title: Influence of culture conditions on the alpha 1,2-fucosyltransferase and MUC gene expression of a transformed cell line MM-39 derived from human tracheal gland cells.
abstract: Human tracheal glands cells (HTGC) in culture are able to respond to adrenergic, cholinergic and purinergic agonists by increasing their serous and mucin secretions. These secretagogues are also able to maintain an optimal responsiveness of serous cells to stimulation when they are regularly and briefly delivered to the cells, making the HTGC a suitable model to study the serous secretion (Merten, in press). Our interest has been focused on the effects of cholinergic and purinergic secretagogues associated to histamine, on the mucous function of the transformed human tracheal gland cell line MM-39, which has a mixed, both serous and mucous, phenotype. When the cells were exposed to short stimulation every 2 days for 3 weeks with 10 or 100 microM carbachol, UTP and histamine, modifications of their mucous phenotype were observed. The expression of MUC genes appeared dependent on the culture conditions. Transcripts of MUC1, MUC4, and MUC5B genes were observed when the cells were regularly exposed to the mixture of secretagogues at a concentration of 10 microM, in contrast to the unstimulated expression of MUC1 and MUC4 in control cells. MUC1, MUC4, MUC7, MUC6 and MUC11 transcripts were observed when the cells were regularly exposed to the mixture of secretagogues at a concentration of 100 microM. These culture conditions were also able to induce an alpha 1,2-fucosyltransferase activity absent in the MM-39 cells cultivated with standard conditions. There was no marked effect on the alpha 2,3-sialyltransferase activity although the expression pattern of the sialyltransferase genes was reduced to the unique presence of ST3Gal III. In conclusion, MM-39 cells exposed to repeated stimulation by secretagogues at different concentrations express different sero-mucous phenotypes.
authors.affiliation: Unité INSERM no. 377, place de Verdun, 59045 Lille, France.
authors.forename: P
authors.initials: P
authors.lastname: Delmotte
authors.forename: S
authors.initials: S
authors.lastname: Degroote
authors.forename: M
authors.initials: M
authors.lastname: Merten
authors.forename: A
authors.initials: A
authors.lastname: Bernigaud
authors.forename: I
authors.initials: I
authors.lastname: Van Seuningen
authors.forename: C
authors.initials: C
authors.lastname: Figarella
authors.forename: P
authors.initials: P
authors.lastname: Roussel
authors.forename: J M
authors.initials: JM
authors.lastname: Perini
mesh_terms: D000818:Animals; D002417:Cattle; D018929:Cell Culture Techniques / Q000379:methods*; D002461:Cell Line, Transformed; D005647:Fucosyltransferases / Q000235:genetics*; D015870:Gene Expression; D006801:Humans; D018396:Mucin-1 / Q000235:genetics; D055264:Mucin-4; D055257:Mucin-5B; D055272:Mucin-6; D009077:Mucins / Q000235:genetics*; D010446:Peptide Fragments / Q000235:genetics; D012471:Salivary Proteins and Peptides / Q000235:genetics; D012799:Sialyltransferases / Q000235:genetics; D014132:Trachea / Q000166:cytology; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase; D000097631:Galactoside 2-alpha-L-fucosyltransferase
chemical_list: D005647:Fucosyltransferases; D018396:Mucin-1; D055264:Mucin-4; D055257:Mucin-5B; D055272:Mucin-6; D009077:Mucins; D010446:Peptide Fragments; D012471:Salivary Proteins and Peptides; D012799:Sialyltransferases; D000094663:beta-Galactoside alpha-2,3-Sialyltransferase; D000097631:Galactoside 2-alpha-L-fucosyltransferase; C116055:MUC1 tandem repeat peptide; C524658:MUC4 protein, human; C524578:MUC5B protein, human; C524734:MUC6 protein, human; C083238:MUC7 protein, human; C031692:galactoside 3-fucosyltransferase; C019818:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase