PL EN


Preferencje help
Widoczny [Schowaj] Abstrakt
Liczba wyników
2002 | 49 | 4 |

Tytuł artykułu

Species- and substrate-specific stimulation of human plasma paraoxonase 1 [PON1] activity by high chloride concentration

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Paraoxonase 1 (PON1), contained in plasma high-density lipoproteins, plays an im­portant role in the protection of plasma lipoproteins and cell membranes from oxida­tive damage. Previous studies indicate that human PON1 is stimulated by high NaCl concentrations. The aim of this study was to characterize in more detail the effect of salts on serum PON1. Paraoxon-hydrolyzing activity of human serum was stimulated by 81.6% following the addition of 1 M NaCl. The effect of NaCl was dose-dependent between 0.5 and 2 M. PON1 activity toward phenyl acetate was reduced by 1 M NaCl by 55.2%. Both the paraoxon- and phenyl acetate-hydrolysing activity was slightly lower in heparinized plasma than in serum, but NaCl had similar stimulatory and in­hibitory effects on these activities, respectively. In rat, rabbit, and mouse, NaCl re­duced PON1 activity. KCl had a similar effect on human PON1 as NaCl. Sodium nitrite also stimulated human PON1 but much less effectively than chloride salts. In contrast, sucrose, sodium acetate and sodium lactate had no significant effect. NaBr was a less effective PON1 activator than NaCl, whereas the effect of NaJ was non-significant. The activity of human PON1 toward homogentisic acid lactone and y-decanolactone was unaltered by NaCl. These data indicate that: 1) high concentrations of chlorides stimulate human PON1 activity toward paraoxon but not other substrates, 2) PON1 is inhibited by Cl- in other mammalian species, 3) the potency of human PON1 activa­tion by halogene salts increases with decreasing atomic mass of the halide anion.

Wydawca

-

Rocznik

Tom

49

Numer

4

Opis fizyczny

p.927-936,fig.

