Characterization of fertilization‐modulated myelin basic protein kinases from sea star: Regulation of Mapk
Identifieur interne : 001637 ( Istex/Corpus ); précédent : 001636; suivant : 001638Characterization of fertilization‐modulated myelin basic protein kinases from sea star: Regulation of Mapk
Auteurs : Diana L. Lefebvre ; David L. Charest ; Arthur Yee ; Bruce J. Crawford ; Steven L. PelechSource :
- Journal of Cellular Biochemistry [ 0730-2312 ] ; 1999-11-01.
English descriptors
- KwdEn :
- Teeft :
- Assay, Biol, British columbia, Cdna, Dramatic increase, Early development, Early embryogenesis, Embryo, Embryogenesis, Error bars, Extract, Fertilization, Fertilization membrane, Germinal vesicle breakdown, Gvbd, Human erk1, Immature oocytes, Immunoblotting, Inhibitor, Kinase, Lefebvre, Ltered seawater, Mapk, Maturation, Mature oocytes, Meiosis, Meiotic, Meiotic maturation, Mono, Monoq, Monoq column fractions, Monoq fractions, Myelin, Nacl, Nitrocellulose membranes, Ochraceus, Oocyte, Oocyte maturation, Pelech, Peptide, Phosphoamino acid analysis, Phosphorylated, Phosphorylating, Phosphorylating activity, Phosphorylation, Phosphorylation site, Phosphotransferase, Phosphotransferase activities, Phosphotransferase activity, Phosphotransferase activity assays, Pisaster, Pisaster ochraceus, Previous studies, Protein kinase, Protein kinases, Pseudosubstrate inhibitor peptide, Room temperature, Sanghera, Separate experiments, Sperm, Sperm addition, Star embryogenesis, Star fertilization, Star mapk, Star oocyte maturation, Star oocytes, Threonine residues, Time point, Time points, Tyrosine phosphorylation.
Abstract
The myelin basic protein (MBP)‐phosphorylating enzymes present during maturation and early embryogenesis of the sea star (Pisaster ochraceus) were investigated. The major maturation‐activated MBP kinase (p45 Mapk) was molecularly cloned based on tryptic sequence information obtained with the purified enzyme and shown to be highly related to human Erk1 with 76% amino acid identity. Kinase assays and immunoblotting studies revealed that Mapk remained highly active until 12 h post‐fertilization (PF), after which it declined. By 4 days PF, Mapk protein was no longer detectable. At 3 h PF, about half of the detectable MBP phosphotransferase activity could be attributed to a 75 kDa protein kinase that was distinct from Mapk. Like Mapk, this protein phosphorylated MBP mostly on threonine residues, but it failed to phosphorylate a peptide (APRTPGGRR) based upon the Thr‐97 MAP kinase phosphorylation site in MBP. Rather, it phosphorylated a peptide (AAQKRPSQRTKYLA) patterned after the N‐terminus of MBP. Our studies also showed a dramatic increase in MBP phosphotransferase activity occurred by 4 days PF that arose from a third kinase that phosphorylated MBP solely on serine residues. This kinase exhibited the following substrate substrate preference: AAQKRPSQRTKYLA, peptide substrate for S6 kinases (AKRRRLSSLRASTSKSESSQK) > MBP > histone H1 > prota‐mine > casein > APRTPGGRR. This kinase was not appreciably affected by addition of phosphatidylserine/diacylglycerol, or the staurosporine analogue Roche Compound 3, but it was partly inhibited by a protein kinase C pseudosubstrate peptide. Gel filtration analysis revealed an apparent molecular mass of 41 kDa for the enzyme. Therefore, at least two novel MBP‐phosphorylating enzymes distinct from Mapk are preferentially activated following fertilization and early embryogenesis of the sea star. J. Cell. Biochem. 75:272–287, 1999. © 1999 Wiley‐Liss, Inc.
