Selective Changes in Protein Kinase C Isoforms and Phosphorylation of Endogenous Substrate Proteins in Rat Cerebral Cortex during Pre- and Postnatal Ethanol Exposure
The effect of pre- and postnatal ethanol exposure on protein kinase C (PKC) activity, immunochemical analysis of PKC α, βI, βII, γ, δ, ϵ, η, and ζ by isoform-specific antibodies, andin vitrophosphorylation of endogenous substrate proteins was investigated in rat cerebral cortex. The PKC activity was...
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| Veröffentlicht in: | Archives of biochemistry and biophysics 1998-08, Vol.356 (2), p.249-257 |
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| description | The effect of pre- and postnatal ethanol exposure on protein kinase C (PKC) activity, immunochemical analysis of PKC α, βI, βII, γ, δ, ϵ, η, and ζ by isoform-specific antibodies, andin vitrophosphorylation of endogenous substrate proteins was investigated in rat cerebral cortex. The PKC activity was increased throughout the development. However, the activity at the age of 8 days was significantly high in cytosolic and membrane fractions from ethanol-treated rats. Immunochemical analysis showed increased levels of PKC βI and βII at the age of 8 days, and a decrease in δ isoform at 8, 30, and 90 days of age. PKC isoforms α, γ, ϵ, and η showed no appreciable change in ethanol-treated rats. PKC ζ levels were high in the cytosolic fraction from ethanol-treated samples of 90 days age.In vitrophosphorylation of endogenous substrate proteins in the presence of Ca2+/phospholipid showed increased phosphorylation of selective membrane and cytosolic proteins with 87, 65, 50, 43, 36, and 29 kDa in ethanol-treated rats. The phosphorylation of these proteins decreased in the presence of staurosporine, which also supported PKC-mediated phosphorylation. Increased PKC activity, activation of βI and βII isoforms, decreased levels of δ isoform, and phosphorylation of selective substrate proteins in cerebral cortex due to alcohol exposure might be relevant in ethanol-induced central nervous system dysfunction and fetal alcohol syndrome. |
| doi_str_mv | 10.1006/abbi.1998.0773 |
| format | Article |
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The PKC activity was increased throughout the development. However, the activity at the age of 8 days was significantly high in cytosolic and membrane fractions from ethanol-treated rats. Immunochemical analysis showed increased levels of PKC βI and βII at the age of 8 days, and a decrease in δ isoform at 8, 30, and 90 days of age. PKC isoforms α, γ, ϵ, and η showed no appreciable change in ethanol-treated rats. PKC ζ levels were high in the cytosolic fraction from ethanol-treated samples of 90 days age.In vitrophosphorylation of endogenous substrate proteins in the presence of Ca2+/phospholipid showed increased phosphorylation of selective membrane and cytosolic proteins with 87, 65, 50, 43, 36, and 29 kDa in ethanol-treated rats. The phosphorylation of these proteins decreased in the presence of staurosporine, which also supported PKC-mediated phosphorylation. Increased PKC activity, activation of βI and βII isoforms, decreased levels of δ isoform, and phosphorylation of selective substrate proteins in cerebral cortex due to alcohol exposure might be relevant in ethanol-induced central nervous system dysfunction and fetal alcohol syndrome.</description><identifier>ISSN: 0003-9861</identifier><identifier>EISSN: 1096-0384</identifier><identifier>DOI: 10.1006/abbi.1998.0773</identifier><identifier>PMID: 9705215</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Administration, Oral ; Animals ; Animals, Newborn - growth & development ; Animals, Newborn - metabolism ; brain ; Cerebral Cortex - embryology ; Cerebral Cortex - enzymology ; Cerebral Cortex - growth & development ; development ; Enzyme Activation - drug effects ; ethanol ; Ethanol - administration & dosage ; Female ; Isoenzymes - drug effects ; Isoenzymes - metabolism ; Male ; Maternal-Fetal Exchange - drug effects ; Nerve Tissue Proteins - metabolism ; phosphorylation ; Phosphorylation - drug effects ; PKC isoforms ; Pregnancy ; Protein Kinase C - drug effects ; Protein Kinase C - metabolism ; Rats ; Rats, Wistar ; Substrate Specificity - drug effects</subject><ispartof>Archives of biochemistry and biophysics, 1998-08, Vol.356 (2), p.249-257</ispartof><rights>1998 Academic Press</rights><rights>Copyright 1998 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c339t-5c651573d94837dbdb08a1579fc16cd99e24de48319296d3d79297f4a86605d53</citedby><cites>FETCH-LOGICAL-c339t-5c651573d94837dbdb08a1579fc16cd99e24de48319296d3d79297f4a86605d53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/abbi.1998.0773$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9705215$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mahadev, Kalyankar</creatorcontrib><creatorcontrib>Vemuri, Mohan C.