Photofrin II Sensitized Modifications of Ion Transport Across the Plasma Membrane of an Epithelial Cell Line: II. Analysis at the Level of Membrane Patches

1998 ◽  
Vol 166 (3) ◽  
pp. 187-196 ◽  
Author(s):  
L. Kunz ◽  
G. Stark
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cell ◽  
Ion Transport ◽  
Cell Line ◽  
Epithelial Cell Line ◽  
Photofrin Ii

NCL-SG3: a human eccrine sweat gland cell line that retains the capacity for transepithelial ion transport

1989 ◽  
Vol 92 (2) ◽  
pp. 241-249
Author(s):  
C.M. Lee ◽  
J. Dessi
Keyword(s):  
Epithelial Cell ◽  
Ion Transport ◽  
Cell Line ◽  
Intermediate Filament ◽  
Primary Cultures ◽  
Simian Virus 40 ◽  
T Antigen ◽  
Sweat Glands ◽  
Epithelial Cell Line ◽  
Eccrine Sweat

An ion-transporting human epithelial cell line, NCL-SG3, has been established by simian virus 40 (SV40) infection of primary cultures from eccrine sweat glands. The line has been passaged 38 times (over 100 population doublings), has an aneuploid karyotype but has not undergone any ‘crisis’. The cells have retained epithelial morphology and expression of cytokeratin, the intermediate filament characteristic of epithelial cells. Approximately 85% of the population shows at least weak co-expression of vimentin, an intermediate filament associated with mesenchymal and some other non-epithelial cell types in vivo. In addition, SV40 large T-antigen is present, in a predominantly nuclear localization. Electrically resistant cell sheets are formed on dialysis tubing and cellulose-ester permeable supports. Electrogenic ion transport can be stimulated by the beta-adrenergic agonist isoproterenol (10(−6) M) and by lysylbradykinin (10(−7) M) but not by the cholinergic agonist carbachol at 10(−6) M).

Extracellular ATP Modulates Ion Transport via P2Y Purinoceptors in a Middle-Ear Epithelial Cell Line

ORL ◽  
1997 ◽  
Vol 59 (3) ◽  
pp. 170-175 ◽  
Author(s):  
P.-T. Yen ◽  
P. Herman ◽  
T. van den Abbeele ◽  
C.-T. Tan ◽  
P. Bordure ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Ion Transport ◽  
Cell Line ◽  
Middle Ear ◽  
Extracellular Atp ◽  
Epithelial Cell Line

Vasoactive intestinal peptide stimulates protein phosphorylation in a colonic epithelial cell line

1987 ◽  
Vol 253 (3) ◽  
pp. G420-G424 ◽  
Author(s):  
J. A. Cohn
Keyword(s):  
Epithelial Cell ◽  
Ion Transport ◽  
Protein Phosphorylation ◽  
Cell Line ◽  
Vasoactive Intestinal Peptide ◽  
Epithelial Cell Line ◽  
Colonic Epithelial Cell ◽  
Ussing Chambers ◽  
Colonic Epithelial Cell Line ◽  
Stimulation Of

The T84 colonic epithelial cell line was used to examine protein phosphorylation during neurohumoral stimulation of ion transport. T84 cell monolayers grown on collagen-coated filters were mounted in Ussing chambers to measure ion transport stimulated by vasoactive intestinal peptide. Maximal stimulation of active secretion occurred after 8-10 min of stimulation. Protein phosphorylation events accompanying stimulated secretion were detected using two-dimensional gel electrophoresis to resolve phosphoproteins from monolayers previously labeled using 32Pi. Within 8 min of exposure to vasoactive intestinal peptide, several phosphorylation events were detected, including a two- to fivefold increase in 32P incorporation into four soluble proteins with apparent molecular weights of 17,000, 18,000, 23,000, and 37,000. The same phosphorylation response occurs in monolayers stimulated by dibutyryl adenosine 3',5'-cyclic monophosphate (cAMP), suggesting that cAMP mediates these intracellular events. This study indicates that changes in protein phosphorylation accompany the secretory action of vasoactive intestinal peptide and suggests that T84 cells offer a useful model for studying the possibility that such phosphorylation events regulate enterocyte ion transport.

scholarly journals Plasma membrane reorganization induced by tumor promoters in an epithelial cell line.

1984 ◽  
Vol 81 (2) ◽  
pp. 449-452 ◽  
Author(s):  
B. S. Packard ◽  
M. J. Saxton ◽  
M. J. Bissell ◽  
M. P. Klein
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cell ◽  
Cell Line ◽  
Epithelial Cell Line ◽  
Tumor Promoters ◽  
Membrane Reorganization

Regulated endocytosis in a chloride secretory epithelial cell line

1992 ◽  
Vol 262 (3) ◽  
pp. C752-C759 ◽  
Author(s):  
N. A. Bradbury ◽  
T. Jilling ◽  
K. L. Kirk ◽  
R. J. Bridges
Keyword(s):  
Plasma Membrane ◽  
Epithelial Cell ◽  
Adenylate Cyclase ◽  
Cell Line ◽  
Fluid Phase ◽  
Second Messenger ◽  
Transport Proteins ◽  
Epithelial Cell Line ◽  
Cl Secretion ◽  
Cyclic Monophosphate

The colonic epithelial cell line T84 has been shown to be a good model to investigate the regulation of Cl- secretion by the adenosine 3',5'-cyclic monophosphate (cAMP)-mediated second messenger cascade. Regulated exocytic insertion and endocytic retrieval of transport proteins, or proteins that regulate transport proteins, is one mechanism proposed to regulate plasma membrane solute permeabilities. The aims of our studies were to characterize endocytic processes in T84 cells and to investigate their regulation by known activators of Cl- secretion that are mediated by the cAMP second messenger cascade. Forskolin, an activator of adenylate cyclase, caused a marked inhibition of endocytic uptake of the fluid-phase marker horseradish peroxidase (HRP) and the adsorptive marker wheat germ agglutinin conjugated to HRP. Similar inhibition was obtained with vasoactive intestinal peptide, a secretagogue whose receptor is coupled to adenylate cyclase, and 8-(4-chlorophenylthio)adenosine 3',5'-cyclic monophosphate, a membrane-permeable cAMP analogue. 1,9-Dideoxy-forskolin, a forskolin analogue that fails to activate adenylate cyclase, was without effect on endocytosis. Our data show that the net rate of endocytosis, as measured by fluid-phase uptake, is decreased by a cAMP-mediated mechanism. Because the number of Cl- channels or associated regulatory proteins in the plasma membrane reflects a balance between their exocytic insertion and endocytic retrieval, we propose that the cAMP-mediated decrease in endocytosis could contribute to the concomitant increase in plasma membrane Cl- permeability.

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