Gap junction function

Meda, Paolo; Spray, David C.

doi:10.1016/s1569-2558(00)30008-x

Cited by 25 publications

(44 citation statements)

References 295 publications

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“…Additional experiments, in which different levels of specific Cx isoforms are compared in the absence of other connexins, will now be required unambiguously to establish the relative contributions to this fine tuning of the amount of each Cx isoform, on the one hand, and of its specific conductance and permeability characteristics, on the other. Addressing this important question might help us to identify the still-elusive gap-junction-permeant signals that influence insulin secretion (Meda and Spray, 2000;Serre-Beinier et al, 2003). As a first approach to this central issue, we have recently shown an essential role of Cx36 channels in synchronizing stimulus-induced Ca 2+ oscillations between the insulinproducing cells of the MIN6 line (Calabrese et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

“…With the availability of these tools, several questions about the (patho)physiological function(s) of gap junction proteins (Meda and Spray, 2000) can now be taken to direct experimental testing in primary tissues. In this perspective, we document that appropriate levels of specific Cx isoforms selectively influence distinct aspects of insulin secretion of primary pancreatic β-cells.…”

Section: Discussionmentioning

confidence: 99%

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Lentivirus-mediated transduction of connexin cDNAs shows level- and isoform-specific alterations in insulin secretion of primary pancreaticβ-cells

Caton

Calabrese

Mas

et al. 2003

Journal of Cell Science

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secretagogues similarly to controls. By contrast, pseudoislets made by cells expressing connexin32, a connexin exogenous to pancreatic islets, or over-expressing connexin36, the endogenous islet connexin, featured a marked decrease in the secretory response to glucose. The data show: (1) that lentiviral vectors allow stable modulation of various connexin in primary, nonproliferating cells; (2) that specific connexin isoforms affect insulin secretion differently; and (3) that adequate levels of coupling via connexin36 channels are required for proper β-cell function.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Lentivirus-mediated transduction of connexin cDNAs shows level- and isoform-specific alterations in insulin secretion of primary pancreaticβ-cells

Caton

Calabrese

Mas

et al. 2003

Journal of Cell Science

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“…These proteins differ in vertebrate and invertebrate species (134,167,291) and are expressed in most cell types, with few exceptions (291,343,347,460). There is no longer any question that vertebrate channels that mediate the cytosolic exchanges of cytosolic molecules at gap junctions are made by various combinations of different connexin (Cx) proteins (200,201,(211)(212)(213)316).…”

Section: Connexins Innexins and Pannexinsmentioning

confidence: 99%

“…Connexins form the electrical synapses, i.e., the sites where current-carrying ions allow for bidirectional neuronal interaction (24,54,55,347,(493)(494)(495). This electrical coupling, which is particularly frequent among the interneurons of several CNS regions during prenatal and early postnatal life, helps synchronize firing and ␥ oscillations, across neuronal and glial populations (24,154).…”

Section: Neural Synchronizationmentioning

confidence: 99%

Connexins: Key Mediators of Endocrine Function

Bosco

Haefliger

Meda

2011

Physiological Reviews

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158

185

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The appearance of multicellular organisms imposed the development of several mechanisms for cell-to-cell communication, whereby different types of cells coordinate their function. Some of these mechanisms depend on the intercellular diffusion of signal molecules in the extracellular spaces, whereas others require cell-to-cell contact. Among the latter mechanisms, those provided by the proteins of the connexin family are widespread in most tissues. Connexin signaling is achieved via direct exchanges of cytosolic molecules between adjacent cells at gap junctions, for cell-to-cell coupling, and possibly also involves the formation of membrane “hemi-channels,” for the extracellular release of cytosolic signals, direct interactions between connexins and other cell proteins, and coordinated influence on the expression of multiple genes. Connexin signaling appears to be an obligatory attribute of all multicellular exocrine and endocrine glands. Specifically, the experimental evidence we review here points to a direct participation of the Cx36 isoform in the function of the insulin-producing β-cells of the endocrine pancreas, and of the Cx40 isoform in the function of the renin-producing juxtaglomerular epithelioid cells of the kidney cortex.

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“…Channels located at gap junctions represent one way in which vertebrate cells communicate (1)(2)(3), by sharing ions, second messengers, small metabolites, and other signaling molecules (4,5). This type of intercellular communication permits coordinated cellular activity, including secretion (6)(7)(8)(9)(10)(11)(12)(13), by allowing cells to review the functional state of their neighbors, a critical feature for the homeostasis of multicellular systems (14).…”

Section: Introductionmentioning

confidence: 99%

Connexin43-dependent mechanism modulates renin secretion and hypertension

Haefliger¹

2006

Journal of Clinical Investigation

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To investigate the function of Cx43 during hypertension, we studied the mouse line Cx43KI32 (KI32), in which the coding region of Cx32 replaces that of Cx43. Within the kidneys of homozygous KI32 mice, Cx32 was expressed in cortical and medullary tubules, as well as in some extra-and intraglomerular vessels, i.e., at sites where Cx32 and Cx43 are found in WT mice. Under such conditions, renin expression was much reduced compared with that observed in the kidneys of WT and heterozygous KI32 littermates. After exposure to a high-salt diet, all mice retained a normal blood pressure. However, whereas the levels of renin were significantly reduced in the kidneys of WT and heterozygous KI32 mice, reaching levels comparable to those observed in homozygous littermates, they were not further affected in the latter animals. Four weeks after the clipping of a renal artery (the 2-kidney, 1-clip [2K1C] model), 2K1C WT and heterozygous mice showed an increase in blood pressure and in the circulating levels of renin, whereas 2K1C homozygous littermates remained normotensive and showed unchanged plasma renin activity. Hypertensive, but not normotensive, mice also developed cardiac hypertrophy. The data indicate that replacement of Cx43 by Cx32 is associated with decreased expression and secretion of renin, thus preventing the renin-dependent hypertension that is normally induced in the 2K1C model.

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Gap junction function

Cited by 25 publications

References 295 publications

Lentivirus-mediated transduction of connexin cDNAs shows level- and isoform-specific alterations in insulin secretion of primary pancreaticβ-cells

Lentivirus-mediated transduction of connexin cDNAs shows level- and isoform-specific alterations in insulin secretion of primary pancreaticβ-cells

Connexins: Key Mediators of Endocrine Function

Connexin43-dependent mechanism modulates renin secretion and hypertension

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