Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Accumulation of sialic acid in endocytic compartments interferes with the formation of mature lysosomes - Impaired proteolytic processing of cathepsin B in fibroblasts of patients with lysosomal sialic acid storage disease
Autore:
Schmid, JA; Mach, L; Paschke, E; Glossl, J;
Indirizzi:
Univ Vienna, Dept Vasc Biol & Thrombosis Res, A-1235 Vienna, Austria Univ Vienna Vienna Austria A-1235 Thrombosis Res, A-1235 Vienna, Austria Univ Agr Sci, Ctr Appl Genet, A-1190 Vienna, Austria Univ Agr Sci ViennaAustria A-1190 tr Appl Genet, A-1190 Vienna, Austria Univ Western Australia, Dept Biochem, Nedlands, WA 6907, Australia Univ Western Australia Nedlands WA Australia 6907 nds, WA 6907, Australia Childrens Hosp, A-8036 Graz, Austria Childrens Hosp Graz Austria A-8036Childrens Hosp, A-8036 Graz, Austria
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 27, volume: 274, anno: 1999,
pagine: 19063 - 19071
SICI:
0021-9258(19990702)274:27<19063:AOSAIE>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
CULTURED HUMAN-FIBROBLASTS; MANNOSE 6-PHOSPHATE RECEPTOR; N-ACETYLNEURAMINIC ACID; LATE ENDOSOMES; BETA-HEXOSAMINIDASE; PROCATHEPSIN-B; SALLA DISEASE; MULTIVESICULAR ENDOSOMES; PROTEIN-DEGRADATION; TERMINAL LYSOSOMES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Glossl, J Univ Vienna, Dept Vasc Biol & Thrombosis Res, Brunnerstr 59, A-1235 Vienna, Austria Univ Vienna Brunnerstr 59 Vienna Austria A-1235 Vienna, Austria
Citazione:
J.A. Schmid et al., "Accumulation of sialic acid in endocytic compartments interferes with the formation of mature lysosomes - Impaired proteolytic processing of cathepsin B in fibroblasts of patients with lysosomal sialic acid storage disease", J BIOL CHEM, 274(27), 1999, pp. 19063-19071

Abstract

The impact of an altered endocytic environment on the biogenesis of lysosomes was studied in fibroblasts of patients suffering from sialic acid storage disease (SASD). This inherited disorder is characterized by the accumulation of acidic monosaccharides in lysosomal compartments and a concomitant decrease of their buoyant density. We demonstrate that C-terminal trimming of the lysosomal cysteine proteinase cathepsin B is inhibited in SASD fibroblasts. This late event in the biosynthesis of cathepsin B normally takes place in mature lysosomes, suggesting an impaired biogenesis of these organelles in SASD cells. When normal fibroblasts are loaded with sucrose, which inhibits transport from late endosomes to lysosomes, C-terminal cathepsin Bprocessing is prevented to the same extent. Further characterization of the terminal endocytic compartments of SASD cells revealed properties usuallyassociated with late endosomes/prelysosomes. In addition to a decreased buoyant density, SASD "lysosomes" show a reduced acidification capacity and appear smaller than their normal counterparts. We conclude that the accumulation of small non-diffusible compounds within endocytic compartments interferes with the formation of mature lysosomes and that the acidic environmentof the latter organelles is a prerequisite for C-terminal processing of lysosomal hydrolases.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 15:42:17