FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2083259778> ?p ?o ?g. }

• W2083259778 endingPage "341" @default.
• W2083259778 startingPage "334" @default.
• W2083259778 abstract "The oxidative modification of low-density lipoprotein (LDL) is suggested to play an important role in the pathogenesis of atherosclerosis. The present study examined the role of the formation of LDL-copper (Cu) complex in the peroxidation of LDL. The amount of copper bound to LDL increased during incubation performed with increasing concentrations of CuSO4. More than 80% of the copper bound to the LDL particle was observed in the protein phase of LDL, suggesting that most of the copper ions formed complexes with the ligand-binding sites of apoprotein. The addition of histidine (1 mM), known to form a high affinity complex with copper, and EDTA (1 mM), a metal chelator, during the incubation of LDL with CuSO4 prevented the formation of both thiobarbituric acid-reactive substances (TBARS) and LDL-Cu complexes. EDTA inhibited the copper-catalyzed ascorbate oxidation whereas histidine had no effect, suggesting that the copper within the complex with histidine is available to catalyze the reaction, in contrast to EDTA. These observations indicate that the preventive effect of histidine on the copper-catalyzed peroxidation of LDL is not simply mediated by chelating free copper ions in aqueous phase. Evidence that copper bound to LDL particle still has a redox potential was provided by the observed increase in TBARS content during incubation of LDL-Cu complexes in the absence of free copper ions. The addition of either histidine or EDTA to LDL-Cu complexes inhibited the formation of TBARS by removing copper ions from the LDL forming the corresponding complexes. However, there still remained small amounts of copper in the LDL particles following the treatment of LDL-Cu complexes with histidine or EDTA. The copper ions remaining in the LDL particle lacked the ability to catalyze LDL peroxidation, suggesting that there may be two types of copper binding sites in LDL: tight-binding sites, from which the copper ions are not removed by chelation, and weak-binding sites, from which copper ions are easily removed by chelators. The formation of TBARS in the LDL preparation during incubation with CuSO4 was comparable to the incubation with FeSO4. In contrast, the formation of TBARS in the LDL-lipid micelles by CuSO4 was nearly eliminated even in the presence of ascorbate to promote metal-catalyzed lipid peroxidation, although a marked increase in TBARS content was observed in the LDL-lipid micelles with FeSO4, and with FeCl3 in the presence of ascorbate.(ABSTRACT TRUNCATED AT 400 WORDS)" @default.
• W2083259778 created "2016-06-24" @default.
• W2083259778 creator A5010916565 @default.
• W2083259778 creator A5019147041 @default.
• W2083259778 creator A5023932932 @default.
• W2083259778 creator A5040827130 @default.
• W2083259778 creator A5049254565 @default.
• W2083259778 creator A5067102417 @default.
• W2083259778 creator A5073659794 @default.
• W2083259778 date "1992-02-01" @default.
• W2083259778 modified "2023-09-28" @default.
• W2083259778 title "Role of lipoprotein-copper complex in copper catalyzed-peroxidation of low-density lipoprotein" @default.
• W2083259778 cites W1484860178 @default.
• W2083259778 cites W1505154018 @default.
• W2083259778 cites W1512559452 @default.
• W2083259778 cites W1528987274 @default.
• W2083259778 cites W1542526845 @default.
• W2083259778 cites W1554009894 @default.
• W2083259778 cites W1562522900 @default.
• W2083259778 cites W1775749144 @default.
• W2083259778 cites W1816728254 @default.
• W2083259778 cites W1871621847 @default.
• W2083259778 cites W1970357567 @default.
• W2083259778 cites W1971123289 @default.
• W2083259778 cites W1978481197 @default.
• W2083259778 cites W1981815722 @default.
• W2083259778 cites W1983304194 @default.
• W2083259778 cites W1984393490 @default.
• W2083259778 cites W1990599831 @default.
• W2083259778 cites W1990962890 @default.
• W2083259778 cites W2003599469 @default.
• W2083259778 cites W2005182309 @default.
• W2083259778 cites W2015643800 @default.
• W2083259778 cites W2017315967 @default.
• W2083259778 cites W2034393548 @default.
• W2083259778 cites W2036660517 @default.
• W2083259778 cites W2039415379 @default.
• W2083259778 cites W2046382167 @default.
• W2083259778 cites W2064580030 @default.
• W2083259778 cites W2070951814 @default.
• W2083259778 cites W2082327493 @default.
• W2083259778 cites W2109068111 @default.
• W2083259778 cites W2109330288 @default.
• W2083259778 cites W2110569594 @default.
• W2083259778 cites W2113553969 @default.
• W2083259778 cites W2121972309 @default.
• W2083259778 cites W2125570349 @default.
• W2083259778 cites W2140328938 @default.
• W2083259778 cites W2158883979 @default.
• W2083259778 cites W2161188230 @default.
• W2083259778 cites W2168526937 @default.
• W2083259778 cites W2185726806 @default.
• W2083259778 cites W2291592525 @default.
• W2083259778 cites W2326202471 @default.
• W2083259778 doi "https://doi.org/10.1016/0005-2760(92)90015-n" @default.
• W2083259778 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1536873" @default.
• W2083259778 hasPublicationYear "1992" @default.
• W2083259778 type Work @default.
• W2083259778 sameAs 2083259778 @default.
• W2083259778 citedByCount "140" @default.
• W2083259778 countsByYear W20832597782012 @default.
• W2083259778 countsByYear W20832597782013 @default.
• W2083259778 countsByYear W20832597782014 @default.
• W2083259778 countsByYear W20832597782015 @default.
• W2083259778 countsByYear W20832597782016 @default.
• W2083259778 countsByYear W20832597782018 @default.
• W2083259778 countsByYear W20832597782019 @default.
• W2083259778 countsByYear W20832597782020 @default.
• W2083259778 crossrefType "journal-article" @default.
• W2083259778 hasAuthorship W2083259778A5010916565 @default.
• W2083259778 hasAuthorship W2083259778A5019147041 @default.
• W2083259778 hasAuthorship W2083259778A5023932932 @default.
• W2083259778 hasAuthorship W2083259778A5040827130 @default.
• W2083259778 hasAuthorship W2083259778A5049254565 @default.
• W2083259778 hasAuthorship W2083259778A5067102417 @default.
• W2083259778 hasAuthorship W2083259778A5073659794 @default.
• W2083259778 hasConcept C116569031 @default.
• W2083259778 hasConcept C170493617 @default.
• W2083259778 hasConcept C178790620 @default.
• W2083259778 hasConcept C179104552 @default.
• W2083259778 hasConcept C185592680 @default.
• W2083259778 hasConcept C197404232 @default.
• W2083259778 hasConcept C2777352226 @default.
• W2083259778 hasConcept C2777504301 @default.
• W2083259778 hasConcept C2778004101 @default.
• W2083259778 hasConcept C2778163477 @default.
• W2083259778 hasConcept C2778460671 @default.
• W2083259778 hasConcept C2779620165 @default.
• W2083259778 hasConcept C2780072125 @default.
• W2083259778 hasConcept C2780829032 @default.
• W2083259778 hasConcept C515207424 @default.
• W2083259778 hasConcept C544778455 @default.
• W2083259778 hasConcept C55493867 @default.
• W2083259778 hasConceptScore W2083259778C116569031 @default.
• W2083259778 hasConceptScore W2083259778C170493617 @default.
• W2083259778 hasConceptScore W2083259778C178790620 @default.
• W2083259778 hasConceptScore W2083259778C179104552 @default.
• W2083259778 hasConceptScore W2083259778C185592680 @default.

• next