</creatorcontrib><title>Selective Changes in Protein Kinase C Isoforms and Phosphorylation of Endogenous Substrate Proteins in Rat Cerebral Cortex during Pre- and Postnatal Ethanol Exposure</title><title>Archives of biochemistry and biophysics</title><addtitle>Arch Biochem Biophys</addtitle><description>The effect of pre- and postnatal ethanol exposure on protein kinase C (PKC) activity, immunochemical analysis of PKC α, βI, βII, γ, δ, ϵ, η, and ζ by isoform-specific antibodies, andin vitrophosphorylation of endogenous substrate proteins was investigated in rat cerebral cortex. The PKC activity was increased throughout the development. However, the activity at the age of 8 days was significantly high in cytosolic and membrane fractions from ethanol-treated rats. Immunochemical analysis showed increased levels of PKC βI and βII at the age of 8 days, and a decrease in δ isoform at 8, 30, and 90 days of age. PKC isoforms α, γ, ϵ, and η showed no appreciable change in ethanol-treated rats. PKC ζ levels were high in the cytosolic fraction from ethanol-treated samples of 90 days age.In vitrophosphorylation of endogenous substrate proteins in the presence of Ca2+/phospholipid showed increased phosphorylation of selective membrane and cytosolic proteins with 87, 65, 50, 43, 36, and 29 kDa in ethanol-treated rats. The phosphorylation of these proteins decreased in the presence of staurosporine, which also supported PKC-mediated phosphorylation. Increased PKC activity, activation of βI and βII isoforms, decreased levels of δ isoform, and phosphorylation of selective substrate proteins in cerebral cortex due to alcohol exposure might be relevant in ethanol-induced central nervous system dysfunction and fetal alcohol syndrome.</description><subject>Administration, Oral</subject><subject>Animals</subject><subject>Animals, Newborn - growth & development</subject><subject>Animals, Newborn - metabolism</subject><subject>brain</subject><subject>Cerebral Cortex - embryology</subject><subject>Cerebral Cortex - enzymology</subject><subject>Cerebral Cortex - growth & development</subject><subject>development</subject><subject>Enzyme Activation - drug effects</subject><subject>ethanol</subject><subject>Ethanol - administration & dosage</subject><subject>Female</subject><subject>Isoenzymes - drug effects</subject><subject>Isoenzymes - metabolism</subject><subject>Male</subject><subject>Maternal-Fetal Exchange - drug effects</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>phosphorylation</subject><subject>Phosphorylation - drug effects</subject><subject>PKC isoforms</subject><subject>Pregnancy</subject><subject>Protein Kinase C - drug effects</subject><subject>Protein Kinase C - metabolism</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Substrate Specificity - drug effects</subject><issn>0003-9861</issn><issn>1096-0384</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kUFvEzEQhS0EKmnhyg3JJ24b7HjXuz6iVYCqlVrR9mx57dnEaGMH21u1P4j_yYQEbj09ad7zpxk_Qj5wtuSMyc9mGPySK9UtWduKV2TBmZIVE139miwYY6JSneRvyXnOPxnjvJarM3KmWtaseLMgv-9gAlv8I9B-a8IGMvWB3qZYAPXKB5PRoZc5jjHtMjXB0dttzPttTM-TKT4GGke6Di5uIMQ507t5yCWZAv8of4k_TKE9JBiSmWgfU4En6ubkwwZjUB25MZdgCgbWBXeJqE_7mOcE78ib0UwZ3p_0gjx8Xd_336vrm2-X_ZfrygqhStVY2fCmFU7VnWjd4AbWGRyo0XJpnVKwqh2gx9VKSSdci9qOtemkZI1rxAX5dOTuU_w1Qy5657OFaTIB8Dbd4rciW2FweQzaFHNOMOp98juTnjVn-tCLPvSiD73oQy_44OOJPA87cP_jpyLQ744-4HmPHpLO1kOw4HzCfrSL_iX0H4P9noI</recordid><startdate>19980815</startdate><enddate>19980815</enddate><creator>Mahadev, Kalyankar</creator><creator>Vemuri, Mohan C.