Analysis of vertebrate gap junction protein.

Finbow, Malcolm E.; Shuttleworth, James; Hamilton, Anne E.; Pitts, John D.

doi:10.1002/j.1460-2075.1983.tb01611.x

Cited by 59 publications

(26 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…While many lines of evidence, notably the recovery of GJIC after transfection of connexin genes into GJIC-de®cient cells, indicate that connexins are an essential component of gap junctions, it remains impossible to exclude a role of the 16 K protein in GJIC. Evidence supporting such a role includes the fact that the 16 K protein apparently constitutes the major protein component of gap junction channels of arthropods, which do not appear to contain connexin homologs (Finbow et al, 1983;1984).…”

Section: Introductionmentioning

confidence: 99%

Induction of cell transformation by mutated 16K vacuolar H+-atpase (ductin) is accompanied by down-regulation of gap junctional intercellular communication and translocation of connexin 43 in NIH3T3 cells

et al. 1998

View full text Add to dashboard Cite

The 16 K subunit of the vacuolar H + -ATPase (ductin) has been suggested to also play a role in gap junction channels. Since mutated 16 K subunits have transforming ability when transfected into NIH3T3 cells and since aberrant gap junctional intercellular communication (GJIC) is a hallmark of cancer cells, we hypothesized that mutated 16 K subunits might transform these cells via alteration of GJIC. When GJIC was measured by the dye-transfer assay, NIH3T3 cells transfected with the mutant 16 K protein genes (deletion of the fourth transmembrane domain or a point mutation at codon 143 from glutamic acid to arginine) showed signi®cantly lower levels of GJIC than those transfected with the vector alone or with the wild-type 16 K subunit gene. GJIC levels of NIH3T3 cells transformed by v-ras and v-src were not signi®cantly decreased, suggesting that low GJIC levels are not necessarily the result of cell transformation per se. NIH3T3 cells express C643 as a major connexin gene. Although cells transfected with mutated 16 K subunits showed a level of C643 protein expression similar to non-transfectants, their C643 protein was localized aberrantly, i.e. intracytoplasmically. These results indicate that mutant 16 K subunits with transforming ability translocate C643 proteins, thus inhibiting GJIC of NIH3T3 cells.

show abstract

Section: Introductionmentioning

confidence: 99%

Induction of cell transformation by mutated 16K vacuolar H+-atpase (ductin) is accompanied by down-regulation of gap junctional intercellular communication and translocation of connexin 43 in NIH3T3 cells

et al. 1998

View full text Add to dashboard Cite

show abstract

“…A new method of isolating gap junctions has recently been developed in this laboratory which allows the preparation of gap junction enriched fractions from various tissues and from cultured cells (Finbow et al, 1983). Using this method we have found that a single major protein, mol.…”

Section: Introductionmentioning

confidence: 99%

“…wt. 16 000 (16 K), is associated with gap junction preparations from a variety of vertebrate tissues and cultured cells (Finbow et al, 1983). This method has now been applied to the preparation of gap junctions from arthropod tissues.…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterisation of arthropod gap junctions

et al. 1984

View full text Add to dashboard Cite

Gap junctions have been isolated from the hepatopancreas of the crustacean arthropod, Nephrops norvegicus (Norway lobster). SDS‐PAGE of these preparations shows two major protein bands, mol. wt. 18 000 (18 K) and mol. wt. 28 000 (28 K). The 18‐K and 28‐K proteins are interconvertible, cannot be distinguished by two dimensional tryptic and chymotryptic peptide mapping, and therefore appear to be different (most likely monomeric and dimeric) forms of the same protein. The protein can also aggregate to higher multimeric forms mol. wt. 38 000 (presumed trimer), and mol. wt. 52 000 (presumed tetramer). The buoyant density of the isolated gap junctions in continuous potassium iodide gradients is 1.260 g/cm3. The junctions are progressively solubilized in increasing SDS concentrations, mostly between 0.1% and 0.2% SDS, and this is accompanied by the release of the 18‐K and 28‐K forms of the junctional protein. The Nephrops hepatopancreas 18‐K junctional protein has antigenic determinants in common with the vertebrate 16‐K junctional protein as shown by cross‐reactivity with two different affinity purified antibody preparations. However, no detectable similarity can be seen between the major 125I‐labelled tryptic and chymotrytpic peptides of the Nephrops hepatopancreas 18‐K protein and the mouse liver 16‐K protein.

show abstract

“…TPA, on metabolic cooperation have shown a positive correlation between the efficacy of the agent as a tumor promoter and the severity of the decrease in cooperation (79). In at least one of these systems, V79 cells treated with TPA, there is a decrease in gap junctions and in the amount of a putative junctional protein (18,78); in another system there is a demonstrable decrease in electrical coupling (14). The time required for these junctional responses to develop is appreciable (1 or 2 days), so that the relationship between TPA treatment and the junctional response involves a number of unknown mechanisms (44).…”

Section: Modulation Of Junctional Capacitymentioning

confidence: 99%