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PMID: 7896822 Published · ppublish English Journal Article

The gap junction proteins beta 1-connexin (connexin-32) and beta 2-connexin (connexin-26) can form heteromeric hemichannels.

The Journal of biological chemistry ·Vol. 270 ·No. 12 ·1995-03-24 ·Pages 6768-72

Stauffer KA

Abstract

Two different types of gap junction proteins, beta 1- and beta 2-connexin, were expressed in insect cells, either singly or together, using infection with recombinant baculovirus. Membrane fractions enriched in gap junction proteins were isolated, and connexons (hemichannels) were solubilized with detergent. These solubilized connexons were then run out on a gel filtration column which was capable of partially separating the two homomeric connexons. It was found that connexons from cells co-infected with both types of baculovirus ran together on this column, whereas connexons from cells infected separately and mixed before solubilization did not, suggesting that in the co-infected cells the two types of connexin are assembled into heteromeric hemichannels.

MeSH Terms
Animals Cells, Cultured Connexin 26 Connexins/chemistry Molecular Weight Recombinant Proteins/chemistry Spodoptera
Chemicals
Connexins Recombinant Proteins connexin 32 Connexin 26
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Stauffer K A
Medical Research Council Laboratory of Molecular Biology, Cambridge, United Kingdom.
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1995-03-24
Pages
6768-72
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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