title: A polarized salivary cell monolayer useful for studying transepithelial fluid movement in vitro.
abstract: There are no reported, convenient in vitro models for studying polarized functions in salivary epithelial cells. Accordingly, we examined three often-used salivary cell lines for their ability to form a polarized monolayer on permeable, collagen-coated polycarbonate filters. Only the SMIE line, derived from rat submandibular gland, had this ability. The SMIE cell monolayer exhibited junctional complexes, with a tight-junction-associated protein, ZO-1, localized to cell-cell contact areas. The Na+/K+-ATPase alpha1-subunit was detected predominantly in the basolateral membranes, while the Na+/H+ exchanger isoform 2 appeared primarily in the apical membranes. Using adenovirus-mediated cDNA transfer, SMIE cells were shown to be capable of routing marker proteins (beta-galactosidase +/- a nuclear targeting signal, alpha1-antitrypsin, aquaporin-1) to appropriate locations. Furthermore, this salivary cell monolayer provided a convenient tool for studying aquaporin-1-mediated, osmotically directed, transepithelial fluid movement in vitro. Thus, SMIE cells appear to be a useful experimental model with which to study some polarized functions in a salivary epithelial cell line.
authors.affiliation: Gene Therapy and Therapeutics Branch, National Institute of Dental Research, 10 Center Drive, MSC 1190, Bldg 10/Rm 1N113, Bethesda MD 20892-1190, USA.
authors.forename: X
authors.initials: X
authors.lastname: He
authors.forename: G A
authors.initials: GA
authors.lastname: Kuijpers
authors.forename: G
authors.initials: G
authors.lastname: Goping
authors.forename: J A
authors.initials: JA
authors.lastname: Kulakusky
authors.forename: C
authors.initials: C
authors.lastname: Zheng
authors.forename: C
authors.initials: C
authors.lastname: Delporte
authors.forename: C M
authors.initials: CM
authors.lastname: Tse
authors.forename: R S
authors.initials: RS
authors.lastname: Redman
authors.forename: M
authors.initials: M
authors.lastname: Donowitz
authors.forename: H B
authors.initials: HB
authors.lastname: Pollard
authors.forename: B J
authors.initials: BJ
authors.lastname: Baum
mesh_terms: D000256:Adenoviridae; D000818:Animals; D051398:Aquaporin 1; D020346:Aquaporins; D001789:Blood Group Antigens; D002450:Cell Communication; D002461:Cell Line, Transformed; D002462:Cell Membrane / Q000737:chemistry; D016764:Cell Polarity; D018076:DNA, Complementary; D004847:Epithelial Cells / Q000502:physiology / Q000648:ultrastructure; D018014:Gene Transfer Techniques; D006801:Humans; D007365:Intercellular Junctions / Q000737:chemistry; D007473:Ion Channels / Q000235:genetics / Q000502:physiology; D008565:Membrane Proteins / Q000032:analysis; D008854:Microscopy, Electron; D009997:Osmotic Pressure; D010750:Phosphoproteins / Q000032:analysis; D051381:Rats; D017923:Sodium-Hydrogen Exchangers / Q000032:analysis; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis; D013363:Submandibular Gland / Q000502:physiology* / Q000648:ultrastructure*; D062826:Zonula Occludens-1 Protein; D000515:alpha 1-Antitrypsin / Q000235:genetics; D001616:beta-Galactosidase / Q000235:genetics
chemical_list: C496020:AQP1 protein, human; C496022:Aqp1 protein, rat; D020346:Aquaporins; D001789:Blood Group Antigens; D018076:DNA, Complementary; D007473:Ion Channels; D008565:Membrane Proteins; D010750:Phosphoproteins; D017923:Sodium-Hydrogen Exchangers; C569042:TJP1 protein, human; C569044:Tjp1 protein, rat; D062826:Zonula Occludens-1 Protein; D000515:alpha 1-Antitrypsin; D051398:Aquaporin 1; D001616:beta-Galactosidase; D000254:Sodium-Potassium-Exchanging ATPase