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Titolo:
SYNTHESIS AND PROPERTIES OF THE VERY-LOW-DENSITY-LIPOPROTEIN RECEPTORAND A COMPARISON WITH THE LOW-DENSITY-LIPOPROTEIN RECEPTOR
Autore:
PATEL DD; FORDER RA; SOUTAR AK; KNIGHT BL;
Indirizzi:
HAMMERSMITH HOSP,ROYAL POSTGRAD MED SCH,MRC LIPOPROT TEAM,CTR CLIN SCI,DU CANE RD LONDON W12 0NN ENGLAND HAMMERSMITH HOSP,ROYAL POSTGRAD MED SCH,MRC LIPOPROT TEAM,CTR CLIN SCI LONDON W12 0NN ENGLAND ZENECA PHARMACEUT MACCLESFIELD SK10 4TG CHESHIRE ENGLAND
Titolo Testata:
Biochemical journal
, volume: 324, anno: 1997,
parte:, 2
pagine: 371 - 377
SICI:
0264-6021(1997)324:<371:SAPOTV>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
MONOCYTE-DERIVED MACROPHAGES; CULTURED HUMAN-FIBROBLASTS; LDL RECEPTOR; FAMILIAL HYPERCHOLESTEROLEMIA; DIFFERENT PROTEINS; BINDING; GENE; DEGRADATION; DOMAIN; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
D.D. Patel et al., "SYNTHESIS AND PROPERTIES OF THE VERY-LOW-DENSITY-LIPOPROTEIN RECEPTORAND A COMPARISON WITH THE LOW-DENSITY-LIPOPROTEIN RECEPTOR", Biochemical journal, 324, 1997, pp. 371-377

Abstract

The properties of the very-low-density lipoprotein (VLDL) receptor have been studied in Chinese hamster ovary (CHO) cells stably transfected with human VLDL-receptor cDNA and compared with those of the low-density lipoprotein (LDL) receptor expressed under the same conditions. Immunoblotting showed that the cells produced a mature VLDL receptor protein, of apparent M-r 123000 on non-reduced and 158000 on reduced gels, that was less extensively glycosylated than the LDL receptor. The VLDL receptor was more slowly processed than the LDL receptor, with only approx. 70 % of the precursor being converted into the mature protein. Nevertheless, the majority of the receptor in the cells was in the mature form, and most of this was present on the cell surface. The human VLDL receptor bound rabbit very-low-density lipoprotein with beta electrophoretic mobility (beta VLDL), but not human LDL, and uptake through the receptor led to stimulation of oleate incorporation into cholesteryl esters. At 37 degrees C, the characteristics of VLDL-receptor-mediated uptake and degradation of beta VLDL were essentially the sameas those mediated by the LDL receptor. However, the VLDL receptor apparently did not show the increase in affinity and decrease in binding of beta VLDL on cooling to 4 degrees C that was exhibited by the LDL receptor. Thus the overexpressed VLDL receptor in CHO cells appears to behave as a lipoprotein receptor with similar, but not identical, properties to the LDL receptor.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 13:29:00