Transepithelial Transport of Rosmarinic Acid in Intestinal Caco-2 Cell Monolayers

2005 ◽  
Vol 69 (3) ◽  
pp. 583-591 ◽  
Author(s):  
Yutaka KONISHI ◽  
Shoko KOBAYASHI
Keyword(s):  
Rosmarinic Acid ◽  
Transepithelial Transport ◽  
Cell Monolayers

Transepithelial transport of Cerulenin across Caco-2 cell monolayers

2009 ◽  
Vol 34 (2) ◽  
pp. 67-72 ◽  
Author(s):  
Da-Hua Fu ◽  
Zhi-Li Liu ◽  
Jun-Shi Liu ◽  
Yun Luo ◽  
Yong Shu ◽  
...  
Keyword(s):  
Transepithelial Transport ◽  
Cell Monolayers

scholarly journals TRANSEPITHELIAL TRANSPORT CHARACTERISTICS OF DIPHENHYDRAMINE ACROSS Caco-2 CELL MONOLAYERS

1998 ◽  
Vol 13 (supplement) ◽  
pp. 104-105
Author(s):  
Hiroshi MIZUUCHI ◽  
Toshiya KATSURA ◽  
Yukiya HASHIMOTO ◽  
Ken-ichi INUI
Keyword(s):  
Transepithelial Transport ◽  
Cell Monolayers

Transepithelial phosphate transport in rabbit proximal tubular cells adapted to phosphate deprivation

1994 ◽  
Vol 266 (6) ◽  
pp. C1609-C1618 ◽  
Author(s):  
S. J. Scheinman ◽  
R. Reid ◽  
R. Coulson ◽  
D. B. Jones ◽  
S. M. Ford
Keyword(s):  
Primary Cultures ◽  
Phosphate Transport ◽  
Progressive Increase ◽  
Transepithelial Transport ◽  
Cortical Cells ◽  
Cell Monolayers ◽  
Pi Transport ◽  
Overnight Incubation ◽  
Proximal Tubular

Both renal and nonrenal cells in culture adapt to deprivation of Pi by increasing Na-dependent Pi uptake. We studied whether this change in uptake is reflected in an increased renal transepithelial Pi transport. We grew primary cultures of rabbit renal cortical cells in plastic flasks and subcultured them onto Millicell-HA filters. This produced cell monolayers, which structurally and functionally resembled proximal tubule. These cells performed Na-dependent net transepithelial transport of 32Pi in the apical-to-basolateral direction that was inhibited by phosphonoformic acid in the apical fluid or by ouabain in the basolateral fluid or by preincubation with parathyroid hormone. Overnight incubation at low Pi concentrations led to a progressive increase in 5-min Na-dependent Pi uptake into cell monolayers. Na-dependent Pi uptake was threefold higher following overnight incubation at 25 microM Pi, compared with 3 mM Pi, and the increase was one-half maximal with incubation at an extracellular Pi concentration ([Pi]) of 300 microM. This was associated with a decrease in Na-dependent transepithelial Pi flux to the basolateral fluid by the same cells, which fell dramatically following incubation at < or = 300 microM Pi. There was no change in Na-dependent uptake or transepithelial transport of L-glutamine. This adaptation to Pi deprivation in vitro appears to serve to restore depleted cell stores of Pi rather than to regulate transepithelial Pi transport.

Intracellular traffic of the MHC class I-like IgG Fc receptor, FcRn, expressed in epithelial MDCK cells

1999 ◽  
Vol 112 (14) ◽  
pp. 2291-2299 ◽  
Author(s):  
A. Praetor ◽  
I. Ellinger ◽  
W. Hunziker
Keyword(s):  
Mhc Class I ◽  
Direct Evidence ◽  
Mdck Cells ◽  
Intracellular Localization ◽  
Fc Receptor ◽  
Class I ◽  
Transepithelial Transport ◽  
Passive Immunity ◽  
Intracellular Traffic ◽  
Cell Monolayers

Transfer of passive immunity from mother to the fetus or newborn involves the transport of IgG across several epithelia. Depending on the species, IgG is transported prenatally across the placenta and yolk sac or is absorbed from colostrum and milk by the small intestine of the suckling newborn. In both cases apical to basolateral transepithelial transport of IgG is thought to be mediated by FcRn, an IgG Fc receptor with homology to MHC class I antigens. We have now expressed the human FcRn in polarized MDCK cells and analyzed the intracellular routing of the receptor. FcRn showed a predominant intracellular localization at steady state. Newly synthesized FcRn was delivered in a non-vectorial fashion to both the apical and basolateral surfaces of MDCK cell monolayers. Following internalization from the apical or basolateral domain, the receptor transcytosed to the opposite surface. These findings provide direct evidence for the transepithelial transport function of FcRn and indicate that the receptor undergoes multiple rounds of transcytosis.

