Cited by 84Connexins and lens biologyPancreatic function and diabetesIon channel regulation and function

Biophysical evidence that connexin-36 forms functional gap junction channels between pancreatic mouse β-cells

Moreno, Alonso P., Berthoud, Viviana M., Pérez-Palacios, Gregorio, Pérez-Armendariz, E. Martha·2005·American Journal of Physiology-Endocrinology and Metabolism

Abstract

Connexin-36 (Cx36) is the only gap junction protein that has been unambiguously identified in rodent pancreatic β-cells. However, properties of gap junction channel unitary currents between β-cells remain unrevealed. To address whether Cx36 forms functional channels in β-cells, we characterized biophysical properties of macro- and microscopic junctional currents recorded from dual whole cell voltage clamp isolated pairs of dispersed mouse β-cells. Electrical coupling was recorded in 80% of cell pairs with a junctional conductance ( g j ) of 355 ± 45 pS ( n = 20). Transjunctional voltage dependence was identified in three of seven cell pairs with high-input membrane resistances. Normalized steady-state g j ( G j ) and transjunctional-voltage relation were well described by a two-state Boltzmann equation [maximal conductance ( G max ) = 1.0, voltage-insensitive conductance ( G min ) = 0.3 and 0.28, voltage gating sensitivity ( A) = 0.21 and 0.23, and voltage at which one-half of the initial voltage-dependent conductance was reached ( V o ) = −85 and 87 mV for negative and positive potentials, respectively]. Halothane reversibly uncoupled β-cell pairs, and, during recovery, unitary conductances of 5–10 pS were recorded while using patch pipettes containing mainly CsCl. Although these properties are similar to those previously described for Cx36 channels in mammalian cell systems, we found that β-cell junctional currents were insensitive to quinine. Cx36 transcript and protein expression in islets and freshly dispersed cell preparations was confirmed by RT-PCR and immunofluorescence. In conclusion, biophysical properties of junctional channels between β-cells are similar but not identical to those previously described for homomeric Cx36 channels. Cell type-specific mechanisms that may account for these differences are discussed.

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Crossref · 10.1152/ajpendo.00216.2004

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Authors
Moreno, A. P., Berthoud, V. M., Pérez-Palacios, G., & Pérez-Armendariz, E. M.
Affiliations
Indiana University School of Medicine (US)
Venue
American Journal of Physiology-Endocrinology and Metabolism
Published
2005-05
Volume
288
Issue
5
Pages
E948-E956
ISSN
  • 0193-1849 (ISSN-L)
  • 1522-1555
OpenAlex
W2149800898
Cited by
84
References
53
Citations by year
2026: 3 · 2025: 2 · 2024: 4 · 2023: 1 · 2022: 4 · 2021: 8 · 2020: 2 · 2019: 2 · 2018: 4 · 2017: 4 · 2016: 4 · 2015: 3 · 2014: 10 · 2013: 8 · 2012: 6
FWCI
1.76
Type
journal article
Language
en
Open access
closed
Locations
  • American Journal of Physiology-Endocrinology and Metabolism (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Heart, Lung, and Blood Institute (R01HL063969, R01 HL-63969-05)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Connexins and lens biology
  • Health Sciences › Medicine › Surgery › Pancreatic function and diabetes
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
Keywords
connexin 36, gap junction channels, pancreatic beta cells, electrical coupling, junctional conductance, voltage-dependent conductance, islets
MeSH terms
Gap Junction delta-2 Protein, Animals, Biophysics, Cell Communication, Cells, Cultured, Eye Proteins, Islets of Langerhans, Membrane Potentials, Gap Junctions, Connexins, Mice

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