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Plasminogen binding and activation at the surface of Helicobacter pylori CCUG 17874

Pantzar, Martina; Ljungh, Åsa LU and Wadström, Torkel LU (1998) In Infection and Immunity 66(10). p.4976-4980
Abstract
The binding of iodine-labelled plasminogen to Helicobacter pylori CCUG 17874 was characterized. Inhibition of the binding was observed after preincubation of H. pylori cells with nonradiolabelled plasminogen, lysine, or the lysine analogue -aminocaproic acid. Fragments of plasminogen, kringles 1 to 3, kringle 4, and mini-plasminogen, were also studied as potential inhibitors. Mini-plasminogen caused total inhibition of the plasminogen binding, while the other fragments caused only partial inhibition. These findings suggest that H. pylori binds specifically the fifth kringle structure of the plasminogen molecule. Plasminogen binding to H. pylori seems to be independent of culture media and independent of the presence of the... (More)
The binding of iodine-labelled plasminogen to Helicobacter pylori CCUG 17874 was characterized. Inhibition of the binding was observed after preincubation of H. pylori cells with nonradiolabelled plasminogen, lysine, or the lysine analogue -aminocaproic acid. Fragments of plasminogen, kringles 1 to 3, kringle 4, and mini-plasminogen, were also studied as potential inhibitors. Mini-plasminogen caused total inhibition of the plasminogen binding, while the other fragments caused only partial inhibition. These findings suggest that H. pylori binds specifically the fifth kringle structure of the plasminogen molecule. Plasminogen binding to H. pylori seems to be independent of culture media and independent of the presence of the cytotoxin-associated CagA antigen. Immunoblot analysis identified two plasminogen binding proteins of 57 and 42 kDa. Scatchard plot analysis revealed one binding mechanism with a Kd value of 7 × 107 M. Conversion of H. pylori cell-bound plasminogen to plasmin in the presence of a tissue-type plasminogen activator was demonstrated by digestion of the chromogenic substrate S-2251. No activation was noted when plasminogen or tissue-type plasminogen activator was incubated with H. pylori cells alone. Formation of H. pylori cell surface-bound plasmin may be important to provide a powerful proteolytic mechanism for gastric tissue penetration in type B gastritis and peptic ulcer disease, since plasmin degrades not only fibrin but also extracellular matrix proteins such as various collagens and fibronectin. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Infection and Immunity
volume
66
issue
10
pages
4976 - 4980
publisher
American Society for Microbiology
external identifiers
  • wos:000076095100054
  • scopus:0031680277
ISSN
1098-5522
language
English
LU publication?
yes
id
647bc080-7535-4010-966a-3d1fad12c300 (old id 132406)
alternative location
http://iai.asm.org/cgi/content/abstract/66/10/4976
date added to LUP
2007-07-10 12:41:14
date last changed
2017-03-26 03:40:44
@article{647bc080-7535-4010-966a-3d1fad12c300,
  abstract     = {The binding of iodine-labelled plasminogen to Helicobacter pylori CCUG 17874 was characterized. Inhibition of the binding was observed after preincubation of H. pylori cells with nonradiolabelled plasminogen, lysine, or the lysine analogue -aminocaproic acid. Fragments of plasminogen, kringles 1 to 3, kringle 4, and mini-plasminogen, were also studied as potential inhibitors. Mini-plasminogen caused total inhibition of the plasminogen binding, while the other fragments caused only partial inhibition. These findings suggest that H. pylori binds specifically the fifth kringle structure of the plasminogen molecule. Plasminogen binding to H. pylori seems to be independent of culture media and independent of the presence of the cytotoxin-associated CagA antigen. Immunoblot analysis identified two plasminogen binding proteins of 57 and 42 kDa. Scatchard plot analysis revealed one binding mechanism with a Kd value of 7 × 107 M. Conversion of H. pylori cell-bound plasminogen to plasmin in the presence of a tissue-type plasminogen activator was demonstrated by digestion of the chromogenic substrate S-2251. No activation was noted when plasminogen or tissue-type plasminogen activator was incubated with H. pylori cells alone. Formation of H. pylori cell surface-bound plasmin may be important to provide a powerful proteolytic mechanism for gastric tissue penetration in type B gastritis and peptic ulcer disease, since plasmin degrades not only fibrin but also extracellular matrix proteins such as various collagens and fibronectin.},
  author       = {Pantzar, Martina and Ljungh, Åsa and Wadström, Torkel},
  issn         = {1098-5522},
  language     = {eng},
  number       = {10},
  pages        = {4976--4980},
  publisher    = {American Society for Microbiology},
  series       = {Infection and Immunity},
  title        = {Plasminogen binding and activation at the surface of Helicobacter pylori CCUG 17874},
  volume       = {66},
  year         = {1998},
}