{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,9]],"date-time":"2026-07-09T02:19:07Z","timestamp":1783563547922,"version":"3.55.0"},"reference-count":57,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2003,1,1]],"date-time":"2003-01-01T00:00:00Z","timestamp":1041379200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[2003,1]]},"abstract":"<jats:p>Angiotensin II (Ang II) receptor subtype 1, AT1, is expressed by the rat thyroid. A relationship between thyroid function and several components of the renin\u2010angiotensin system has also been established, but the Ang II cellular effects in thyrocytes and its transduction signalling remain undefined. The aim of the present paper was to investigate the modulation of the activity of the Na<jats:sup>+<\/jats:sup>\u2010K<jats:sup>+<\/jats:sup>ATPase by Ang II and its intracellular transduction pathway in PC\u2010Cl3 cells, an established epithelial cell line derived from rat thyroid. Here we have demonstrated, by RT\u2010PCR analysis, the expression of mRNA for the Ang II AT1 receptor in PC\u2010Cl3 cells; mRNA for the Ang II AT2 receptor was not detected. Ang II was not able to affect the intracellular Ca<jats:sup>2+<\/jats:sup> concentration in fura\u20102\u2010loaded cells, but it stimulated the translocation from the cytosol to the plasma membrane of atypical protein kinase C\u2010zeta (PKC\u2010\u03b6) and \u2010iota (PKC\u2010\u03b9) isoforms with subsequent phosphorylation of the extracellular signal\u2010regulated kinases 1 and 2 (ERK1 and 2). Translocated atypical PKCs displayed temporally different activations, the activation of PKC\u2010\u03b6 being the fastest. PC\u2010Cl3 cells stimulated with increasing Ang II concentrations showed dose\u2010 and time\u2010dependent activation of the Na<jats:sup>+<\/jats:sup>\u2010K<jats:sup>+<\/jats:sup>ATPase activity, which paralleled the PKC\u2010\u03b6 translocation time course. Na<jats:sup>+<\/jats:sup>\u2010K<jats:sup>+<\/jats:sup>ATPase activity modulation was dependent on PKC activation since the PKC antagonist staurosporine abolished the stimulatory effect of Ang II. The inhibition of the ERK kinases 1 and 2 (MEK1 and 2) by PD098059 (2\u2032\u2010amino\u20103\u2032\u2010methoxyflavone) failed to block the effect of Ang II on the Na<jats:sup>+<\/jats:sup>\u2010K<jats:sup>+<\/jats:sup>ATPase activity. In conclusion, our results suggest that Ang II modulates Na<jats:sup>+<\/jats:sup>\u2010K<jats:sup>+<\/jats:sup>ATPase activity in PC\u2010Cl3 cells through the AT1 receptor via activation of atypical PKC\u2010\u03b6 while the Ang II\u2010activated PKC\u2010\u03b6 appears to have other as yet unknown functions.<\/jats:p>","DOI":"10.1113\/jphysiol.2002.027466","type":"journal-article","created":{"date-parts":[[2003,1,15]],"date-time":"2003-01-15T01:22:42Z","timestamp":1042593762000},"page":"461-470","source":"Crossref","is-referenced-by-count":16,"title":["Angiotensin II AT1 receptor stimulates Na<sup>+<\/sup>\u2013k<sup>+<\/sup>atpase activity through a pathway involving pkc\u2010\u03b6 in rat thyroid cells"],"prefix":"10.1113","volume":"546","author":[{"given":"S.","family":"Marsigliante","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"A.","family":"Muscella","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. 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