全部 标题 作者
关键词 摘要

OALib Journal期刊
ISSN: 2333-9721
费用:99美元

查看量下载量

相关文章

更多...

Lipid Peroxidation and Paraoxonase-1 Activity in Celiac Disease

DOI: 10.1155/2012/587479

Full-Text   Cite this paper   Add to My Lib

Abstract:

Paraoxonase-1 (PON1) plays an antioxidant and anti-inflammatory role. Aim of the study was to investigate the alteration of paraoxonase-1 activity in celiac disease (CD), an intestinal disorder characterized by toxic injury exerted by gluten peptides. Activities of PON1, levels of biochemical markers of lipid peroxidation and total antioxidant capacity were evaluated in serum obtained from 27 celiac patients (11 at diagnosis, 16 treated with gluten free diet) and 25 healthy subjects. Moreover, the serum susceptibility of Cu2+-induced lipid peroxidation was investigated in controls and patients. The results showed a lower PON1 activity in serum of both groups of celiac patients with respect to control subjects. PON1 activity in CD was related with markers of disease severity and was negatively correlated with the levels of lipid hydroperoxide and with the susceptibility of serum to lipid peroxidation induced in vitro by metal ions. The alteration of PON1 activity and markers of lipid peroxidation realized at lower extent in patients who were on a gluten-free diet. 1. Introduction Environmental, genetic, and immunologic factors are involved in the pathogenesis of celiac disease (CD) [1], a chronic inflammatory disease characterised by flattened villi on the small bowel mucosa. CD is induced by the ingestion of cereals containing proline-rich and glutamine-rich proteins (such as wheat, rye, and barley) in genetically susceptible individuals [2, 3]. From a clinical point of view, CD is characterised by a clinical heterogeneity that ranges from asymptomatic to severely symptomatic and by increased morbidity and mortality [4]. At present, the only proven treatment for CD is strict and life-long adherence to a gluten-free diet (GFD) [1–4]. An increase of markers of oxidative damage of lipids (thiobarbituric acid-reactive substances and lipid hydroperoxides) and proteins (carbonyl groups) and a decrease of antioxidant enzymes have been demonstrated in plasma, in circulating cells and in intestinal cells of patients with CD with respect to controls [5–8]. Higher levels of nitric oxide (NO) and biochemical markers of oxidative damage of DNA has been demonstrated in leukocytes and in urine samples of celiac children [9, 10], suggesting that oxidative stress could be involved in the pathogenesis of CD. Paraoxonase-1 (PON1) is an enzyme associated with the high-density lipoproteins (HDL) that plays both an antioxidant and an anti-inflammatory role [11–13]. A decrease in PON1 has been reported in several human diseases associated with inflammation and alteration of