Transepithelial transport of biperiden hydrochloride in Caco-2 cell monolayers

2012 ◽  
Vol 34 (2) ◽  
pp. 223-227 ◽  
Author(s):  
Ivana S. Abalos ◽  
Yanina I. Rodríguez ◽  
Verónica Lozano ◽  
Marina Cereseto ◽  
Maria V. Mussini ◽  
...  
Keyword(s):  
Transepithelial Transport ◽  
Cell Monolayers

scholarly journals AICAR decreases the activity of two distinct amiloride-sensitive Na+-permeable channels in H441 human lung epithelial cell monolayers

2008 ◽  
Vol 295 (5) ◽  
pp. L837-L848 ◽  
Author(s):  
A. P. Albert ◽  
A. M. Woollhead ◽  
O. J. Mace ◽  
D. L. Baines
Keyword(s):  
Epithelial Cell ◽  
Apical Membrane ◽  
Short Circuit ◽  
Adenosine Monophosphate ◽  
Transepithelial Transport ◽  
Open Probability ◽  
Pipette Solution ◽  
Cell Monolayers ◽  
Compound C ◽  
Epithelial Cell Monolayers

Transepithelial transport of Na+ across the lung epithelium via amiloride-sensitive Na+ channels (ENaC) regulates fluid volume in the lung lumen. Activators of AMP-activated protein kinase (AMPK), the adenosine monophosphate mimetic AICAR, and the biguanide metformin decreased amiloride-sensitive apical Na+ conductance (GNa+) in human H441 airway epithelial cell monolayers. Cell-attached patch-clamp recordings identified two distinct constitutively active cation channels in the apical membrane that were likely to contribute to GNa+: a 5-pS highly Na+ selective ENaC-like channel (HSC) and an 18-pS nonselective cation channel (NSC). Substituting NaCl with NMDG-Cl in the patch pipette solution shifted the reversal potentials of HSC and NSC, respectively, from +23 mV to −38 mV and 0 mV to −35 mV. Amiloride at 1 μM inhibited HSC activity and 56% of short-circuit current ( Isc), whereas 10 μM amiloride partially reduced NSC activity and inhibited a further 30% of Isc. Neither conductance was associated with CNG channels as there was no effect of 10 μM pimoside on Isc, HSC, or NSC activity, and 8-bromo-cGMP (0.3–0.1 mM) did not induce or increase HSC or NSC activity. Pretreatment of H441 monolayers with 2 mM AICAR inhibited HSC/NSC activity by 90%, and this effect was reversed by the AMPK inhibitor Compound C. All three ENaC proteins were identified in the apical membrane of H441 monolayers, but no change in their abundance was detected after treatment with AICAR. In conclusion, activation of AMPK with AICAR in H441 cell monolayers is associated with inhibition of two distinct amiloride-sensitive Na+-permeable channels by a mechanism that likely reduces channel open probability.

scholarly journals Transepithelial Transport and Metabolism of Boronated Dipeptides Across Caco-2 and HCT-8 Cell Monolayers

1996 ◽  
Vol 3 (6) ◽  
pp. 277-286
Author(s):  
Amy L. Elkins ◽  
John G. Eley ◽  
Merrill C. Miller III ◽  
Iris H. Hall ◽  
Anup Sood ◽  
...  
Keyword(s):  
Oral Delivery ◽  
Cell Monolayer ◽  
Therapeutic Agents ◽  
Transepithelial Transport ◽  
Passive Transport ◽  
Cell Monolayers ◽  
Proteins And Peptides

Oral delivery of proteins and peptides as therapeutic agents is problematic due to their low bioavailability. This study examined the effect of boronation on the transepithelial transport and metabolism of three glycine-phenylalanine dipeptides in Caco-2 and HCT-8 cell monolayers. The three dipeptides exhibited passive transport characteristics in the monolayer systems. However, metabolism of the boronated dipeptides did occur, but to a lesser extent than the non-boronated glycine-phenylalanine dipeptide. The same metabolic scheme was seen in both cell monolayer system, but greater metabolism was seen in the HCT-8 cell monolayers.

Transepithelial Transport ofp-Coumaric Acid and Gallic Acid in Caco-2 Cell Monolayers

2003 ◽  
Vol 67 (11) ◽  
pp. 2317-2324 ◽  
Author(s):  
Yutaka KONISHI ◽  
Shoko KOBAYASHI ◽  
Makoto SHIMIZU
Keyword(s):  
Gallic Acid ◽  
Transepithelial Transport ◽  
Coumaric Acid ◽  
Cell Monolayers
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