Twórcy

autor
  • Medical University, Jaczewskiego 8, 20-090 Lublin, Poland
autor
autor

Bibliografia

  • Aviram M, Billecke S, Sorenson R, Bisgaier C, Newton R, Rosenblat M, Erogul J, Hsu C, Dunlop C, La Du B. (1998a) Paraoxonase active site required for protection against LDL oxidation involves its free sulfhydryl group and is different from that required for its arylesterase/paraoxonase activities: selective action of human paraoxonase allozymes Q and R. Arterioscler Thromb Vasc Biol.; 18: 1617-24.
  • Aviram M, Rosenblat M, Bisgaier CL, Newton RS, Primo-Parmo SL, La Du BN. (1998b) Paraoxonase inhibits high- density lipoprotein oxidation and preserves its functions. J Clin Invest.; 101: 1581-90.
  • Aviram M, Hardak E, Vaya J, Mahmood S, Milo S, Hoffman A, Billicke S, Draganov D, Rosenblat M. (2000) Human serum paraoxonase (PON) Q and R selectively decrease lipid peroxides in human coronary and carotid atherosclerotic lesions: PON1 esterase and peroxidase-like activities. Circulation.; 101: 2510-7.
  • Ayub A, Mackness MI, Arrol S, Mackness B, Patel J, Durrington PM. (1999) Serum paraoxonase after myocardial infarction. Arterioscler Thromb Vasc Biol.; 19: 330-5.
  • Billecke S, Draganov D, Counsell R, Stetson P, Watson C, Hsu C, La Du BN. (2000) Human serum paraoxonase (PON1) isozymes Q and R hydrolyze lactones and cyclic carbonate esters. DrugMetab Dispos.; 28: 1335-42.
  • Draganov DI, Stetson PL, Watson CE, Billecke SS, La Du BN. (2000) Rabbit serum paraoxonase-3 (PON3) is a high density lipoprotein-associated lactonase and protects low density lipoprotein against oxidation. J Biol Chem.; 275: 33435-42.
  • Durrington PN, Mackness B, Mackness MI. (2001) Paraoxonase and atherosclerosis. Arterioscler Thromb Vasc Biol.; 21: 473-80.
  • Eckerson HW, Wyte CM, La Du BN. (1983a) The human serum paraoxonase/arylesterase polymorphism. Am J Hum Genet.; 35: 1126-8.
  • Eckerson HW, Ramson J, Wyte C, La Du BN. (1983b) The human paraoxonase polymorphism: identification of phenotypes by their response to salts. Am J Hum Genet.; 35: 214-7.
  • Geldmacher von Mallinckrodt M, Diepgen TL, Duhme C, Hommel G. (1983) A study of the polymorphism and ethnic distribution difference of human serum paraoxonase. Am JPhys Anthropol.; 62: 235-41.
  • Hasselwander O, McEneny J, McMaster D, Fogarty DG, Nicholls DP, Maxwell AP, Young IS. (1999) HDL composition and HDL antioxidant capacity in patients on regular hemodialysis. Atherosclerosis.; 143: 125-33.
  • Jakubowski H. (2000) Calcium-dependent human serum homocysteine thiolactone hydrolase. J Biol Chem.; 275: 3957-62.
  • Juretic D, Tadijanovic M, Rekic B, Simeon- Rudolf V, Reiner E, Baricic M. (2001) Serum paraoxonase activities in hemodialyzed uremic patients: cohort study. Croat Med J.; 42: 146-50.
  • La Du BN, Adkins S, Kuo CL, Lipsig D. (1993) Studies on human serum paraoxonase/arylesterase. Chem Biol Interact.; 87: 25-34.
  • Mackness ML, Durrington PN. (1995) HDL, its enzymes and its potential to influence lipid peroxidation. Atherosclerosis.; 115: 243-53.
  • Mackness ML, Arrol S, Durrington PN. (1991) Paraoxonase prevents accumulation of lipoperoxides in low-density lipoproteins. FEBSLett; 286: 152-4.
  • Mackness MI, Arrol S, Abbott C, Durrington PN. (1993) Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase. Atherosclerosis.; 104: 129-35.
  • Mackness ML, Mackness B, Durrington PN, Connelly PW, Hegele RA. (1996) Paraoxonase: biochemistry, genetics and relationship to plasma lipoproteins. Curr Opin Lipidol.; 7: 69-76.
  • Mackness ML, Arrol S, Mackness B, Durrington PN. (1997) The alloenzymes of paraoxonase determine the effectiveness of high-density lipoproteins in protecting low density lipoprotein against lipid-peroxidation. Lancet.; 349: 851-2.
  • Mackness B, Mackness ML, Arrol S, Turkie W, Durrington PN. (1998) Effect of the human paraoxonase 55 and 192 genetic polymorphisms on the protection by high density lipoprotein against low density lipoprotein oxidative modification. FEBS Lett.; 423: 57-60.
  • Ng CJ, Wadleigh DJ, Gangopadhyay A, Hama S, Grijalva V, Navab M, Fogelman AM, Reddy ST. (2001) Paraoxonase-2 is a ubiquitously expressed protein with antioxidant properties and is capable of preventing cell-mediated oxidative modification of low density lipoprotein. J Biol Chem.; 276: 44444-9.
  • Reddy ST, Wadleigh DJ, Grijalva V, Ng C, Hama S, Gangopadhyay A, Shih DM, Lusis AJ, Navab M, Fogelman AM. (2001) Human paraoxonase-3 is an HDL-associated enzyme with biological activity similar to paraoxonase-1 protein but is not regulated by oxidized lipids. Arterioscler Thromb Vasc Biol.; 21: 542-7.
  • Rodrigo L, Mackness B, Durrington PN, Hernandez A, Mackness MI. (2001) Hydrolysis of platelet-activating factor by human serum paraoxonase. Biochem J.; 354: 1-7.
  • Schiavon R, De Fanti E, Giavarina D, Biasioli S, Cavalcanto G, Guidi G. (1996) Serum paraoxonase activity is decreased in uremic patients. Clin Chim Acta.; 247: 71-80.
  • Sorenson RC, Bisgaier CL, Aviram M, Hsu C, Billecke S, La Du BN. (1999) Human serum paraoxonase/arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids. Arterioscler Thromb Vasc Biol.; 19: 2214-25.
  • Watson AD, Berliner JA, Hama SY, La Du BN, Faull KF, Fogelman AM, Navab M. (1995) Protective effect of high density lipoprotein associated paraoxonase. Inhibition of the biological activity of minimally oxidized low density lipoprotein. J Clin Invest.; 96: 2882-91.

Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

bwmeta1.element.agro-article-e05ab10c-39c1-4dcd-b437-ad92fb83e688
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.