preincubated with human plasma, resulted in BK release. This mechanism, by which a potent vasoactive and proinflammatory peptide is generated at the site of infection, should influence the host-parasite relationship during S. pyogenes infections.

KW - Bradykinin

KW - Humans

KW - Kininogens

KW - Protein Binding

KW - Streptococcus pyogenes

M3 - SCORING: Journal article

C2 - 9307013

VL - 326 ( Pt 3)

SP - 657

EP - 660

JO - BIOCHEM J

JF - BIOCHEM J

SN - 0264-6021

ER -