References

[1]  L. Shan, O. Molberg, I. Parrot et al., “Structural basis for gluten intolerance in celiac Sprue,” Science, vol. 297, no. 5590, pp. 2275–2279, 2002.
[2]  B. Diosdado, E. van Oort, and C. Wijmenga, “‘Coelionomics’: towards understanding the molecular pathology of coeliac disease,” Clinical Chemistry and Laboratory Medicine, vol. 43, no. 7, pp. 685–695, 2005.
[3]  F. Koning, D. Schuppan, N. Cerf-Bensussan, and L. M. Sollid, “Pathomechanisms in celiac disease,” Best Practice and Research, vol. 19, no. 3, pp. 373–387, 2005.
[4]  P. H. R. Green, K. Rostami, and M. N. Marsh, “Diagnosis of coeliac disease,” Best Practice and Research, vol. 19, no. 3, pp. 389–400, 2005.
[5]  P. Odetti, S. Valentini, I. Aragno et al., “Oxidative stress in subjects affected by celiac disease,” Free Radical Research, vol. 29, no. 1, pp. 17–24, 1998.
[6]  V. Stojiljkovi?, A. Todorovi?, N. Radlovi? et al., “Antioxidant enzymes, glutathione and lipid peroxidation in peripheral blood of children affected by coeliac disease,” Annals of Clinical Biochemistry, vol. 44, no. 6, pp. 537–543, 2007.
[7]  K. K. Hozyasz, M. Chelchowska, and T. Laskowska-Klita, “Vitamin E levels in patients with celiac disease,” Medycyna Wieku Rozwojowego, vol. 7, no. 4, pp. 593–604, 2003.
[8]  V. Stojiljkovi?, A. Todorovi?, S. Peji? et al., “Antioxidant status and lipid peroxidation in small intestinal mucosa of children with celiac disease,” Clinical Biochemistry, vol. 42, no. 13-14, pp. 1431–1437, 2009.
[9]  A. Szaflarska-Poplawska, A. Siomek, M. Czerwionka-Szaflarska et al., “Oxidatively damaged DNA/oxidative stress in children with celiac disease,” Cancer Epidemiology Biomarkers and Prevention, vol. 19, no. 8, pp. 1960–1965, 2010.
[10]  L. H?gberg, C. Webb, K. F?lth-Magnusson et al., “Children with screening-detected coeliac disease show increased levels of nitric oxide products in urine,” Acta Paediatrica, vol. 100, no. 7, pp. 1023–1027, 2011.
[11]  M. I. Mackness, S. Arrol, C. Abbott, and P. N. Durrington, “Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase,” Atherosclerosis, vol. 104, no. 1-2, pp. 129–135, 1993.
[12]  B. MacKness and M. MacKness, “Anti-inflammatory properties of paraoxonase-1 in atherosclerosis,” Advances in Experimental Medicine and Biology, vol. 660, pp. 143–151, 2010.
[13]  B. Goswami, D. Tayal, N. Gupta, and V. Mallika, “Paraoxonase: a multifaceted biomolecule,” Clinica Chimica Acta, vol. 410, no. 1-2, pp. 1–12, 2009.
[14]  B. Mackness, P. Durrington, P. McElduff et al., “Low paraoxonase activity predicts coronary events in the Caerphilly Prospective Study,” Circulation, vol. 107, no. 22, pp. 2775–2779, 2003.
[15]  G. Ferretti, T. Bacchetti, S. Masciangelo et al., “Lipid peroxidation in stroke patients,” Clinical Chemistry and Laboratory Medicine, vol. 46, no. 1, pp. 113–117, 2008.
[16]  G. Ferretti, T. Bacchetti, S. Masciangelo, and V. Bicchiega, “HDL-paraoxonase and membrane lipid peroxidation: a comparison between healthy and obese subjects,” Obesity, vol. 18, no. 6, pp. 1079–1084, 2010.
[17]  G. Ferretti, T. Bacchetti, D. Busni, R. A. Rabini, and G. Curatola, “Protective effect of paraoxonase activity in high-density lipoproteins against erythrocyte membranes peroxidation: a comparison between healthy subjects and type 1 diabetic patients,” Journal of Clinical Endocrinology and Metabolism, vol. 89, no. 6, pp. 2957–2962, 2004.
[18]  L. Rothem, C. Hartman, A. Dahan, J. Lachter, R. Eliakim, and R. Shamir, “Paraoxonases are associated with intestinal inflammatory diseases and intracellularly localized to the endoplasmic reticulum,” Free Radical Biology and Medicine, vol. 43, no. 5, pp. 730–739, 2007.
[19]  D. Boehm, M. Krzystek-Korpacka, K. Neubauer et al., “Paraoxonase-1 status in Crohn's disease and ulcerative colitis,” Inflammatory Bowel Diseases, vol. 15, no. 1, pp. 93–99, 2009.
[20]  G. Baskol, M. Baskol, A. Yurci, O. Ozbakir, and M. Yucesoy, “Serum paraoxonase 1 activity and malondialdehyde levels in patients with ulcerative colitis,” Cell Biochemistry and Function, vol. 24, no. 3, pp. 283–286, 2006.
