Protein Kinase A Subunit α Catalytic and A Kinase Anchoring Protein 79 in Human Placental Mitochondria.

Q3 Biochemistry, Genetics and Molecular Biology Open Biochemistry Journal Pub Date : 2012-01-01 Epub Date: 2012-04-11 DOI:10.2174/1874091X01206010023
Maggie Pui Chi Ma, Murray Thomson
{"title":"Protein Kinase A Subunit α Catalytic and A Kinase Anchoring Protein 79 in Human Placental Mitochondria.","authors":"Maggie Pui Chi Ma,&nbsp;Murray Thomson","doi":"10.2174/1874091X01206010023","DOIUrl":null,"url":null,"abstract":"<p><p>Components of protein phosphorylation signalling systems have been discovered in mitochondria and it has been proposed that these molecules modulate processes including oxidative phosphorylation, apoptosis and steroidogenesis. We used electrophoresis and Western blots probed with specific antibodies to protein kinase A α catalytic subunit (PKAα Cat) and A kinase anchoring protein of approximately 79 kDa molecular weight (AKAP79) to demonstrate the presence of these two proteins in human placental mitochondria. Heavy mitochondria characteristic of cytotrophoblast were separated from light mitochondria characteristic of syncytiotrophoblast by centrifugation. PKAα Cat and AKAP79 were present in both heavy and light mitochondria with no significant difference in concentration. Sucrose density gradient separation of submitochondrial fractions indicated PKAα Cat is located predominantly in the outer membrane whereas AKAP79 is present mainly in the contact site fractions. These data indicate that PKAα Cat is present in the cytoplasm, nucleus and mitochondria of placental cells. AKAP79 is also present in human placental mitochondria but there may be anchoring proteins other than AKAP79 responsible for fixing PKA to the outer membrane. PKA may play roles in mitochondrial protein phosphorylation systems in both cytotrophoblast and syncytiotrophoblast.</p>","PeriodicalId":38958,"journal":{"name":"Open Biochemistry Journal","volume":" ","pages":"23-30"},"PeriodicalIF":0.0000,"publicationDate":"2012-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/03/82/TOBIOCJ-6-23.PMC3330370.pdf","citationCount":"10","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Open Biochemistry Journal","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.2174/1874091X01206010023","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2012/4/11 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 10

Abstract

Components of protein phosphorylation signalling systems have been discovered in mitochondria and it has been proposed that these molecules modulate processes including oxidative phosphorylation, apoptosis and steroidogenesis. We used electrophoresis and Western blots probed with specific antibodies to protein kinase A α catalytic subunit (PKAα Cat) and A kinase anchoring protein of approximately 79 kDa molecular weight (AKAP79) to demonstrate the presence of these two proteins in human placental mitochondria. Heavy mitochondria characteristic of cytotrophoblast were separated from light mitochondria characteristic of syncytiotrophoblast by centrifugation. PKAα Cat and AKAP79 were present in both heavy and light mitochondria with no significant difference in concentration. Sucrose density gradient separation of submitochondrial fractions indicated PKAα Cat is located predominantly in the outer membrane whereas AKAP79 is present mainly in the contact site fractions. These data indicate that PKAα Cat is present in the cytoplasm, nucleus and mitochondria of placental cells. AKAP79 is also present in human placental mitochondria but there may be anchoring proteins other than AKAP79 responsible for fixing PKA to the outer membrane. PKA may play roles in mitochondrial protein phosphorylation systems in both cytotrophoblast and syncytiotrophoblast.

Abstract Image

Abstract Image

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
人胎盘线粒体蛋白激酶A亚基α催化和A激酶锚定蛋白79。
在线粒体中发现了蛋白质磷酸化信号系统的组成部分,并提出这些分子调节包括氧化磷酸化、细胞凋亡和甾体生成在内的过程。我们使用蛋白激酶Aα催化亚基(PKAα Cat)和分子量约为79 kDa的激酶锚定蛋白(AKAP79)特异性抗体进行电泳和Western blots检测,证实这两种蛋白存在于人胎盘线粒体中。用离心分离法分离出具有细胞滋养层特征的重线粒体和具有合胞滋养层特征的轻线粒体。PKAα Cat和AKAP79均存在于重质线粒体和轻质线粒体中,但浓度差异不显著。线粒体亚区蔗糖密度梯度分离表明,PKAα Cat主要位于外膜,而AKAP79主要存在于接触部位。这些数据表明,PKAα Cat存在于胎盘细胞的细胞质、细胞核和线粒体中。AKAP79也存在于人类胎盘线粒体中,但除了AKAP79之外,可能还有其他锚定蛋白负责将PKA固定在外膜上。PKA可能在细胞滋养细胞和合胞滋养细胞线粒体蛋白磷酸化系统中发挥作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Open Biochemistry Journal
Open Biochemistry Journal Biochemistry, Genetics and Molecular Biology-Biochemistry, Genetics and Molecular Biology (all)
CiteScore
1.50
自引率
0.00%
发文量
5
期刊最新文献
The Activity of α-glucosidase Inhibition of Pediococcus Acidilactici BAMA 4 Isolated from “Naniura” Traditional Foods from North Sumatera, Indonesia Nitric oxide and its metabolites in the critical phase of illness: rapid biomarkers in the making. Protein Kinase A Subunit α Catalytic and A Kinase Anchoring Protein 79 in Human Placental Mitochondria. High G+C Content of Herpes Simplex Virus DNA: Proposed Role in Protection Against Retrotransposon Insertion. Increased endogenous nitric oxide release by iron chelation and purinergic activation in the rat carotid body.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1