Connexin40, a component of gap junctions in vascular endothelium, is restricted in its ability to interact with other connexins.
0301 basic medicine
571
Base Sequence
Xenopus
Molecular Sequence Data
Fluorescent Antibody Technique
Membrane Proteins
Cell Communication
DNA
Cardiovascular System
Connexins
Peptide Fragments
Rats
03 medical and health sciences
Intercellular Junctions
Chemicals And Cas Registry Numbers
Electrochemistry
Oocytes
Animals
Amino Acid Sequence
Endothelium, Vascular
DOI:
10.1091/mbc.4.1.7
Publication Date:
2013-08-16T22:53:46Z
AUTHORS (4)
ABSTRACT
The cellular distribution of connexin40 (Cx40), a newly cloned gap junction structural protein, was examined by immunofluorescence microscopy using two different specific anti-peptide antibodies. Cx40 was detected in the endothelium of muscular as well as elastic arteries in a punctate pattern consistent with the known distribution of gap junctions. However, it was not detected in other cells of the vascular wall. By contrast, Cx43, another connexin present in the cardiovascular system, was not detected in endothelial cells of muscular arteries but was abundant in the myocardium and aortic smooth muscle. We have tested the ability of these connexins to interact functionally. Cx40 was functionally expressed in pairs of Xenopus oocytes and induced the formation of intercellular channels with unique voltage dependence. Unexpectedly, communication did not occur when oocytes expressing Cx40 were paired with those expressing Cx43, although each could interact with a different connexin, Cx37, to form gap junction channels in paired oocytes. These findings indicate that establishment of intercellular communication can be spatially regulated by the selective expression of different connexins and suggest a mechanism that may operate to control the extent of communication between cells.
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