The association of serum prolidase activity with the presence and severity of coronary artery disease

ObjectivesProlidase is a cytosolic exopeptidase that cleaves iminodipeptides with carboxy-terminal proline or hydroxyproline and plays major role in collagen turnover. Collagen is the essential content in atherosclerotic plaque playing a key role in the stability/instability of and progression of coronary artery disease (CAD). Consequently, in this study we sought to determine serum prolidase activity and markers of oxidative stress such as lipid hydroperoxide and total free sulfhydryl in CAD. Design and methodsWe have evaluated 199 patients with CAD and 122 control cases with clinical, electrocardiographic, and laboratory investigation. We have measured serum prolidase activity and serum total free sulfhydryl levels spectrophotometrically. Serum lipid hydroperoxide levels were determined with ferrous ion oxidation-xylenol orange method. We assessed the association of serum prolidase activity with the presence and severity of CAD and clinical characteristics, and laboratory parameters. ResultsSerum prolidase activity (52.5±5.6 vs. 46.7±5.1 U/l, respectively, P<0.001) and serum lipid hydroperoxide levels were significantly increased in patients with CAD compared with control cases whereas, serum total free sulfhydryl levels were significantly decreased in patients with CAD compared with control cases. Serum prolidase activity and total free sulfhydryl levels were independent predictors of the presence of CAD [(χ2=75.532, ß=0.212, P=0.003) and (χ2=25.969, ß=−30.486, P=0.019), respectively] and Gensini score [(&bgr;=0.276, P<0.001) and (&bgr;=−0.274, P<0.001), respectively]. Independent predictors of serum prolidase activity were serum high-density lipoprotein cholesterol (&bgr;=−0.138, P=0.023) and urea levels (&bgr;=0.146, P=0.036), and Gensini score (&bgr;=0.317, P<0.001). ConclusionFindings of this study have shown that serum prolidase activity is significantly associated with the presence and severity of CAD, and elevated serum prolidase activity might be an independent predictor of coronary atherosclerosis.

[1]  N. Aksoy,et al.  Serum prolidase activity in patients with hypertension and its relation with left ventricular hypertrophy. , 2007, Clinical biochemistry.

[2]  M. Manabe,et al.  Prolidase Isoenzymes in the Rat: Their Organ Distribution, Developmental Change and Specific Inhibitors , 2007, Pediatric Research.

[3]  H. Çelik,et al.  Serum prolidase activity and oxidative status in Helicobacter pylori infection. , 2007, Clinical biochemistry.

[4]  H. Çelik,et al.  Increased oxidative stress and its relation with collagen metabolism in knee osteoarthritis , 2007, Rheumatology International.

[5]  O. Erel,et al.  Paraoxonase and arylesterase activities in coronary artery disease , 2006, European journal of clinical investigation.

[6]  M. Wojtukiewicz,et al.  Enhanced prolidase activity and decreased collagen content in breast cancer tissue , 2006, International journal of experimental pathology.

[7]  A. V. Rij,et al.  Elevated Plasma Active Matrix Metalloproteinase-9 Level Is Associated With Coronary Artery In-Stent Restenosis , 2006, Arteriosclerosis, thrombosis, and vascular biology.

[8]  D. Messadi,et al.  Elevated prolidase activity in keloids: correlation with type I collagen turnover , 2006, The British journal of dermatology.

[9]  V. Chopra,et al.  Tissue inhibitor of metalloproteinase-1 (TIMP-1) is an independent predictor of all-cause mortality, cardiac mortality, and myocardial infarction. , 2006, American heart journal.

[10]  S. Unver,et al.  The Role of Prolidase Activity in the Diagnosis of Uremic Bone Disease , 2006, Renal failure.

[11]  R. Schnabel,et al.  Prognostic value of tissue inhibitor of metalloproteinase-1 for cardiovascular death among patients with cardiovascular disease: results from the AtheroGene study. , 2006, European heart journal.

[12]  H. Leu,et al.  Plasma matrix metalloproteinase‐3 level is an independent prognostic factor in stable coronary artery disease , 2005, European journal of clinical investigation.

[13]  Reiko Ohmori,et al.  Plasma matrix metalloproteinase-8 concentrations are associated with the presence and severity of coronary artery disease. , 2005, Circulation journal : official journal of the Japanese Circulation Society.

[14]  G. Lip,et al.  Plasma matrix metalloproteinase-9, tissue inhibitor of metalloproteinase-2, and CD40 ligand levels in patients with stable coronary artery disease. , 2005, The American journal of cardiology.

