scholarly journals Functional Expression of the Murine Connexin 36 Gene Coding for a Neuron-Specific Gap Junctional Protein

2000 ◽  
Vol 176 (3) ◽  
pp. 249-262 ◽  
Author(s):  
B. Teubner ◽  
J. Degen ◽  
G. Söhl ◽  
M. Güldenagel ◽  
F.F. Bukauskas ◽  
...  
2000 ◽  
Vol 176 (3) ◽  
pp. 249-262 ◽  
Author(s):  
B. Teubner ◽  
J. Degen ◽  
G. Söhl ◽  
M. Güldenagel ◽  
F.F. Bukauskas ◽  
...  

1998 ◽  
Vol 140 (6) ◽  
pp. 1453-1461 ◽  
Author(s):  
Heinz-Dieter Gabriel ◽  
Dirk Jung ◽  
Christoph Bützler ◽  
Achim Temme ◽  
Otto Traub ◽  
...  

Mice that harbor a targeted homozygous defect in the gene coding for the gap junctional protein connexin26 died in utero during the transient phase from early to midgestation. From day 10 post coitum onwards, development of homozygous embryos was retarded, which led to death around day 11 post coitum. Except for growth retardation, no gross morphological alterations were detected between homozygous connexin26-defective embryos and wild-type littermates. At day 9 postcoitum, when chorioallantoic placenta started to function, connexin26 was weakly expressed in the yolk sac epithelium, between syncytiotrophoblasts I and II in the labyrinth region of the placenta, and in the skin of the embryo. At day 10 post coitum, expression of connexin26 in the placenta was much stronger than at the other locations. To analyze involvement of connexin26 in the placental transfer of nutrients, we have measured embryonic uptake of the nonmetabolizable glucose analogue 3-O-[14C]methylglucose, injected into the maternal tail vein. At day 10 post coitum, viable, homozygous connexin26-defective embryos accumulated only ∼40% of the radioactivity measured in wild-type and heterozygous littermates of the same size. We conclude that the uptake of glucose, and presumably other nutrients as well, from maternal blood into connexin26-deficient mouse embryos was severely impaired and apparently not sufficient to support the rapid organogenesis during midgestation. Our results suggest that connexin26 gap junction channels likely fulfill an essential role in the transfer of maternal nutrients and embryonic waste products between syncytiotrophoblast I and II in the labyrinth layer of the mouse placenta.


2020 ◽  
Vol 21 (15) ◽  
pp. 5401
Author(s):  
Anna Kotova ◽  
Ksenia Timonina ◽  
Georg R. Zoidl

The gap junctional protein connexin 36 (Cx36) has been co-purified with the lipid raft protein caveolin-1 (Cav-1). The relevance of an interaction between the two proteins is unknown. In this study, we explored the significance of Cav-1 interaction in the context of intracellular and membrane transport of Cx36. Coimmunoprecipitation assays and Förster resonance energy transfer analysis (FRET) were used to confirm the interaction between the two proteins in the Neuro 2a cell line. We found that the Cx36 and Cav-1 interaction was dependent on the intracellular calcium levels. By employing different microscopy techniques, we demonstrated that Cav-1 enhances the vesicular transport of Cx36. Pharmacological interventions coupled with cell surface biotinylation assays and FRET analysis revealed that Cav-1 regulates membrane localization of Cx36. Our data indicate that the interaction between Cx36 and Cav-1 plays a role in the internalization of Cx36 by a caveolin-dependent pathway.


1994 ◽  
Vol 652 (2) ◽  
pp. 311-322 ◽  
Author(s):  
M.Z. Hossain ◽  
J. Peeling ◽  
G.R. Sutherland ◽  
E.L. Hertzberg ◽  
J.I. Nagy

1998 ◽  
Vol 114 ◽  
pp. A1171
Author(s):  
Gilbert R. Ortega ◽  
Rosh Caroppo ◽  
Edgar B. Rodas ◽  
Athar M. Qureshi ◽  
David C. Spray ◽  
...  

2009 ◽  
Vol 81 (Suppl_1) ◽  
pp. 560-560
Author(s):  
Jerzy J. Bilski ◽  
Kimberly A. Vonnahme ◽  
Samantha Billings ◽  
Joel S. Caton ◽  
Dale A. Redmer ◽  
...  

1993 ◽  
Vol 105 (4) ◽  
pp. 985-991 ◽  
Author(s):  
R.G. Gourdie ◽  
N.J. Severs ◽  
C.R. Green ◽  
S. Rothery ◽  
P. Germroth ◽  
...  

Electrical coupling between heart muscle cells is mediated by specialised regions of sarcolemmal interaction termed gap junctions. In previous work, we have demonstrated that connexin42, a recently identified gap-junctional protein, is present in the specialised conduction tissues of the avian heart. In the present study, the spatial distribution of the mammalian homologue of this protein, connexin40, was examined using immunofluorescence, confocal scanning laser microscopy and quantitative digital image analysis in order to determine whether a parallel distribution occurs in rat. Connexin40 was detected by immunofluorescence in all main components of the atrioventricular conduction system including the atrioventricular node, atrioventricular bundle, and Purkinje fibres. Quantitation revealed that levels of connexin40 immunofluorescence increased along the axis of atrioventricular conduction, rising over 10-fold between atrioventricular node and atrioventricular bundle and a further 10-fold between atrioventricular bundle and Purkinje fibres. Connexin40 and connexin43, the principal gap-junctional protein of the mammalian heart, were co-localised within atrioventricular nodal tissues and Purkinje fibres. By applying a novel photobleach/double-labelling protocol, it was demonstrated that connexin40 and connexin43 are co-localised in precisely the same Purkinje fibre myocytes. A model, integrating data on the spatial distribution and relative abundance of connexin40 and connexin43 in the heart, proposes how myocyte-type-specific patterns of connexin isform expression account for the electrical continuity of cardiac atrioventricular conduction.


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