TY - JOUR
T1 - Protein Kinase C recognition sites in the cytoplasmic domain of Endothelin Converting Enzyme-1c
AU - Kuruppu, DM Sanjaya
AU - Tochon-Danguy, Nathalie
AU - Smith, Alexander Ian
PY - 2012
Y1 - 2012
N2 - 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
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
UR - http://www.sciencedirect.com/science/article/pii/S0006291X12018633
UR - https://www.scopus.com/pages/publications/84867867194
U2 - 10.1016/j.bbrc.2012.09.105
DO - 10.1016/j.bbrc.2012.09.105
M3 - Article
SN - 0006-291X
VL - 427
SP - 606
EP - 610
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -