{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,26]],"date-time":"2025-09-26T22:16:01Z","timestamp":1758924961521,"version":"3.37.3"},"reference-count":31,"publisher":"Oxford University Press (OUP)","issue":"6","license":[{"start":{"date-parts":[[1992,6,1]],"date-time":"1992-06-01T00:00:00Z","timestamp":707356800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/501100007155","name":"Medical Research Council of Canada","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100007155","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[1992,6,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The response of the parathyroid gland to low Ca2+ may be mediated in part by protein kinase C (PKC). We assessed the effect of two PKC activators, SC-9 and SC-10, and one PKC inhibitor, H-7, on Ca2+-regulated PTH release and degradation in primary cultures of bovine parathyroid cells. Both SC-9 and SC-10 stimulated PTH release, compared to high Ca2+ alone, in parathyroid cells incubated in high Ca2+, with maximal PTH release of at least twofold occurring at a concentration of either activator of 10 nM (p &amp;lt; 0.05). We have previously shown that another PKC activator, PMA, not only enhances PTH release in the presence of high Ca2+ but suppresses low Ca2+-stimulated PTH secretion. In the present study, neither SC-9 nor SC-10 caused a comparable suppression of PTH release at low Ca2+. However, the PKC inhibitor, H-7 (1 \u03bcM), blocked low Ca2+-stimulated (compared to the low Ca2+ control) PTH secretion by approximately 50% (p &amp;lt; 0.01) and did not affect high Ca2+ suppression of PTH secretion. H-7 (1 \u03bcM) was able to oppose the stimulation of PTH release by the PKC activators SC-9, SC-10, and PMA at high Ca2+ and negated the PTH release-inhibiting effect of PMA at low Ca2+. Culture medium from these experiments was subjected to reversed-phase HPLC and the eluted fractions analyzed by RIA for the presence of intact and C-terminal fragments of PTH. The release of C-terminal fragments of PTH, when expressed as a percentage of total (fragment plus intact) PTH released, was greatest at high Ca2+ (\u223c80%) and considerably less at low Ca2+ (\u223c57%). Although the relative proportion of intact PTH released was increased when SC-9 and SC-10 stimulated PTH secretion at high Ca2+, analysis of variance suggests that the level of extracellular Ca2+ was the major determinant of PTH degradation to C-terminal fragments. At low Ca2+, H-7 blocked the previously reported ability of PMA to suppress PTH secretion but did not block the ability of PMA to enhance PTH degradation. These results indicate that (1) PKC activation is an important component of low Ca2+-stimulated PTH release, (2) the Ca2+ effect on PTH degradation may not be entirely mediated by PKC, and (3) the PMA effect on PTH degradation is not mediated through PKC.<\/jats:p>","DOI":"10.1002\/jbmr.5650070611","type":"journal-article","created":{"date-parts":[[2010,2,3]],"date-time":"2010-02-03T17:08:01Z","timestamp":1265216881000},"page":"667-674","source":"Crossref","is-referenced-by-count":8,"title":["Activation and inhibition of protein kinase c in cultured bovine parathyroid cells: Effect on the release of c-terminal fragments of parathyroid hormone"],"prefix":"10.1093","volume":"7","author":[{"given":"Patricia H. (Wood)","family":"Watson","sequence":"first","affiliation":[{"name":"Division of Endocrinology and Metabolism, Department of Medicine, Foothills Hospital and the University of Calgary, Alberta, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shane T.","family":"Mortimer","sequence":"additional","affiliation":[{"name":"Division of Endocrinology and Metabolism, Department of Medicine, Foothills Hospital and the University of Calgary, Alberta, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Karen E.","family":"Tanguay","sequence":"additional","affiliation":[{"name":"Division of Endocrinology and Metabolism, Department of Medicine, Foothills Hospital and the University of Calgary, Alberta, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"David A.","family":"Hanley","sequence":"additional","affiliation":[{"name":"Division of Endocrinology and Metabolism, Department of Medicine, Foothills Hospital and the University of Calgary, Alberta, Canada"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[1992,6,1]]},"reference":[{"issue":"4","key":"2024013112173993700_bib1","first-page":"F377","article-title":"Stimulation of renin release in perfused kidney by low calcium and high magnesium.","volume":"232","author":"Fray","year":"1977","journal-title":"Am J Physiol"},{"key":"2024013112173993700_bib2","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1210\/endo-97-2-431","article-title":"Calcium-dependent intracellular degradation of parathyroid hormone: A possible mechanism for the regulation of hormone stores.","volume":"97","author":"Habener","year":"1975","journal-title":"Endocrinology"},{"key":"2024013112173993700_bib3","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1210\/edrv-2-1-1","article-title":"The biosynthesis, intracellular processing and secretion of 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