Filipin-sterol complexes in molluscan gill ciliated epithelial cell membranes: intercalation into ciliary necklaces and induction of gap junctional particle arrays

1990 ◽  
Vol 262 (2) ◽  
pp. 301-306 ◽  
Author(s):  
R. E. Stephens ◽  
M. J. Good
Keyword(s):  
Epithelial Cell ◽  
Cell Membranes ◽  
Ciliary Necklaces ◽  
Ciliated Epithelial Cell ◽  
Gap Junctional

scholarly journals Establishment of a ciliated epithelial cell line from human Fallopian tube

2000 ◽  
Vol 15 (7) ◽  
pp. 1597-1603 ◽  
Author(s):  
Hisao Ando ◽  
Miya Kobayashi ◽  
Shigeru Toda ◽  
Fumitaka Kikkawa ◽  
Tetsuo Masahashi ◽  
...  
Keyword(s):  
Epithelial Cell ◽  
Cell Line ◽  
Fallopian Tube ◽  
Epithelial Cell Line ◽  
Human Fallopian Tube ◽  
Ciliated Epithelial Cell

scholarly journals Characterization of glycopeptides labelled from d-[2-3H]mannose and l-[6-3H]fucose in intestinal epithelial cell membranes during differentiation

1980 ◽  
Vol 192 (1) ◽  
pp. 145-153 ◽  
Author(s):  
A Herscovics ◽  
B Bugge ◽  
A Quaroni ◽  
K Kirsch
Keyword(s):  
Epithelial Cell ◽  
Intestinal Epithelial Cell ◽  
Time Course ◽  
Cell Membranes ◽  
Alkali Treatment ◽  
Gel Filtration ◽  
Intestinal Epithelial ◽  
Membrane Glycoproteins ◽  
High Mannose ◽  
Fraction I

The labelled glycopeptides obtained by Pronase digestion of rat intestinal epithelial cell membranes were examined by gel filtration after injection of D-[2-3H]mannose and L-[6-3H]fucose. Three labelled fraction were eluted in the following order from Bio-Gel P-6, Fraction I, which was excluded from the gel, was labelled mostly with [3H]fucose and slightly with [3H]mannose. Fraction II contained “complex” asparagine-linked oligosaccharides since it was labelled with [3H]mannose and [3H]fucose, was stable to mild alkali treatment, and resistant to endo-beta-N-acetyl-glucosaminidase H. Fraction III contained “high-mannose” asparagine-linked oligosaccharides, which were labelled with [3H]mannose, but not with [3H]fucose; these were sensitive to endo-beta-N-acetylglucosaminidase H, and were adsorbed on concanavalin A-Sepharose and subsequently eluted with methyl alpha-D-mannopyranoside. The time course of incorporation of [3H]mannose into these glycopeptides in microsomal fractions showed that high-mannose oligosaccharides were precursors of complex oligosaccharides. The rate of this processing was faster in rapidly dividing crypt cells than in differentiated villus cells. The ratio of radioactively labelled complex oligosaccharides to high-mannose oligosaccharides, 3h after [3H]mannose injection, was greater in crypt than in villus-cell lateral membranes. Luminal membranes of both crypt and villus cells were greatly enriched in labelled complex oligosaccharides compared with the labelling in lateral-basal membranes. These studies show that intestinal epithelial cells are polarized with respect to the structure of the asparagine-linked oligosaccharides on their membrane glycoproteins. During differentiation of these cells quantitative differences in labelled membrane glycopeptides, But no major qualitative change, were observed.

Novel Specific Inhibitors of Epithelial Phosphate Transport

Physiology ◽  
1988 ◽  
Vol 3 (4) ◽  
pp. 154-157
Author(s):  
SA Kempson
Keyword(s):  
Epithelial Cell ◽  
Cell Membranes ◽  
Phosphate Transport ◽  
Phosphate Transporter ◽  
Transport Function ◽  
Major Difficulty ◽  
Membrane Bound ◽  
Specific Label ◽  
Specific Inhibitors

The characteristics of phosphate transport across epithelial cell membranes and the influence of hormones and other factors have been studied in detail. Almost no information has emerged about the identity, structure, and biogenesis of the membrane-bound phosphate transporting proteins or how their transport function is regulated by intracellular events. One major difficulty has been the unavailability of a highly specific label for the phosphate transporter.

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