[15]  D. Brieger,et al.  Elevated circulating levels of matrix metalloproteinase‐9 and ‐2 in patients with symptomatic coronary artery disease , 2005, Internal medicine journal.

[16]  A. Surazynski,et al.  Differential effects of echistatin and thrombin on collagen production and prolidase activity in human dermal fibroblasts and their possible implication in beta1-integrin-mediated signaling. , 2005, Pharmacological research.

[17]  Reiko Ohmori,et al.  Levels of matrix metalloproteinase-1 in patients with and without coronary artery disease and relation to complex and noncomplex coronary plaques. , 2005, The American journal of cardiology.

[18]  J. Steghens,et al.  Plasma lipid hydroperoxides measurement by an automated xylenol orange method. , 2004, Analytical biochemistry.

[19]  A. Surazynski,et al.  Phosphorylation of prolidase increases the enzyme activity , 2001, Molecular and Cellular Biochemistry.

[20]  H. Lijnen.  Metalloproteinases in Development and Progression of Vascular Disease , 2003, Pathophysiology of Haemostasis and Thrombosis.

[21]  P. Giral,et al.  Serum matrix metalloproteinase-3 and tissue inhibitor of metalloproteinases-1 as potential markers of carotid atherosclerosis in infraclinical hyperlipidemia. , 2003, Atherosclerosis.

[22]  A. Erbaǧci,et al.  Serum prolidase activity as a marker of osteoporosis in type 2 diabetes mellitus. , 2002, Clinical biochemistry.

[23]  H. Ishizaka,et al.  Plasma levels of matrix metalloproteinase-9 and tissue inhibitor of metalloproteinase-1 are increased in the coronary circulation in patients with acute coronary syndrome. , 2001, American heart journal.

[24]  F. Spinale,et al.  Increased matrix metalloproteinase activity and selective upregulation in LV myocardium from patients with end-stage dilated cardiomyopathy. , 1998, Circulation.

[25]  P. Shah,et al.  Role of inflammation and metalloproteinases in plaque disruption and thrombosis , 1998, Vascular medicine.

[26]  A. Girotti.  Lipid hydroperoxide generation, turnover, and effector action in biological systems. , 1998, Journal of lipid research.

[27]  A. Henney,et al.  Matrix metalloproteinases: implication in vascular matrix remodelling during atherogenesis. , 1998, Clinical science.

[28]  J. Phang,et al.  Prolidase activity in fibroblasts is regulated by interaction of extracellular matrix with cell surface integrin receptors , 1997, Journal of cellular biochemistry.

[29]  M. Lewis,et al.  Prolidase deficiency and systemic lupus erythematosus , 1997, Archives of disease in childhood.

[30]  T. Oono,et al.  Localization of prolidase gene expression in scar tissue using in situ hybridization. , 1996, Journal of dermatological science.

[31]  P. Libby,et al.  Increased expression of matrix metalloproteinases and matrix degrading activity in vulnerable regions of human atherosclerotic plaques. , 1994, The Journal of clinical investigation.

[32]  G. Cetta,et al.  Prolidase deficiency: biochemical study of erythrocyte and skin fibroblast prolidase activity in Italian patients. , 1994, Haematologica.

[33]  A. Newby,et al.  Extracellular matrix degrading metalloproteinases in the pathogenesis of arteriosclerosis. , 1994, Basic research in cardiology.

[34]  C. Cross,et al.  Antioxidant protection against hypochlorous acid in human plasma. , 1993, The Journal of laboratory and clinical medicine.

[35]  I. Myara,et al.  Plasma prolidase activity: a possible index of collagen catabolism in chronic liver disease. , 1984, Clinical chemistry.

[36]  B. Kishore,et al.  Prolidase and prolinase activities in the erythrocytes of patients with chronic uremia. , 1983, Nephron.

[37]  G. Gensini,et al.  A more meaningful scoring system for determining the severity of coronary heart disease. , 1983, The American journal of cardiology.

[38]  I. Myara,et al.  Optimal conditions for prolidase assay by proline colorimetric determination: application to iminodipeptiduria. , 1982, Clinica chimica acta; international journal of clinical chemistry.

[39]  G. Ellman,et al.  Tissue sulfhydryl groups. , 1959, Archives of biochemistry and biophysics.

[40]  F. Chinard.  Photometric estimation of proline and ornithine. , 1952, The Journal of biological chemistry.