Protein Kinase C recognition sites in the cytoplasmic domain of Endothelin Converting Enzyme-1c

DM Sanjaya Kuruppu, Nathalie Tochon-Danguy, Alexander Ian Smith

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Endothelin Converting Enzyme-1 (ECE-1) is essential for the production of the potent vasoconstrictor Endothelin-1 (ET-1). The activation of Protein Kinase C (PKC) by phorbol 12-myristate 13-acetate (PMA) can increase ECE-1 phosphorylation, which in turn promotes ECE-1c trafficking to the cell surface where ET-1 production occurs. This study has identified the specific residues in the N-terminal cytoplasmic tail of ECE-1c isoform that are phosphorylated upon the activation of PKC. Levels of phosphorylation are expressed as a phosphorylation in untreated CHO-K1 cells. We transfected CHO-K1 cells with wild type and mutant forms of ECE-1c (Ala(4)-ECE-1c, Ala(35)ECE-1c and Ala(4/35)ECE-1c) to confirm the involvement of Thr(4) and Ser(35) residues in PMA induced phosphorylation of ECE-1c. Phosphorylation of wild type ECE-1c increased in response to PMA treatment (150+/-13 , unpaired t-test, P
Original languageEnglish
Pages (from-to)606 - 610
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume427
Issue number3
DOIs
Publication statusPublished - 2012

Cite this

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title = "Protein Kinase C recognition sites in the cytoplasmic domain of Endothelin Converting Enzyme-1c",
abstract = "Endothelin Converting Enzyme-1 (ECE-1) is essential for the production of the potent vasoconstrictor Endothelin-1 (ET-1). The activation of Protein Kinase C (PKC) by phorbol 12-myristate 13-acetate (PMA) can increase ECE-1 phosphorylation, which in turn promotes ECE-1c trafficking to the cell surface where ET-1 production occurs. This study has identified the specific residues in the N-terminal cytoplasmic tail of ECE-1c isoform that are phosphorylated upon the activation of PKC. Levels of phosphorylation are expressed as a phosphorylation in untreated CHO-K1 cells. We transfected CHO-K1 cells with wild type and mutant forms of ECE-1c (Ala(4)-ECE-1c, Ala(35)ECE-1c and Ala(4/35)ECE-1c) to confirm the involvement of Thr(4) and Ser(35) residues in PMA induced phosphorylation of ECE-1c. Phosphorylation of wild type ECE-1c increased in response to PMA treatment (150+/-13 , unpaired t-test, P",
author = "Kuruppu, {DM Sanjaya} and Nathalie Tochon-Danguy and Smith, {Alexander Ian}",
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doi = "10.1016/j.bbrc.2012.09.105",
language = "English",
volume = "427",
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journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
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Protein Kinase C recognition sites in the cytoplasmic domain of Endothelin Converting Enzyme-1c. / Kuruppu, DM Sanjaya; Tochon-Danguy, Nathalie; Smith, Alexander Ian.

In: Biochemical and Biophysical Research Communications, Vol. 427, No. 3, 2012, p. 606 - 610.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Protein Kinase C recognition sites in the cytoplasmic domain of Endothelin Converting Enzyme-1c

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AU - Tochon-Danguy, Nathalie

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PY - 2012

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AB - Endothelin Converting Enzyme-1 (ECE-1) is essential for the production of the potent vasoconstrictor Endothelin-1 (ET-1). The activation of Protein Kinase C (PKC) by phorbol 12-myristate 13-acetate (PMA) can increase ECE-1 phosphorylation, which in turn promotes ECE-1c trafficking to the cell surface where ET-1 production occurs. This study has identified the specific residues in the N-terminal cytoplasmic tail of ECE-1c isoform that are phosphorylated upon the activation of PKC. Levels of phosphorylation are expressed as a phosphorylation in untreated CHO-K1 cells. We transfected CHO-K1 cells with wild type and mutant forms of ECE-1c (Ala(4)-ECE-1c, Ala(35)ECE-1c and Ala(4/35)ECE-1c) to confirm the involvement of Thr(4) and Ser(35) residues in PMA induced phosphorylation of ECE-1c. Phosphorylation of wild type ECE-1c increased in response to PMA treatment (150+/-13 , unpaired t-test, P

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