scholarly journals Inwardly rectifying K+ channel Kir7.1 is highly expressed in thyroid follicular cells, intestinal epithelial cells and choroid plexus epithelial cells: implication for a functional coupling with Na+,K+-ATPase

1999 ◽  
Vol 342 (2) ◽  
pp. 329 ◽  
Author(s):  
Nobuhiro NAKAMURA ◽  
Yoshiro SUZUKI ◽  
Hidenari SAKUTA ◽  
Kayoko OOKATA ◽  
Katsumasa KAWAHARA ◽  
...  
1999 ◽  
Vol 342 (2) ◽  
pp. 329-336 ◽  
Author(s):  
Nobuhiro NAKAMURA ◽  
Yoshiro SUZUKI ◽  
Hidenari SAKUTA ◽  
Kayoko OOKATA ◽  
Katsumasa KAWAHARA ◽  
...  

A novel inwardly rectifying K+ channel, Kir7.1, with unique pore properties, was cloned recently. Working in the field of osmoregulation, we have also identified the same human and rat channel and found that the channel is unique not only in its pore sequence but also in its dense localization in the follicular cells of the thyroid gland. Northern blot analysis revealed that the channel message was abundantly expressed in the thyroid gland and small intestine, and moderately in the kidney, stomach, spinal cord and brain. Immunohistochemistry of the rat thyroid, intestine and choroid plexus demonstrated the expression of the channel protein in the follicular cells and epithelial cells, suggesting a role in the regulation of the ion-transporting functions of these specialized cells. The unique pore properties of Kir7.1 make it a strong candidate for the hypothetical low-conductance K+ channel that is functionally coupled with Na+,K+-ATPase by recycling K+. We therefore further examined the co-localization of Kir7.1 and Na+,K+-ATPase and found that both are localized in the basolateral membrane of the thyroid follicular cell; in the choroid plexus, which is known to be unique in having Na+,K+-ATPase in the apical side of the epithelial cells, Kir7.1 was found in the apical membrane, implying a close functional coupling between the channel and Na+,K+-ATPase.


2001 ◽  
Vol 120 (5) ◽  
pp. A146
Author(s):  
Rao N. Jaladanki ◽  
Li Li ◽  
Oleksandr Platoshyn ◽  
Vera A. Golovina ◽  
Jason X-J Yuan ◽  
...  

2001 ◽  
Vol 120 (5) ◽  
pp. A146-A146
Author(s):  
R JALADANKI ◽  
L LI ◽  
O PLATOSHYN ◽  
V GOLOVINA ◽  
J YUAN ◽  
...  

1991 ◽  
Vol 159 (1) ◽  
pp. 45-64
Author(s):  
CHRISTOPHER A. LORETZ ◽  
CHARLES R. FOURTNER

Using patch-clamp techniques, a Ca2+-dependent, voltage-gated K+ channel [K(Ca) channel] was isolated from the basolateral membrane of NaCl-absorbing intestinal epithelial cells of the goby Gillichthys mirabilis. This K(Ca) channel had a high conductance (approximately 150 pS) in the physiological range of membrane potential. Conclusive identification as a K+ channel is supported by dependence of the reversal potential for single-channel current on the K+ concentration gradient and the ability of Ba2+, Cs+ and other pharmacological agents to block the channel. The channel was highly selective for K+ over Na+ (PNa/PK=0.04). Channel activity, expressed as open probability (Po), was dependent on membrane potential with depolarization increasing Po over the physiological range in the presence of Ca2+. Channel activity was also dependent on cytoplasmic-side Ca2+. Po was reduced to near-zero levels following EGTA chelation of Ca2+ in the solution bathing the cytoplasmic face of excised membrane patches; channel activity was most sensitive to changes in Ca2+ concentration between 10nmoll−1 and 10μmoll−1. This K(Ca) channel may be one of several avenues for K+ exit across the basolateral cell membrane and, as such, may play roles in both transepithelial salt transport and maintenance of intracellular ionic composition.


PLoS ONE ◽  
2016 ◽  
Vol 11 (1) ◽  
pp. e0147736 ◽  
Author(s):  
Sebastian Zundler ◽  
Massimiliano Caioni ◽  
Martina Müller ◽  
Ulrike Strauch ◽  
Claudia Kunst ◽  
...  

Author(s):  
Julian P. Heath ◽  
Buford L. Nichols ◽  
László G. Kömüves

The newborn pig intestine is adapted for the rapid and efficient absorption of nutrients from colostrum. In enterocytes, colostral proteins are taken up into an apical endocytotic complex of channels that transports them to target organelles or to the basal surface for release into the circulation. The apical endocytotic complex of tubules and vesicles clearly is a major intersection in the routes taken by vesicles trafficking to and from the Golgi, lysosomes, and the apical and basolateral cell surfaces.Jejunal tissues were taken from piglets suckled for up to 6 hours and prepared for electron microscopy and immunocytochemistry as previously described.


2001 ◽  
Vol 120 (5) ◽  
pp. A504-A504
Author(s):  
A NEUMANN ◽  
M DEPKAPRONDZINSKI ◽  
C WILHELM ◽  
K FELGENHAUER ◽  
T CASPRITZ ◽  
...  

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