The production of 85kDa N-terminal fragment of apolipoprotein B in mutant HepG2 cells generated by targeted modification of apob gene occurs by ALLN-inhibitable protease cleavage during translocation

Biochemical and Biophysical Research Communications

Volumn 398, Issue 4, 2010, Pages 665-670

  Srivastava, Neelam ^a   Cefalu, A B ^b   Noto, Davide ^b   Schonfeld, Gustav ^a   Averna, Maurizio ^b   Srivastava, Rai Ajit K ^c  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF PALERMO   (Italy)

^c Esperion Therapeutics Inc   (United States)

Author keywords

ApoB 15; Apolipoprotein B; Cysteine protease; Familial hypobetalipoproteinemia; Gene targeting; Translocational degradation

Indexed keywords

APOLIPOPROTEIN; APOLIPOPROTEIN B; APOLIPOPROTEIN B100; APOLIPOPROTEIN B15; APOLIPOPROTEIN B82; CYSTEINE PROTEINASE; MEMBRANE PROTEIN; METHIONINE; METHIONINE S 35; N ACETYLLEUCYLLEUCYLNORLEUCINAL; OLEIC ACID; PROTEIN; PROTEINASE; SULFUR 35; UNCLASSIFIED DRUG; ACETYLLEUCYL LEUCYL NORLEUCINAL; ACETYLLEUCYL-LEUCYL-NORLEUCINAL; CYSTEINE PROTEINASE INHIBITOR; LEUPEPTIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CELL MEMBRANE; CELL STRAIN HEPG2; CONTROLLED STUDY; DENSITY GRADIENT CENTRIFUGATION; ENDOPLASMIC RETICULUM; FRACTIONATION; GENE FREQUENCY; GENE TRANSLOCATION; HETEROZYGOSITY; HOMOLOGOUS RECOMBINATION; HUMAN; HUMAN CELL; INTRACELLULAR MEMBRANE; MUTANT; NONSENSE MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CLEAVAGE; PROTEIN DEGRADATION; PROTEIN METABOLISM; PROTEIN MODIFICATION; PROTEIN SECRETION; PROTEIN SYNTHESIS; REDUCTION; CHEMISTRY; FAMILIAL HYPOBETALIPOPROTEINEMIA; GENETICS; METABOLISM; PROTEIN FOLDING; PROTEIN TRANSPORT; STOP CODON;

APOLIPOPROTEINS B; CODON, NONSENSE; CYSTEINE PROTEASES; CYSTEINE PROTEINASE INHIBITORS; HEP G2 CELLS; HUMANS; HYPOBETALIPOPROTEINEMIA, FAMILIAL, APOLIPOPROTEIN B; LEUPEPTINS; PROTEIN FOLDING; PROTEIN TRANSPORT;

EID: 77955422961     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2010.06.130     Document Type: Article

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