Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells.

Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells. Research Abstract Details 

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Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells. Abstract Text:

S Iwasaki,M Kataoka,M Sekiguchi,Y Shimazaki,K Sato,M Takahashi,

Phorbol ester treatment induces the phosphorylation of SNAP-25 at Ser(187) and the potentiation of Ca(2+)-induced dopamine (DA) and acetylcholine (Ach) release from PC12 cells. In order to evaluate the functional consequences of phosphorylation, quantitative analysis was carried out using an anti-phosphopeptide antibody that specifically recognizes SNAP-25 phosphorylated at Ser(187). DA and ACh release, assayed in low-K(+) as well as high-K(+) solution, increased by treating the cells with phorbol-12-myristate-13-acetate (PMA); however, the stimulation of high-K(+)-dependent release occurred at lower concentrations and with shorter exposures to PMA than that of the basal release in low-K(+)-solution. The PMA-induced phosphorylation of SNAP-25 did not correlate with the potentiation of high-K(+)-dependent neurotransmitter release. The potentiation of high-K(+)-dependent DA release by phorbol 12,13-diacetate (PDA), a water soluble phorbol ester, almost completely disappeared within 1 min after washing PDA in the presence of okadaic acid, conditions under which the phosphorylation of SNAP-25 persisted for at least 15 min. PMA-induced phosphorylation of SNAP-25 was inhibited by staurosporine, however, the potentiation of high-K(+)-dependent DA release was suppressed only partially. These results indicate that protein kinase activation does not account for a large fraction of the phorbol ester-induced potentiation of depolarization-dependent neurotransmitter release from PC12 cells.

Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells. Publishing Authors By Initials

S Iwasaki,M Kataoka,M Sekiguchi,Y Shimazaki,K Sato,M Takahashi,

For similar proteins: membrane proteins: membrane fusion proteins: snare proteins: q-snare proteins: qb-snare proteins: synaptosomal-associated protein 25 research abstracts see: proteins: membrane proteins: membrane fusion proteins: snare proteins: q-snare proteins: qb-snare proteins: synaptosomal-associated protein 25 research

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Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 128

Page Numbers: 407-14

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Sep

YEAR: 2000

Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells. Keywords Mesh Terms:

KEYWORDS: Synaptosomal-Associated Protein 25

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells. Information

Substance Name: Protein Kinase C

Registry Number: EC 2.7.11.13

Grant and Affiliation Information for Two distinct mechanisms underlie the stimulation of neurotransmitter release by phorbol esters in clonal rat pheochromocytoma PC12 cells.

AFFILIATION: Department of Life Sciences (Biology), Graduate School of Arts and Sciences, The University of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902, Japan.

Country: JAPAN

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MEDLINETA: J Biochem

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