Glycation of extracellular matrix proteins impairs migration of immune cells

The immune response during aging and diabetes is disturbed and may be due to the altered migration of immune cells in an aged tissue. Our study should prove the hypothesis that age and diabetes‐related advanced glycation end products (AGEs) have an impact on the migration and adhesion of human T‐cells. To achieve our purpose, we used in vitro AGE‐modified proteins (soluble albumin and fibronectin [FN]), as well as human collagen obtained from bypass graft. A Boyden chamber was used to study cell migration. Migrated Jurkat T‐cells were analyzed by flow cytometry and cell adhesion by crystal violet staining. Actin polymerization was determined by phalloidin‐Alexa‐fluor 488‐labeled antibody and fluorescence microscopy. We found that significantly fewer cells (50%, p = 0.003) migrated through methylglyoxal modified FN. The attachment to FN in the presence of AGE‐bovine serum albumin (BSA) was also reduced (p