Elucidation of correlation between structure and function of glyceraldehyde modified products

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P4 was identified as a novel dihydropyridinium compound formed by two molecules of glyceraldehyde (GLA), lysine, and arginine. The amount of P4 in serum protein, collagen, and lens proteins significantly increased compared with those in control subjects. The sequence analysis of GLA modified lysozyme revealed that K33, K97, and K116 were modified with GLA, and glyceraldehydes derived pyridinium-type AGE (GLAP) was generated in their lysine residues. Moreover, MG-H1 was also identified in arginine residues. Similar tendency was observed in GLA modified ribonuclease A and cytochrome c. The results of immunized mice with antigen caproyl-GLAP showed that GLAP polyclonal antibody which recognized the pyridinium skeleton of GLAP structure was obtained. The addition of GLA-BSA inhibited the cell proliferation of PC12, HL-60, and differentiated PC12 cells. The inhibition was dose dependent and was restored by the addition of anti-GLAP antibody. The findings were supported that the chemial structure of the epitope showing the physiological effects of GLA modified protein is GLAP.