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Titolo:
SUSCEPTIBILITY OF PHOSPHOLIPIDS OF OXIDIZING LDL TO ENZYMATIC-HYDROLYSIS MODULATES UPTAKE BY P388D(1) MACROPHAGE-LIKE CELLS
Autore:
FYRNYS B; BLENCOWE C; DEIGNER HP;
Indirizzi:
UNIV HEIDELBERG,INST PHARMAZEUT CHEM,NEUENHEIMER FELD 364 D-69120 HEIDELBERG GERMANY UNIV HEIDELBERG,INST PHARMAZEUT CHEM D-69120 HEIDELBERG GERMANY
Titolo Testata:
FEBS letters
fascicolo: 1, volume: 357, anno: 1995,
pagine: 7 - 12
SICI:
0014-5793(1995)357:1<7:SOPOOL>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLATELET-ACTIVATING-FACTOR; LOW-DENSITY-LIPOPROTEIN; HUMAN MONOCYTE-MACROPHAGES; UNSATURATED FATTY-ACIDS; FACTOR ACETYLHYDROLASE; HUMAN-PLASMA; OXIDATIVE MODIFICATION; SCAVENGER RECEPTOR; LIPID-PEROXIDATION; APOLIPOPROTEIN-B;
Keywords:
LOW DENSITY LIPOPROTEIN; PAF-ACETYLHYDROLASE; LIPID OXIDATION; MACROPHAGE UPTAKE; PHOSPHOLIPID;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
46
Recensione:
Indirizzi per estratti:
Citazione:
B. Fyrnys et al., "SUSCEPTIBILITY OF PHOSPHOLIPIDS OF OXIDIZING LDL TO ENZYMATIC-HYDROLYSIS MODULATES UPTAKE BY P388D(1) MACROPHAGE-LIKE CELLS", FEBS letters, 357(1), 1995, pp. 7-12

Abstract

Addition of the phospholipids exadecyl-2-arachidonyl-sn-glycero-3-phosphocholine (PLE) and y-2-amino-arachidonoyl-sn-glycero-3-phosphocholine (PLA) to [I-125]LDL and subsequent Cu2+-induced oxidation result insignificant differences in protein modification and uptake by P388D(1) macrophage-like cells, PLE-treated LDL is ingested at a 1.27-fold rate compared to PLE-treated LDL and displays enhanced electrophilic mobility, Similar results (1.43-fold enhanced uptake of LDL preloaded with PLE) are obtained when the uptake of phospholipid-enriched oxLDL particles are examined, The preference for ingestion as well as protein modification of both preparations is, however, reversed under experimental conditions allowing diffusion and inactivation of a fraction of the peroxidation products, These findings suggest that LDL-associated PAF-acetylhydrolase can exert a dual role and, to be protective to LDL, require an appropriate microenvironment, capable of binding certain species of oxidatively fragmented lipids.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/02/20 alle ore 09:18:23