Role of estrogenic compounds (diethylstibestrol, 17β-estradiol, and bisphenol A) in the phosphorylation of substrate by protein kinase Cα

Jeong Hun Kang, Takuro Niidome, Yoshiki Katayama

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2 Citations (Scopus)

Abstract

Estrogenic compounds can activate protein kinase C (PKC), which is a calcium and phospholipid-dependent serine/threonine kinase. In the present study, we investigated the role of 17β-estradiol (E2), diethylstibestrol (DES), and bisphenol A (BPA) in the phosphorylation of substrate by PKCα using the matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The level of phosphorylated peptide was low in the absence of phosphatidylserine (PS). Moreover, reduction of phosphorylation ratios was identified in the presence of diacylglycerol (DAG) and Ca2+ or PS and Ca2+ after adding E2, DES, and BPA. However, no change in phosphorylation ratios was found in the presence of DAGand PS. Addition of E2, DES, and BPA also had no influence on the phosphorylation reaction of substrate by cell or tissue lysate samples. Our study suggests that E2, DES, and BPA can bind to the C2 domain of PKCα but have no effects on the phosphorylation reaction of substrates in the presence of DAG and PS.

Original languageEnglish
Pages (from-to)318-323
Number of pages6
JournalJournal of Biochemical and Molecular Toxicology
Volume23
Issue number5
DOIs
Publication statusPublished - Sep 1 2009

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Phosphorylation
Protein Kinase C
Phosphatidylserines
Estradiol
Estrogens
Substrates
Diglycerides
Protein-Serine-Threonine Kinases
Ionization
Mass spectrometry
Desorption
Mass Spectrometry
Phospholipids
Lasers
compound 17
bisphenol A
Tissue
Calcium
Peptides

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Toxicology
  • Health, Toxicology and Mutagenesis

Cite this

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title = "Role of estrogenic compounds (diethylstibestrol, 17β-estradiol, and bisphenol A) in the phosphorylation of substrate by protein kinase Cα",
abstract = "Estrogenic compounds can activate protein kinase C (PKC), which is a calcium and phospholipid-dependent serine/threonine kinase. In the present study, we investigated the role of 17β-estradiol (E2), diethylstibestrol (DES), and bisphenol A (BPA) in the phosphorylation of substrate by PKCα using the matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The level of phosphorylated peptide was low in the absence of phosphatidylserine (PS). Moreover, reduction of phosphorylation ratios was identified in the presence of diacylglycerol (DAG) and Ca2+ or PS and Ca2+ after adding E2, DES, and BPA. However, no change in phosphorylation ratios was found in the presence of DAGand PS. Addition of E2, DES, and BPA also had no influence on the phosphorylation reaction of substrate by cell or tissue lysate samples. Our study suggests that E2, DES, and BPA can bind to the C2 domain of PKCα but have no effects on the phosphorylation reaction of substrates in the presence of DAG and PS.",
author = "Kang, {Jeong Hun} and Takuro Niidome and Yoshiki Katayama",
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T1 - Role of estrogenic compounds (diethylstibestrol, 17β-estradiol, and bisphenol A) in the phosphorylation of substrate by protein kinase Cα

AU - Kang, Jeong Hun

AU - Niidome, Takuro

AU - Katayama, Yoshiki

PY - 2009/9/1

Y1 - 2009/9/1

N2 - Estrogenic compounds can activate protein kinase C (PKC), which is a calcium and phospholipid-dependent serine/threonine kinase. In the present study, we investigated the role of 17β-estradiol (E2), diethylstibestrol (DES), and bisphenol A (BPA) in the phosphorylation of substrate by PKCα using the matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The level of phosphorylated peptide was low in the absence of phosphatidylserine (PS). Moreover, reduction of phosphorylation ratios was identified in the presence of diacylglycerol (DAG) and Ca2+ or PS and Ca2+ after adding E2, DES, and BPA. However, no change in phosphorylation ratios was found in the presence of DAGand PS. Addition of E2, DES, and BPA also had no influence on the phosphorylation reaction of substrate by cell or tissue lysate samples. Our study suggests that E2, DES, and BPA can bind to the C2 domain of PKCα but have no effects on the phosphorylation reaction of substrates in the presence of DAG and PS.

AB - Estrogenic compounds can activate protein kinase C (PKC), which is a calcium and phospholipid-dependent serine/threonine kinase. In the present study, we investigated the role of 17β-estradiol (E2), diethylstibestrol (DES), and bisphenol A (BPA) in the phosphorylation of substrate by PKCα using the matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The level of phosphorylated peptide was low in the absence of phosphatidylserine (PS). Moreover, reduction of phosphorylation ratios was identified in the presence of diacylglycerol (DAG) and Ca2+ or PS and Ca2+ after adding E2, DES, and BPA. However, no change in phosphorylation ratios was found in the presence of DAGand PS. Addition of E2, DES, and BPA also had no influence on the phosphorylation reaction of substrate by cell or tissue lysate samples. Our study suggests that E2, DES, and BPA can bind to the C2 domain of PKCα but have no effects on the phosphorylation reaction of substrates in the presence of DAG and PS.

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