<oai_dc:dc xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:oai_dc="http://www.openarchives.org/OAI/2.0/oai_dc/" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://www.openarchives.org/OAI/2.0/oai_dc/ http://www.openarchives.org/OAI/2.0/oai_dc.xsd">
  <dc:creator>Calabrese A</dc:creator>
  <dc:creator>Zhang M</dc:creator>
  <dc:creator>Serre-Beinier V</dc:creator>
  <dc:creator>Caton D</dc:creator>
  <dc:creator>Mas C</dc:creator>
  <dc:creator>Satin LS</dc:creator>
  <dc:creator>Meda P</dc:creator>
  <dc:date>2003</dc:date>
  <dc:description xmlns:ns0="xml" ns0:lang="en">Cx36 is the predominant connexin isoform expressed by pancreatic beta-cells. However, little is known about the role of this protein in the functioning of insulin-secreting cells. To address this question, we searched for a cell line expressing Cx36 and having glucose-induced insulin secretion comparable to that of primary beta-cells. By evaluating Cx36 expression in MIN6, betaTC3, RIN2A, INS1, and HIT cell lines, which differ in their sensitivity to glucose, we found that wild-type MIN6 cells fit these requirements. Therefore, we stably transfected MIN6 cells with a cDNA coding for a Cx36 antisense sequence to study the role of Cx36 in these cells. Independent clones of MIN6 cells were obtained that had a markedly reduced Cx36 expression. Loss of Cx36 decreased functional gap junctional conductance in these clones. This alteration impaired the synchronization of glucose-induced [Ca(2+)](i) oscillations and insulin secretion in response to glucose, to secretagogues that increase [cAMP](i), and to depolarizing conditions. These data provide the first evidence that Cx36-made channels 1) mediate functional coupling in MIN6 cells, 2) provide for synchronous [Ca(2+)](i) oscillations, and 3) are necessary for proper insulin secretion in response to metabolizable and nonmetabolizable secretagogues.</dc:description>
  <dc:format>application/pdf</dc:format>
  <dc:identifier>https://sonar.rero.ch/global/documents/5307</dc:identifier>
  <dc:language>eng</dc:language>
  <dc:relation>info:eu-repo/semantics/altIdentifier/doi/10.2337/diabetes.52.2.417</dc:relation>
  <dc:relation>info:eu-repo/semantics/altIdentifier/pmid/12540616</dc:relation>
  <dc:rights>info:eu-repo/semantics/openAccess</dc:rights>
  <dc:source>Diabetes. - 2003</dc:source>
  <dc:subject xmlns:ns1="xml" ns1:lang="en">Amphotericin B</dc:subject>
  <dc:subject xmlns:ns2="xml" ns2:lang="en">Animals</dc:subject>
  <dc:subject xmlns:ns3="xml" ns3:lang="en">Base Sequence</dc:subject>
  <dc:subject xmlns:ns4="xml" ns4:lang="en">Calcium Signaling</dc:subject>
  <dc:subject xmlns:ns5="xml" ns5:lang="en">Cell Line</dc:subject>
  <dc:subject xmlns:ns6="xml" ns6:lang="en">Connexins</dc:subject>
  <dc:subject xmlns:ns7="xml" ns7:lang="en">DNA Primers</dc:subject>
  <dc:subject xmlns:ns8="xml" ns8:lang="en">Electric Conductivity</dc:subject>
  <dc:subject xmlns:ns9="xml" ns9:lang="en">Electrophysiology</dc:subject>
  <dc:subject xmlns:ns10="xml" ns10:lang="en">Gap Junctions</dc:subject>
  <dc:subject xmlns:ns11="xml" ns11:lang="en">Gene Expression Regulation</dc:subject>
  <dc:subject xmlns:ns12="xml" ns12:lang="en">Glucose</dc:subject>
  <dc:subject xmlns:ns13="xml" ns13:lang="en">Insulin</dc:subject>
  <dc:subject xmlns:ns14="xml" ns14:lang="en">Insulin Secretion</dc:subject>
  <dc:subject xmlns:ns15="xml" ns15:lang="en">Islets of Langerhans</dc:subject>
  <dc:subject xmlns:ns16="xml" ns16:lang="en">Reverse Transcriptase Polymerase Chain Reaction</dc:subject>
  <dc:title xmlns:ns17="xml" ns17:lang="en">Connexin 36 controls synchronization of Ca2+ oscillations and insulin secretion in MIN6 cells.</dc:title>
  <dc:type>http://purl.org/coar/resource_type/c_6501</dc:type>
</oai_dc:dc>