[21]  M. N. Marsh, “Gluten, major histocompatibility complex, and the small intestine: a molecular and immunobiologic approach to the spectrum of gluten sensitivity (“celiac sprue”),” Gastroenterology, vol. 102, no. 1, pp. 330–354, 1992.
[22]  A. Bürgin-Wolff, I. Dahlbom, F. Hadziselimovic, and C. J. Petersson, “Antibodies against human tissue transglutaminase and endomysium in diagnosing and monitoring coeliac disease,” Scandinavian Journal of Gastroenterology, vol. 37, no. 6, pp. 685–691, 2002.
[23]  W. Rock, M. Rosenblat, R. Miller-Lotan, A. P. Levy, M. Elias, and M. Aviram, “Consumption of Wonderful variety pomegranate juice and extract by diabetic patients increases paraoxonase 1 association with high-density lipoprotein and stimulates its catalytic activities,” Journal of Agricultural and Food Chemistry, vol. 56, no. 18, pp. 8704–8713, 2008.
[24]  A. Kontush and U. Beisiegel, “Measurement of oxidizability of blood plasma,” Methods in Enzymology, vol. 299, pp. 35–49, 1998.
[25]  B. Ou, M. Hampsch-Woodill, and R. L. Prior, “Development and validation of an improved oxygen radical absorbance capacity assay using fluorescein as the fluorescent probe,” Journal of Agricultural and Food Chemistry, vol. 49, no. 10, pp. 4619–4626, 2001.
[26]  M. Rosenblat and M. Aviram, “Paraoxonases role in the prevention of cardiovascular diseases,” Biofactors, vol. 35, no. 1, pp. 98–104, 2009.
[27]  L. G. Costa, A. Vitalone, T. B. Cole, and C. E. Furlong, “Modulation of paraoxonase (PON1) activity,” Biochemical Pharmacology, vol. 69, no. 4, pp. 541–550, 2005.
[28]  O. Khersonsky and D. S. Tawfik, “Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase,” Biochemistry, vol. 44, no. 16, pp. 6371–6382, 2005.
[29]  R. Rivabene, E. Mancini, and M. de Vincenzi, “In vitro cytotoxic effect of wheat gliadin-derived peptides on the Caco-2 intestinal cell line is associated with intracellular oxidative imbalance: implications for coeliac disease,” Biochimica et Biophysica Acta, vol. 1453, no. 1, pp. 152–160, 1999.
[30]  L. Elli, E. Dolfini, and M. T. Bardella, “Gliadin cytotoxicity and in vitro cell cultures,” Toxicology Letters, vol. 146, no. 1, pp. 1–8, 2003.
[31]  P. Bergamo, M. Gogliettino, G. Palmieri et al., “Conjugated linoleic acid protects against gliadin-induced depletion of intestinal defenses,” Molecular Nutrition and Food Research, vol. 55, supplement 2, pp. S248–S256, 2011.
[32]  R. W. James and S. P. Deakin, “The importance of high-density lipoproteins for paraoxonase-1 secretion, stability, and activity,” Free Radical Biology and Medicine, vol. 37, no. 12, pp. 1986–1994, 2004.
[33]  J. K. Kruit, A. K. Groen, T. J. van Berkel, and F. Kuipers, “Emerging roles of the intestine in control of cholesterol metabolism,” World Journal of Gastroenterology, vol. 12, no. 40, pp. 6429–6439, 2006.
[34]  L. P. Precourt, E. Seidman, E. Delvin et al., “Comparative expression analysis reveals differences in the regulation of intestinal paraoxonase family members,” International Journal of Biochemistry and Cell Biology, vol. 41, no. 7, pp. 1628–1637, 2009.
[35]  R. Shamir, C. Hartman, R. Karry et al., “Paraoxonases (PONs) 1, 2, and 3 are expressed in human and mouse gastrointestinal tract and in Caco-2 cell line: selective secretion of PON1 and PON2,” Free Radical Biology and Medicine, vol. 39, no. 3, pp. 336–344, 2005.
[36]  B. Mackness, R. Beltran-Debon, G. Aragones, J. Joven, J. Camps, and M. Mackness, “Human tissue distribution of paraoxonases 1 and 2 mRNA,” IUBMB Life, vol. 62, no. 6, pp. 480–482, 2010.
[37]  M. Aviram, M. Rosenblat, S. Billecke et al., “Human serum paraoxonase (PON 1) is inactivated by oxidized low density lipoprotein and preserved by antioxidants,” Free Radical Biology and Medicine, vol. 26, no. 7-8, pp. 892–904, 1999.
[38]  S. D. Nguyen, N. D. Hung, P. Cheon-Ho, K. M. Ree, and S. Dai-Eun, “Oxidative inactivation of lactonase activity of purified human paraoxonase 1 (PON1),” Biochimica et Biophysica Acta, vol. 1790, no. 3, pp. 155–160, 2009.
[39]  E. Niki, “Lipid peroxidation: physiological levels and dual biological effects,” Free Radical Biology and Medicine, vol. 47, no. 5, pp. 469–484, 2009.

Full-Text

Contact Us

service@oalib.com

QQ:3279437679

WhatsApp +8615387084133