Tissue and species conservation of the vertebrate and arthropod forms of the low molecular weight (16-18000) proteins of gap junctions.
Gap junctions have been isolated from four murine tissues, from rat and Xenopus laevis liver, and from Nephrops norvegicus (Norway lobster) hepatopancreas. The preparations of gap junctions from each vertebrate tissue contain a single major protein, Mr 16,000, and those from Nephrops hepatopancreas a protein, Mr 18,000. Immunocytochemical studies using affinity-purified antibodies raised against gap junctions from Nephrops show the junctional origin of the 18k protein. Immunological studies using Western blotting and biochemical studies using tryptic peptide mapping show no significant differences between the 16k junctional proteins of mouse and hence provide no evidence of tissue variation. These studies also suggest that the mouse, rat, and Xenopus 16k proteins and the Nephrops 18k protein share some common structural features.
Buultjens
T E
TE
Institute of Genetics, University of Glasgow, Scotland.
Finbow
M E
ME
Lane
N J
NJ
Pitts
J D
JD
D000818:Animals; D017630:Connexins; D004591:Electrophoresis, Polyacrylamide Gel; D007150:Immunohistochemistry; D007365:Intercellular Junctions / Q000648:ultrastructure*; D008565:Membrane Proteins / Q000032:analysis*; D051379:Mice; D008854:Microscopy, Electron; D008970:Molecular Weight; D008121:Nephropidae / Q000378:metabolism; D009928:Organ Specificity; D010449:Peptide Mapping; D014714:Vertebrates / Q000378:metabolism*; D014982:Xenopus laevis
D017630:Connexins; D008565:Membrane Proteins