EurekaMag.com logo
+ Site Statistics
References:
47,893,527
Abstracts:
28,296,643
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on Google+Follow on Google+
Follow on LinkedInFollow on LinkedIn

+ Translate

Oxidation of low density lipoprotein by iron or copper at acidic pH


, : Oxidation of low density lipoprotein by iron or copper at acidic pH. Journal of Lipid Research 36(12): 2504-2512

Oxidized low density lipoprotein (LDL) may play a significant role in atherosclerosis. We have investigated the effect of pH on the oxidation of LDL by iron or copper. When LDL was oxidized by iron in the presence of cysteine in either Hanks' balanced salt solution (HBSS) or Ham's F-10 medium, an acidic pH greatly decreased the lag period and increased the rate of formation of hydroperoxides and thiobarbituric acid-reactive substances (TBARS), and increased its uptake by macrophages. There was a dose-dependent increase of LDL oxidation at acidic pH in the presence of increasing concentrations of cysteine. When LDL was oxidized by copper in HBSS, an acidic pH increased the lag phase before the rapid formation of conjugated dienes, hydroperoxides, and TBARS, but increased its uptake by macro. phages. Similar results were obtained using Ham's F-10 medium. Cysteine (100 micromolar) inhibited the modification of LDL by copper in HBSS at both pH 7.4 and 5.5. As atherosclerotic lesions may be acidic, these observations may help to explain why LDL oxidation occurs locally at these sites.


Accession: 002914080

PMID: 8847477

Submit PDF Full Text: Here


Submit PDF Full Text

No spam - Every submission is manually reviewed

Due to poor quality, we do not accept files from Researchgate

Submitted PDF Full Texts will always be free for everyone
(We only charge for PDFs that we need to acquire)

Select a PDF file:
Close
Close

Related references

Lamb, D., J.; Leake, D., S., 1994: Iron released from transferrin at acidic pH can catalyse the oxidation of low density lipoprotein. Low density lipoprotein (LDL) oxidation within the arterial wall may contribute to the disease of atherosclerosis. We have investigated the conditions under which transferrin (the major iron-carrying protein in plasma) may release iron ions to cat...

Lamb, D.J.; Leake, D.S., 1994: Iron released from transferrin at acidic pH can catalyse the oxidation of low density lipoprotein. Low density lipoprotein (LDL) oxidation within the arterial wall may contribute to the disease of atherosclerosis. We have investigated the conditions under which transferrin (the major iron-carrying protein in plasma) may release iron ions to cat...

Kuzuya, M.; Yamada, K.; Hayashi, T.; Funaki, C.; Naito, M.; Asai, K.; Kuzuya, F., 1991: Oxidation of low-density lipoprotein by copper and iron in phosphate buffer. We examined the effect of phosphate buffer on the iron- and copper-catalyzed peroxidation of low-density lipoprotein (LDL). The incubation of LDL with CuSO4 in 0.15 M NaCl led to the peroxidation of LDL as evidenced by the detection of thiobarbitu...

Ani, M.; Moshtaghie, A.Asghar.; Ahmadvand, H., 2007: Comparative effects of copper, iron, vanadium and titanium on low density lipoprotein oxidation in vitro. Introduction: Oxidation of low density lipoprotein (LDL) has been strongly implicated in the pathogenesis of atherosclerosis. The use of oxidants in dietary food stuff may lead to the production of oxidized LDL and may increase both the developmen...

Kleinveld, H.A.; Hak-Lemmers, H.L.; Stalenhoef, A.F.; Demacker, P.N., 1992: Improved measurement of low-density-lipoprotein susceptibility to copper-induced oxidation: application of a short procedure for isolating low-density lipoprotein. Low-density-lipoprotein (LDL) oxidation may provide the crucial link between plasma LDL and atherosclerotic lesion formation. Oxidation can be induced in vitro by incubating LDL with cells or metal ions and can be measured by continuously monitori...

Zhang, A.; Vertommen, J.; Van Gaal, L.; D.L.euw, I., 1994: A rapid and simple method for measuring the susceptibility of low-density-lipoprotein and very-low-density-lipoprotein to copper-catalyzed oxidation. Much evidence has accumulated to suggest a role for the oxidation of low-density-lipoprotein (LDL) and very low-density-lipoprotein (VLDL) in the pathogenesis of atherosclerosis. The susceptibility of lipoprotein to copper-catalyzed oxidation is o...

Lynch, S.M.; Frei, B., 1997: Physiological thiol compounds exert pro- and anti-oxidant effects respectively, on iron- and copper-dependent oxidation of human low-density lipoprotein. The effects of thiol compounds on oxidation of human low-density lipoprotein (LDL, 0.2 mg of protein/ml) by Cu-2+ or Fe-3+ (10 mu-M, each) were investigated in an in vitro system. L-Cysteine (CYS, 25 mu-M-1 mM) inhibited Cu-2+-dependent, but facil...

Huang, J.M.ng; Huang, Z.X.an; Zhu, W., 1998: Mechanism of high-density lipoprotein subfractions inhibiting copper-catalyzed oxidation of low-density lipoprotein. Objective: To investigate the role of HDL subfractions, HDL2 and HDL3, on the oxidation of LDL catalyzed by 5 muM Cu2+ ion, and to Illustrate the mechanism of the generation of conjugated diene and thiobarbituric acid reactive substances (TBARS) d...

Tribble, D.L.; Van Venrooij, F.; Gong, E.L.; Nichols, A.V., 1994: Use of a nonexchangeable probe to monitor particle-specific oxidation kinetics in mixed systems Evidence that high density lipoprotein inhibits low density lipoprotein oxidation by FeCl-3 without simultaneous oxidation. Circulation 90(4 PART 2): I136

Hill, B.C.; Becker, L.; Anand, V.; Kusmierczyk, A.; Marcovina, S.M.; Rahman, M.N.; Gabel, B.R.; Jia, Z.; Boffa, M.B.; Koschinsky, M.L., 2003: A role for apolipoprotein in protection of the low-density lipoprotein component of lipoprotein from copper-mediated oxidation. Low-density lipoprotein (LDL) oxidation is stimulated by copper. Addition of a recombinant form of apolipoprotein(a) (apo(a); the distinguishing protein component of lipoprotein(a)) containing 17 plasminogen kringle IV-like domains (17K r-apo(a))...