Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice

Journal of Biological Chemistry

Volumn 278, Issue 35, 2003, Pages 33194-33199

  Shirahama Noda, Kanae ^a   Yamamoto, Akitsugu ^b,e   Sugihara, Kazushi ^c   Hashimoto, Noriyoshi ^c   Asano, Masahide ^c   Nishimura, Mikio ^a   Hara Nishimura, Ikuko ^d  

^a NATIONAL INSTITUTE FOR BASIC BIOLOGY   (Japan)

^b KANSAI MEDICAL UNIVERSITY   (Japan)

^c KANAZAWA UNIVERSITY   (Japan)

^d KYOTO UNIVERSITY   (Japan)

^e NAGAHAMA INSTITUTE OF BIO SCIENCE AND TECHNOLOGY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; BIOLOGICAL ORGANS; CELLS; DEGRADATION; PLANTS (BOTANY);

ENDOSOMES;

ENZYMES;

ASPARAGINE; CATHEPSIN; CATHEPSIN B; CATHEPSIN H; CATHEPSIN L; CELL ENZYME; CELL PROTEIN; CYSTEINE PROTEINASE; LEGUMAIN; LYSOSOME ENZYME; PROTEINASE; UNCLASSIFIED DRUG; VACUOLAR PROCESSING ENZYME;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BIOACCUMULATION; BODY WEIGHT; CELL VACUOLE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; ELECTRON; ELECTRON MICROSCOPY; ENDOSOME; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME DEFICIENCY; ENZYME LOCALIZATION; ENZYME MECHANISM; ENZYME STRUCTURE; FEMALE; GENE DISRUPTION; IN VIVO STUDY; KIDNEY PROXIMAL TUBULE; KIDNEY TUBULE CELL; LYSOSOME; MACROMOLECULE; MALE; MEMBRANE FUSION; MEMBRANE STRUCTURE; MOLECULAR CLONING; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PROCESSING; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; WILD TYPE;

ANIMALS; ASPARAGINE; BLOTTING, NORTHERN; BODY WEIGHT; CATHEPSINS; CYSTEINE ENDOPEPTIDASES; DNA, COMPLEMENTARY; ENDOPEPTIDASES; ENDOSOMES; GENE LIBRARY; IMMUNOBLOTTING; KIDNEY; LYSOSOMES; MICE; MICE, TRANSGENIC; MICROSCOPY, ELECTRON; MICROSCOPY, FLUORESCENCE; MODELS, GENETIC; MUTATION; PLANT PROTEINS; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA; TISSUE DISTRIBUTION;

ANIMALIA; MAMMALIA;

EID: 0041876230     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M302742200     Document Type: Article

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