Glycation of extracellular matrix proteins impairs migration of immune cells.

摘要: The immune response during aging and diabetes is disturbed may be due to the altered migration of cells in an aged tissue. Our study should prove hypothesis that age diabetes-related advanced glycation end products (AGEs) have impact on adhesion human T-cells. To achieve our purpose, we used vitro AGE-modified proteins (soluble albumin fibronectin [FN]), as well collagen obtained from bypass graft. A Boyden chamber was cell migration. Migrated Jurkat T-cells were analyzed by flow cytometry crystal violet staining. Actin polymerization determined phalloidin-Alexa-fluor 488-labeled antibody fluorescence microscopy. We found significantly fewer (50%, p = 0.003) migrated through methylglyoxal modified FN. attachment FN presence AGE-bovine serum (BSA) also reduced (p < 0.05). In ex vivo experiments, isolated vein graft material negatively affected depending grade AGE modification collagen. Collagen with a low level 30%, high 60%. Interaction matrix, but not soluble AGEs like BSA-AGE per se, responsible for accompanied impaired actin polymerization. conclude AGEs-modified matrix protein inhibits