</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19980815</creationdate><title>Selective Changes in Protein Kinase C Isoforms and Phosphorylation of Endogenous Substrate Proteins in Rat Cerebral Cortex during Pre- and Postnatal Ethanol Exposure</title><author>Mahadev, Kalyankar ; Vemuri, Mohan C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c339t-5c651573d94837dbdb08a1579fc16cd99e24de48319296d3d79297f4a86605d53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Administration, Oral</topic><topic>Animals</topic><topic>Animals, Newborn - growth & development</topic><topic>Animals, Newborn - metabolism</topic><topic>brain</topic><topic>Cerebral Cortex - embryology</topic><topic>Cerebral Cortex - enzymology</topic><topic>Cerebral Cortex - growth & development</topic><topic>development</topic><topic>Enzyme Activation - drug effects</topic><topic>ethanol</topic><topic>Ethanol - administration & dosage</topic><topic>Female</topic><topic>Isoenzymes - drug effects</topic><topic>Isoenzymes - metabolism</topic><topic>Male</topic><topic>Maternal-Fetal Exchange - drug effects</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>phosphorylation</topic><topic>Phosphorylation - drug effects</topic><topic>PKC isoforms</topic><topic>Pregnancy</topic><topic>Protein Kinase C - drug effects</topic><topic>Protein Kinase C - metabolism</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Substrate Specificity - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mahadev, Kalyankar</creatorcontrib><creatorcontrib>Vemuri, Mohan C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of biochemistry and biophysics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mahadev, Kalyankar</au><au>Vemuri, Mohan C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Selective Changes in Protein Kinase C Isoforms and Phosphorylation of Endogenous Substrate Proteins in Rat Cerebral Cortex during Pre- and Postnatal Ethanol Exposure</atitle><jtitle>Archives of biochemistry and biophysics</jtitle><addtitle>Arch Biochem Biophys</addtitle><date>1998-08-15</date><risdate>1998</risdate><volume>356</volume><issue>2</issue><spage>249</spage><epage>257</epage><pages>249-257</pages><issn>0003-9861</issn><eissn>1096-0384</eissn><abstract>The effect of pre- and postnatal ethanol exposure on protein kinase C (PKC) activity, immunochemical analysis of PKC α, βI, βII, γ, δ, ϵ, η, and ζ by isoform-specific antibodies, andin vitrophosphorylation of endogenous substrate proteins was investigated in rat cerebral cortex. The PKC activity was increased throughout the development. However, the activity at the age of 8 days was significantly high in cytosolic and membrane fractions from ethanol-treated rats. Immunochemical analysis showed increased levels of PKC βI and βII at the age of 8 days, and a decrease in δ isoform at 8, 30, and 90 days of age. PKC isoforms α, γ, ϵ, and η showed no appreciable change in ethanol-treated rats. PKC ζ levels were high in the cytosolic fraction from ethanol-treated samples of 90 days age.In vitrophosphorylation of endogenous substrate proteins in the presence of Ca2+/phospholipid showed increased phosphorylation of selective membrane and cytosolic proteins with 87, 65, 50, 43, 36, and 29 kDa in ethanol-treated rats. The phosphorylation of these proteins decreased in the presence of staurosporine, which also supported PKC-mediated phosphorylation. Increased PKC activity, activation of βI and βII isoforms, decreased levels of δ isoform, and phosphorylation of selective substrate proteins in cerebral cortex due to alcohol exposure might be relevant in ethanol-induced central nervous system dysfunction and fetal alcohol syndrome.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9705215</pmid><doi>10.1006/abbi.1998.0773</doi><tpages>9</tpages></addata></record> |
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| subjects | Administration, Oral Animals Animals, Newborn - growth & development Animals, Newborn - metabolism brain Cerebral Cortex - embryology Cerebral Cortex - enzymology Cerebral Cortex - growth & development development Enzyme Activation - drug effects ethanol Ethanol - administration & dosage Female Isoenzymes - drug effects Isoenzymes - metabolism Male Maternal-Fetal Exchange - drug effects Nerve Tissue Proteins - metabolism phosphorylation Phosphorylation - drug effects PKC isoforms Pregnancy Protein Kinase C - drug effects Protein Kinase C - metabolism Rats Rats, Wistar Substrate Specificity - drug effects |
| title | Selective Changes in Protein Kinase C Isoforms and Phosphorylation of Endogenous Substrate Proteins in Rat Cerebral Cortex during Pre- and Postnatal Ethanol Exposure |
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