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In vitro glycoxidation alters the interactions between collagens and human polymorphonuclear leucocytes
J C Monboisse1, L Rittie, H Lamfarraj
1Laboratoire de Biochimie Médicale et Biologie Moléculaire, CNRS UPRESA 6021, IFR-53 Biomolécules, Faculté de Médecine, University of Reims Champagne-Ardenne, 51095 Reims cedex, France. jc.monboisse@univ-reims.fr
The Biochemical Journal
|September 6, 2000
Summary
Glycoxidation of collagen in diabetes increases polymorphonuclear leucocyte (PMN) adhesion and alters migration. This may contribute to the oxidative stress seen in diabetic complications.
Area of Science:
- Biochemistry
- Immunology
- Diabetology
Background:
- Glycation and glycoxidation are implicated in diabetic complications.
- Polymorphonuclear leucocytes (PMNs) contribute to diabetic oxidative stress.
- Previous studies showed differential effects of collagen types I and IV on PMN adhesion and stimulation.
Purpose of the Study:
- To investigate how in vitro glycoxidation of type I and IV collagens affects PMN adhesion, activation, and migration.
- To understand the role of modified extracellular matrix in diabetic complications.
Main Methods:
- In vitro glycoxidation of type I and IV collagens.
- Assessing PMN adhesion to control and glycoxidized collagens.
- Evaluating PMN migration and activation (respiratory burst, priming).
Main Results:
- Glycoxidized collagens I and IV significantly increased PMN adhesion (+37% and +99%, respectively).
- Glycoxidized type I collagen enhanced PMN chemotaxis but not respiratory burst.
- Glycoxidized type IV collagen lost its inhibitory effect on PMN stimulation and migration.
Conclusions:
- Glycoxidation of collagens I and IV alters their interaction with PMNs.
- Modified collagens impact PMN migration and reactive oxygen species production.
- This imbalance in PMN function may contribute to diabetic oxidative stress.