Functional characterization of Na+-independent choline transport in primary cultures of neurons from mouse cerebral cortex

2006 ◽  
Vol 393 (2-3) ◽  
pp. 216-221 ◽  
Author(s):  
Takuya Fujita ◽  
Ayumi Shimada ◽  
Naoki Okada ◽  
Akira Yamamoto
Keyword(s):  
Cerebral Cortex ◽  
Primary Cultures ◽  
Functional Characterization ◽  
Choline Transport ◽  
Mouse Cerebral Cortex

scholarly journals Functional Characterization of a High-Affinity Choline Transport System in Human Keratinocytes

2002 ◽  
Vol 119 (1) ◽  
pp. 118-121 ◽  
Author(s):  
Kathrin Hoffmann ◽  
Franziska Grafe ◽  
Wolfgang Wohlrab ◽  
Reinhard H. Neubert ◽  
Matthias Brandsch
Keyword(s):  
Transport System ◽  
Functional Characterization ◽  
Human Keratinocytes ◽  
Choline Transport ◽  
High Affinity

Functional linkage of H+/peptide transporter PEPT2 and Na+/H+ exchanger in primary cultures of astrocytes from mouse cerebral cortex

2005 ◽  
Vol 1044 (1) ◽  
pp. 33-41 ◽  
Author(s):  
Miyuki Wada ◽  
Sakiko Miyakawa ◽  
Ayumi Shimada ◽  
Naoki Okada ◽  
Akira Yamamoto ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Primary Cultures ◽  
Peptide Transporter ◽  
Functional Linkage ◽  
Mouse Cerebral Cortex

scholarly journals Molecular cloning and functional characterization of chick lens fiber connexin 45.6.

1994 ◽  
Vol 5 (3) ◽  
pp. 363-373 ◽  
Author(s):  
J X Jiang ◽  
T W White ◽  
D A Goodenough ◽  
D L Paul
Keyword(s):  
Molecular Cloning ◽  
Primary Cultures ◽  
Functional Characterization ◽  
Voltage Sensitivity ◽  
Gap Junctional Intercellular Communication ◽  
Ideal System ◽  
Lens Membranes ◽  
Chick Lens

The avian lens is an ideal system to study gap junctional intercellular communication in development and homeostasis. The lens is experimentally more accessible in the developing chick embryo than in other organisms, and chick lens cells differentiate well in primary cultures. However, only two members of the connexin gene family have been identified in the avian lens, whereas three are known in the mammalian system. We report here the molecular cloning and characterization of the third lens connexin, chick connexin45.6 (ChCx45.6), a protein with a predicted molecular mass of 45.6 kDa. ChCx45.6 was encoded by a single copy gene and was expressed specifically in the lens. There were two mRNA species of 6.4 kilobase (kb) and 9.4 kb in length. ChCx45.6 was a functional connexin protein, because expression in Xenopus oocyte pairs resulted in the development of high levels of conductance with a characteristic voltage sensitivity. Antisera were raised against ChCx45.6 and chick connexin56 (ChCx56), another avian lens-specific connexin, permitting the examination of the distribution of both proteins. Immunofluorescence localization showed that both ChCx45.6 and ChCx56 were abundant in lens fibers. Treatment of lens membranes with alkaline phosphatase resulted in electrophoretic mobility shifts, demonstrating that both ChCx45.6 and ChCx56 were phosphoproteins in vivo.

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