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Titolo:
ABNORMAL STRUCTURE AND COOPERATIVE BINDING OF LOW-DENSITY-LIPOPROTEINRECEPTORS CONTAINING THE GLU-80-]LYS MUTATION
Autore:
PATEL DD; SOUTAR AK; KNIGHT BL;
Indirizzi:
HAMMERSMITH HOSP,ROYAL POSTGRAD MED SCH,CTR CLIN SCI,MRC,LIPOPROT TEAM,DU CANE RD LONDON W12 0NN ENGLAND HAMMERSMITH HOSP,ROYAL POSTGRAD MED SCH,CTR CLIN SCI,MRC,LIPOPROT TEAM LONDON W12 0NN ENGLAND
Titolo Testata:
Biochimica et biophysica acta, L. Lipids and lipid metabolism
fascicolo: 3, volume: 1255, anno: 1995,
pagine: 285 - 292
SICI:
0005-2760(1995)1255:3<285:ASACBO>2.0.ZU;2-I
Fonte:
ISI
Lingua:
ENG
Soggetto:
HOMOZYGOUS FAMILIAL HYPERCHOLESTEROLEMIA; MONOCYTE-DERIVED MACROPHAGES; LDL RECEPTOR; CULTURED FIBROBLASTS; DIFFERENT PROTEINS; DEGRADATION; GENE; EXPRESSION; PATIENT; SUBJECT;
Keywords:
LDL-RECEPTOR STRUCTURE; LDL-RECEPTOR MUTATIONS; FAMILIAL HYPERCHOLESTEROLEMIA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
D.D. Patel et al., "ABNORMAL STRUCTURE AND COOPERATIVE BINDING OF LOW-DENSITY-LIPOPROTEINRECEPTORS CONTAINING THE GLU-80-]LYS MUTATION", Biochimica et biophysica acta, L. Lipids and lipid metabolism, 1255(3), 1995, pp. 285-292

Abstract

The properties of low-density lipoprotein (LDL) receptors containing a Glu to Lys substitution at position 80 have been studied in fibroblasts from a homozygous familial hypercholesterolaemic subject (MB) and in monkey COS cells transfected with the mutant cDNA. Receptors containing the Glu-80 --> Lys mutation were processed more slowly than the normal protein and only approx. 50% reached the surface as the mature form. Both cell types exhibited a normal concentration binding curve for beta-very-low-density lipoproteins (beta-VLDL) but an atypical, sigmoidal curve for LDL. The mature mutant receptor protein migrated abnormally slowly on SDS-PAGE under non-reducing conditions but normally under reducing conditions or after treatment with neuraminidase. It alsoshowed an unusual ability to form dimers that were stable in detergents. Transfected normal and mutant receptors were apparently cleaved onthe surface of the cells to give a product lacking the NH2-terminal portion of the protein, which was resistant to further proteolytic digestion. The results suggest that the Glu-80 --> Lys substitution produces a change in the conformation of the protein, stabilized by polysaccharide chains, which results in a strong self-association of receptor molecules that affects their ability to bind LDL.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 15:43:50