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Titolo:
CELL-SURFACE CARBOHYDRATES OF RAT ALVEOLAR TYPE-II CELLS IN PRIMARY CULTURE
Autore:
CRESTANI B; DEHOUX M; SETA N; CUER M; AUBIER M;
Indirizzi:
HOP BICHAT,UNITE PNEUMOL,46 RUE HENRI HUCHARD F-75877 PARIS 18 FRANCE FAC XAVIER BICHAT,BIOCHIM LAB PARIS FRANCE FAC XAVIER BICHAT,INSERM,U226 PARIS FRANCE
Titolo Testata:
American journal of respiratory cell and molecular biology
fascicolo: 2, volume: 8, anno: 1993,
pagine: 145 - 152
SICI:
1044-1549(1993)8:2<145:CCORAT>2.0.ZU;2-E
Fonte:
ISI
Lingua:
ENG
Soggetto:
EPITHELIAL-CELLS; GLYCOPROTEINS; NEURAMINIDASE; LYMPHOCYTES; PERIODATE; GALACTOSE; ADHESION; PROTEINS; BINDING; SYSTEM;
Tipo documento:
Article
Natura:
Periodico
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
B. Crestani et al., "CELL-SURFACE CARBOHYDRATES OF RAT ALVEOLAR TYPE-II CELLS IN PRIMARY CULTURE", American journal of respiratory cell and molecular biology, 8(2), 1993, pp. 145-152

Abstract

Cell surface carbohydrates have been shown to be altered during cellular differentiation. Alveolar type II (ATII) cells in culture gradually lose their differentiated phenotype. Therefore, the aim of this study was (1) to characterize changes in terminal carbohydrates of cell surface glycoproteins of rat ATII cells cultured for 1 to 5 days on plastic, and (2) to assess the concomitant changes in sialidase and sialyltransferase activity of ATII cell homogenates. Cells were surface-labeled with potassium-[H-3]-borohydride after oxidation by sodium periodate at millimolar concentrations, galactose oxidase or neuraminidase plus galactose oxidase, allowing for the specific labeling of terminal sialic acids, terminal galactose/N-acetylgalactosamine (Gal/GalNAc), orterminal and penultimate Gal/GalNAc residues, respectively. Glycoproteins were separated by SDS-PAGE. On day 1, cells were heavily coated with sialic acids, since no labeling could be introduced with galactoseoxidase alone. From day 1 to day 5, we observed a selective and progressive desialylation of two glycoproteins (200 and 165 kD). At the same time, the ATII cells' sialidase activity (pH 4.2) exhibited an 8-fold increase (60.3 +/- 4.0 pmol/min/mg protein on day 1 versus 406.9 +/-3.7 pmol/min/mg protein on day 5), whereas the sialyltransferase activity increased 2-fold (212 +/- 8 fmol/min/mg protein on day 1 versus 395 +/- 82 fmol/min/mg protein on day 5) and the supernatant sialidase activity was unchanged (2.8 +/- 0.7 pmol/min/ml on day 5). Thus, the phenotypic changes of ATII cells in primary culture are accompanied by a partial cell surface desialylation and an increase in intracellular sialidase activity.

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Documento generato il 30/11/20 alle ore 19:50:09