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Sensitization of regulated exocytosis by protein kinase C
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Proceedings of the National Academy of Sciences, 99, 2002, 26, S. 17055-17059 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Zhu, Hongliang Hille, Bertil Xu, Tao Zhu, Hongliang Hille, Bertil Xu, Tao |
|---|---|
| author |
Zhu, Hongliang Hille, Bertil Xu, Tao |
| spellingShingle |
Zhu, Hongliang Hille, Bertil Xu, Tao Proceedings of the National Academy of Sciences Sensitization of regulated exocytosis by protein kinase C Multidisciplinary |
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zhu, hongliang |
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Zhu, Hongliang Hille, Bertil Xu, Tao 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.232588899 <jats:p> Activation of protein kinase C (PKC) increases vesicular secretion in many cell types. We determined the calcium dependence of secretion and the size of the readily releasable pool of secretory granules in pituitary gonadotropes by photorelease of caged-calcium. The calcium affinity for exocytosis was roughly doubled by activation of PKC by a phorbol ester, whereas the size of the readily releasable pool was not greatly increased. The effect was due to activation of PKC, because it was blocked by a PKC inhibitor and was not mimicked by an inactive phorbol ester analogue. A similar increase in calcium sensitivity was induced by preincubation with gonadotropin-releasing hormone, the physiological releasing hormone. These findings provide direct evidence for physiological regulation of secretion by enhancement of Ca <jats:sup>2+</jats:sup> -sensing steps. Because exocytosis depends on the third- to fourth-power of intracellular free Ca <jats:sup>2+</jats:sup> concentration, this mechanism ensures a powerful up-regulation of hormone release and may explain how PKC can stimulate exocytosis without an increase of Ca <jats:sup>2+</jats:sup> above the resting level. </jats:p> Sensitization of regulated exocytosis by protein kinase C Proceedings of the National Academy of Sciences |
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| title |
Sensitization of regulated exocytosis by protein kinase C |
| title_unstemmed |
Sensitization of regulated exocytosis by protein kinase C |
| title_full |
Sensitization of regulated exocytosis by protein kinase C |
| title_fullStr |
Sensitization of regulated exocytosis by protein kinase C |
| title_full_unstemmed |
Sensitization of regulated exocytosis by protein kinase C |
| title_short |
Sensitization of regulated exocytosis by protein kinase C |
| title_sort |
sensitization of regulated exocytosis by protein kinase c |
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Multidisciplinary |
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http://dx.doi.org/10.1073/pnas.232588899 |
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2002 |
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17055-17059 |
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<jats:p>
Activation of protein kinase C (PKC) increases vesicular secretion in many cell types. We determined the calcium dependence of secretion and the size of the readily releasable pool of secretory granules in pituitary gonadotropes by photorelease of caged-calcium. The calcium affinity for exocytosis was roughly doubled by activation of PKC by a phorbol ester, whereas the size of the readily releasable pool was not greatly increased. The effect was due to activation of PKC, because it was blocked by a PKC inhibitor and was not mimicked by an inactive phorbol ester analogue. A similar increase in calcium sensitivity was induced by preincubation with gonadotropin-releasing hormone, the physiological releasing hormone. These findings provide direct evidence for physiological regulation of secretion by enhancement of Ca
<jats:sup>2+</jats:sup>
-sensing steps. Because exocytosis depends on the third- to fourth-power of intracellular free Ca
<jats:sup>2+</jats:sup>
concentration, this mechanism ensures a powerful up-regulation of hormone release and may explain how PKC can stimulate exocytosis without an increase of Ca
<jats:sup>2+</jats:sup>
above the resting level.
</jats:p> |
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| author | Zhu, Hongliang, Hille, Bertil, Xu, Tao |
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| description | <jats:p> Activation of protein kinase C (PKC) increases vesicular secretion in many cell types. We determined the calcium dependence of secretion and the size of the readily releasable pool of secretory granules in pituitary gonadotropes by photorelease of caged-calcium. The calcium affinity for exocytosis was roughly doubled by activation of PKC by a phorbol ester, whereas the size of the readily releasable pool was not greatly increased. The effect was due to activation of PKC, because it was blocked by a PKC inhibitor and was not mimicked by an inactive phorbol ester analogue. A similar increase in calcium sensitivity was induced by preincubation with gonadotropin-releasing hormone, the physiological releasing hormone. These findings provide direct evidence for physiological regulation of secretion by enhancement of Ca <jats:sup>2+</jats:sup> -sensing steps. Because exocytosis depends on the third- to fourth-power of intracellular free Ca <jats:sup>2+</jats:sup> concentration, this mechanism ensures a powerful up-regulation of hormone release and may explain how PKC can stimulate exocytosis without an increase of Ca <jats:sup>2+</jats:sup> above the resting level. </jats:p> |
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| spelling | Zhu, Hongliang Hille, Bertil Xu, Tao 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.232588899 <jats:p> Activation of protein kinase C (PKC) increases vesicular secretion in many cell types. We determined the calcium dependence of secretion and the size of the readily releasable pool of secretory granules in pituitary gonadotropes by photorelease of caged-calcium. The calcium affinity for exocytosis was roughly doubled by activation of PKC by a phorbol ester, whereas the size of the readily releasable pool was not greatly increased. The effect was due to activation of PKC, because it was blocked by a PKC inhibitor and was not mimicked by an inactive phorbol ester analogue. A similar increase in calcium sensitivity was induced by preincubation with gonadotropin-releasing hormone, the physiological releasing hormone. These findings provide direct evidence for physiological regulation of secretion by enhancement of Ca <jats:sup>2+</jats:sup> -sensing steps. Because exocytosis depends on the third- to fourth-power of intracellular free Ca <jats:sup>2+</jats:sup> concentration, this mechanism ensures a powerful up-regulation of hormone release and may explain how PKC can stimulate exocytosis without an increase of Ca <jats:sup>2+</jats:sup> above the resting level. </jats:p> Sensitization of regulated exocytosis by protein kinase C Proceedings of the National Academy of Sciences |
| spellingShingle | Zhu, Hongliang, Hille, Bertil, Xu, Tao, Proceedings of the National Academy of Sciences, Sensitization of regulated exocytosis by protein kinase C, Multidisciplinary |
| title | Sensitization of regulated exocytosis by protein kinase C |
| title_full | Sensitization of regulated exocytosis by protein kinase C |
| title_fullStr | Sensitization of regulated exocytosis by protein kinase C |
| title_full_unstemmed | Sensitization of regulated exocytosis by protein kinase C |
| title_short | Sensitization of regulated exocytosis by protein kinase C |
| title_sort | sensitization of regulated exocytosis by protein kinase c |
| title_unstemmed | Sensitization of regulated exocytosis by protein kinase C |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.232588899 |