Identification of a rat liver cDNA and mRNA coding for the 28 kDa gap junction protein

FEBS Letters ◽  
1986 ◽  
Vol 205 (1) ◽  
pp. 56-60 ◽  
Author(s):  
Roland Heynkes ◽  
Gisela Kozjek ◽  
Otto Traub ◽  
Klaus Willecke
Keyword(s):  
Gap Junction ◽  
Rat Liver ◽  
Junction Protein ◽  
Gap Junction Protein

Analysis of distribution patterns of gap junctions during development of embryonic chick facial primordia and brain

Development ◽  
1991 ◽  
Vol 111 (2) ◽  
pp. 509-522
Author(s):  
R. Minkoff ◽  
S.B. Parker ◽  
E.L. Hertzberg
Keyword(s):  
Gap Junctions ◽  
Gap Junction ◽  
Uniform Distribution ◽  
Rat Liver ◽  
Connexin 43 ◽  
Cell Communication ◽  
Exterior Surface ◽  
Junction Protein ◽  
Primary Palate ◽  
Gap Junction Protein

Gap junction distribution in the facial primordia of chick embryos at the time of primary palate formation was studied employing indirect immunofluorescence localization with antibodies to gap junction proteins initially identified in rat liver (27 × 10(3) Mr, connexin 32) and heart (43 × 10(3) Mr, connexin 43). Immunolocalization with antibodies to the rat liver gap junction protein (27 × 10(3) Mr) demonstrated a ubiquitous and uniform distribution in all regions of the epithelium and mesenchyme except the nasal placode. In the placodal epithelium, a unique non-random distribution was found characterized by two zones: a very heavy concentration of signal in the superficial layer of cells adjacent to the exterior surface and a region devoid of detectable signal in the interior cell layer adjacent to the mesenchyme. This pattern was seen during all stages of placode invagination that were examined. The separation of gap junctions in distinct cell layers was unique to the nasal placode, and was not found in any other region of the developing primary palate. One other tissue was found that exhibited this pattern-the developing neural epithelium of the brain and retina. These observations suggest the presence of region-specific signaling mechanisms and, possibly, an impedance of cell communication among subpopulations of cells in these structures at critical stages of development. Immunolocalization with antibodies to the ‘heart’ 43 × 10(3) Mr gap junction protein also revealed the presence of gap junction protein in facial primordia and neural epithelium. A non-uniform distribution of immunoreactivity was also observed for connexin 43.

scholarly journals Rat liver gap junction protein: properties and partial sequence.

1981 ◽  
Vol 78 (12) ◽  
pp. 7594-7598 ◽  
Author(s):  
B. J. Nicholson ◽  
M. W. Hunkapiller ◽  
L. B. Grim ◽  
L. E. Hood ◽  
J. P. Revel
Keyword(s):  
Gap Junction ◽  
Rat Liver ◽  
Partial Sequence ◽  
Junction Protein ◽  
Protein Properties ◽  
Gap Junction Protein

Analysis of the rat liver gap junction protein : clarification of anomalies in its molecular size

1988 ◽  
Vol 233 (1271) ◽  
pp. 165-174 ◽  
Keyword(s):  
Molecular Mass ◽  
Gap Junction ◽  
Rat Liver ◽  
Cdna Sequence ◽  
Tissue Homogenate ◽  
Polyacrylamide Gels ◽  
Western Blots ◽  
Amino Terminal ◽  
Junction Protein ◽  
Gap Junction Protein

The major gap junction polypeptide in most tissues has an apparent molecular mass of 27 kDa with a 47 kDa dimer present in junction-enriched fractions. However, a 54 kDa protein recognized by gap junction-specific antibodies has been reported and a complementary DNA (cDNA) sequence for both human and rat liver gap junctions codes for a 32 kDa protein. In this paper we show that these are all forms of the same gap junction protein that can be observed on SDS–polyacrylamide gels simply by varying the concentration of acrylamide in the gels. A 64 kDa dimer is also obtainable. Antibodies to the gap junction protein or to a synthetic peptide constructed to match the rat liver gap junction amino-terminal sequence recognize all of these forms. Under some conditions a 54 kDa dimer is ‘preferred’, explaining the presence of this species in whole tissue homogenate Western blots. These results clarify several controversies and indicate that the protein forming the gap junction channel probably undergoes no major post-translational modification as the cDNA sequence codes for a protein of molecular mass 32 kDa and this protein species and its 64 kDa dimer are demonstrable on SDS–polyacrylamide gels under appropriate conditions.

Changes in gap junction protein (connexin 32) gene expression during rat liver carcinogenesis

1989 ◽  
Vol 41 (2) ◽  
pp. 97-102 ◽  
Author(s):  
D. James Fitzgerald ◽  
Marc Mesnil ◽  
Masahito Oyamada ◽  
Hiroyuki Tsuda ◽  
Nobuyuki Ito ◽  
...  
Keyword(s):  
Gene Expression ◽  
Gap Junction ◽  
Rat Liver ◽  
Connexin 32 ◽  
Liver Carcinogenesis ◽  
Junction Protein ◽  
Gap Junction Protein

scholarly journals Voltage-dependent gap junction channels are formed by connexin32, the major gap junction protein of rat liver

1991 ◽  
Vol 59 (4) ◽  
pp. 920-925 ◽  
Author(s):  
A.P. Moreno ◽  
A.C. de Carvalho ◽  
V. Verselis ◽  
B. Eghbali ◽  
D.C. Spray
Keyword(s):  
Gap Junction ◽  
Rat Liver ◽  
Gap Junction Channels ◽  
Junction Protein ◽  
Voltage Dependent ◽  
Gap Junction Protein

scholarly journals Cloning and characterization of human and rat liver cDNAs coding for a gap junction protein.

1986 ◽  
Vol 103 (3) ◽  
pp. 767-776 ◽  
Author(s):  
N M Kumar ◽  
N B Gilula
Keyword(s):  
Gap Junction ◽  
Rat Liver ◽  
Human Liver ◽  
Single Copy ◽  
In Vitro Translation ◽  
Coding Region ◽  
Human Cdna ◽  
Junction Protein ◽  
Gap Junction Protein

An extended synthetic oligonucleotide (58-mer) has been used to identify and characterize a human liver gap junction cDNA. The cDNA is 1,574 bases long and contains the entire coding region for a gap junction protein. In vitro translation of the RNA products of this cDNA is consistent with it coding for a 32,022-D protein. Southern blot analysis indicates that the gap junction gene is present as a single copy, and that it can be detected in a variety of organisms using the human liver cDNA as a probe. The human cDNA has been used to screen a rat liver cDNA library, and a rat liver junction cDNA clone has been isolated. The rat liver clone is 1,127 bases in length, and it has strong sequence homology to the human cDNA in the protein-coding region, but less extensive homology in the 3'-untranslated region.

Phenobarbital specifically reduces gap junction protein mRNA level in rat liver

1988 ◽  
Vol 1 (2) ◽  
pp. 79-81 ◽  
Author(s):  
Marc Mesnil ◽  
D. James Fitzgerald ◽  
Hiroshi Yamasaki
Keyword(s):  
Gap Junction ◽  
Rat Liver ◽  
Mrna Level ◽  
Junction Protein ◽  
Gap Junction Protein
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