Role of estrogenic compounds (diethylstibestrol, 17β-estradiol, and bisphenol A) in the phosphorylation of substrate by protein kinase Cα
✍ Scribed by Jeong-Hun Kang; Takuro Niidome; Yoshiki Katayama
- Publisher
- John Wiley and Sons
- Year
- 2009
- Tongue
- English
- Weight
- 116 KB
- Volume
- 23
- Category
- Article
- ISSN
- 1095-6670
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✦ Synopsis
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 Ca^2+^ or PS and Ca^2+^ after adding E2, DES, and BPA. However, no change in phosphorylation ratios was found in the presence of DAG and 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. © 2009 Wiley Periodicals, Inc. J Biochem Mol Toxicol 23:318–323, 2009; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/jbt.20294