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  • Title: Different effects of sulfur amino acids on prolidase and prolinase activity in normal and prolidase-deficient human erythrocytes.
    Author: Uramatsu M, Liu G, Uramatsu S, Zhang M, Wang W, Nakayama K, Manabe M, Kodama H.
    Journal: Clin Chim Acta; 2007 Jan; 375(1-2):129-35. PubMed ID: 16899234.
    Abstract:
    BACKGROUND: Prolidase and prolinase activity is known to be enhanced significantly in some diseases. Recently, the effect of amino acids on prolidase and prolinase activity in normal and prolidase-deficient human erythrocytes was investigated. It was reported that both enzymes were enhanced by glycine and alanine in the presence of MnCl(2). METHODS: Erythrocytes were isolated from heparinized blood from normal human and a patient with prolidase deficiency. Effects of various sulfur amino acids on prolidase and prolinase activities against iminodipeptides in the presence of 1 or 0.1 mmol/l MnCl(2) were investigated. RESULTS: Prolinase activity against prolylglycine in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, NAc-L-methionine and D,L-methionine in a concentration-dependent manner, but D-methionine enhanced the activity in low concentrations (0-20 mmol/l). D,L-Homocysteine inhibited the activity more strongly than other sulfur amino acids tested in a concentration-dependent manner. On the other hand, prolidase activity against glycylproline was enhanced by L-methionine, D-methionine, D,L-methionine, D,L-homocysteine thiolactone and D,L-ethionine. The rates of enhancement by these sulfur amino acids were in the following order: D,L-ethionine>D,L-methionine, D-methionine, D,L-homocysteine thiolactone>L-methionine (10 mmol/l). CONCLUSION: The prolinase activity in normal and prolidase-deficient erythrocyte lysates was inhibited by L-methionine, D,L-ethionine and D,L-homocysteine. On the other hand, prolidase activity in their erythrocyte lysates was enhanced by D,L-ethionine, D-methionine and L-methionine. These results indicate the effects of these sulfur amino acids on prolidase and prolinase activities were different.
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