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DOI: 10.1002/(SICI)1097-4644(19991101)75:2<272::AID-JCB10>3.0.CO;2-J
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Biochem.</title><idno type="ISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><imprint><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="1999-11-01">1999-11-01</date><biblScope unit="volume">75</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="272">272</biblScope><biblScope unit="page" to="287">287</biblScope></imprint><idno type="ISSN">0730-2312</idno></series><idno type="istex">D8FE53052A71935886C49B30DD5EF68CFBB96CD0</idno><idno type="DOI">10.1002/(SICI)1097-4644(19991101)75:2<272::AID-JCB10>3.0.CO;2-J</idno><idno type="ArticleID">JCB10</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0730-2312</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>MAP kinase</term><term>fertilization</term><term>oocyte maturation</term><term>sea star</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Assay</term><term>Biol</term><term>British columbia</term><term>Cdna</term><term>Dramatic increase</term><term>Early development</term><term>Early embryogenesis</term><term>Embryo</term><term>Embryogenesis</term><term>Error bars</term><term>Extract</term><term>Fertilization</term><term>Fertilization membrane</term><term>Germinal vesicle breakdown</term><term>Gvbd</term><term>Human erk1</term><term>Immature oocytes</term><term>Immunoblotting</term><term>Inhibitor</term><term>Kinase</term><term>Lefebvre</term><term>Ltered seawater</term><term>Mapk</term><term>Maturation</term><term>Mature oocytes</term><term>Meiosis</term><term>Meiotic</term><term>Meiotic maturation</term><term>Mono</term><term>Monoq</term><term>Monoq column fractions</term><term>Monoq fractions</term><term>Myelin</term><term>Nacl</term><term>Nitrocellulose membranes</term><term>Ochraceus</term><term>Oocyte</term><term>Oocyte maturation</term><term>Pelech</term><term>Peptide</term><term>Phosphoamino acid analysis</term><term>Phosphorylated</term><term>Phosphorylating</term><term>Phosphorylating activity</term><term>Phosphorylation</term><term>Phosphorylation site</term><term>Phosphotransferase</term><term>Phosphotransferase activities</term><term>Phosphotransferase activity</term><term>Phosphotransferase activity assays</term><term>Pisaster</term><term>Pisaster ochraceus</term><term>Previous studies</term><term>Protein kinase</term><term>Protein kinases</term><term>Pseudosubstrate inhibitor peptide</term><term>Room temperature</term><term>Sanghera</term><term>Separate experiments</term><term>Sperm</term><term>Sperm addition</term><term>Star embryogenesis</term><term>Star fertilization</term><term>Star mapk</term><term>Star oocyte maturation</term><term>Star oocytes</term><term>Threonine residues</term><term>Time point</term><term>Time points</term><term>Tyrosine phosphorylation</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The myelin basic protein (MBP)‐phosphorylating enzymes present during maturation and early embryogenesis of the sea star (Pisaster ochraceus) were investigated. The major maturation‐activated MBP kinase (p45 Mapk) was molecularly cloned based on tryptic sequence information obtained with the purified enzyme and shown to be highly related to human Erk1 with 76% amino acid identity. Kinase assays and immunoblotting studies revealed that Mapk remained highly active until 12 h post‐fertilization (PF), after which it declined. By 4 days PF, Mapk protein was no longer detectable. At 3 h PF, about half of the detectable MBP phosphotransferase activity could be attributed to a 75 kDa protein kinase that was distinct from Mapk. Like Mapk, this protein phosphorylated MBP mostly on threonine residues, but it failed to phosphorylate a peptide (APRTPGGRR) based upon the Thr‐97 MAP kinase phosphorylation site in MBP. Rather, it phosphorylated a peptide (AAQKRPSQRTKYLA) patterned after the N‐terminus of MBP. Our studies also showed a dramatic increase in MBP phosphotransferase activity occurred by 4 days PF that arose from a third kinase that phosphorylated MBP solely on serine residues. This kinase exhibited the following substrate substrate preference: AAQKRPSQRTKYLA, peptide substrate for S6 kinases (AKRRRLSSLRASTSKSESSQK) > MBP > histone H1 > prota‐mine > casein > APRTPGGRR. This kinase was not appreciably affected by addition of phosphatidylserine/diacylglycerol, or the staurosporine analogue Roche Compound 3, but it was partly inhibited by a protein kinase C pseudosubstrate peptide. Gel filtration analysis revealed an apparent molecular mass of 41 kDa for the enzyme. Therefore, at least two novel MBP‐phosphorylating enzymes distinct from Mapk are preferentially activated following fertilization and early embryogenesis of the sea star. J. Cell. 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Lefebvre</name><affiliations><json:string>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</json:string></affiliations></json:item><json:item><name>David L. Charest</name><affiliations><json:string>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</json:string></affiliations></json:item><json:item><name>Arthur Yee</name><affiliations><json:string>Kinetek Pharmaceuticals, Inc., Vancouver, British Columbia V6P 6P2, Canada</json:string></affiliations></json:item><json:item><name>Bruce J. Crawford</name><affiliations><json:string>Department of Anatomy, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</json:string></affiliations></json:item><json:item><name>Steven L. Pelech</name><affiliations><json:string>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</json:string><json:string>Department of Medicine, 2nd Floor, Koerner Pavilion, 2211 Wesbrook Mall, University of British Columbia, Vancouver, B.C., Canada, V6T 1Z3.</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>MAP kinase</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>sea star</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>oocyte maturation</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>fertilization</value></json:item></subject><articleId><json:string>JCB10</json:string></articleId><language><json:string>eng</json:string></language><originalGenre><json:string>article</json:string></originalGenre><abstract>The myelin basic protein (MBP)‐phosphorylating enzymes present during maturation and early embryogenesis of the sea star (Pisaster ochraceus) were investigated. The major maturation‐activated MBP kinase (p45 Mapk) was molecularly cloned based on tryptic sequence information obtained with the purified enzyme and shown to be highly related to human Erk1 with 76% amino acid identity. Kinase assays and immunoblotting studies revealed that Mapk remained highly active until 12 h post‐fertilization (PF), after which it declined. By 4 days PF, Mapk protein was no longer detectable. At 3 h PF, about half of the detectable MBP phosphotransferase activity could be attributed to a 75 kDa protein kinase that was distinct from Mapk. Like Mapk, this protein phosphorylated MBP mostly on threonine residues, but it failed to phosphorylate a peptide (APRTPGGRR) based upon the Thr‐97 MAP kinase phosphorylation site in MBP. Rather, it phosphorylated a peptide (AAQKRPSQRTKYLA) patterned after the N‐terminus of MBP. Our studies also showed a dramatic increase in MBP phosphotransferase activity occurred by 4 days PF that arose from a third kinase that phosphorylated MBP solely on serine residues. This kinase exhibited the following substrate substrate preference: AAQKRPSQRTKYLA, peptide substrate for S6 kinases (AKRRRLSSLRASTSKSESSQK) > MBP > histone H1 > prota‐mine > casein > APRTPGGRR. This kinase was not appreciably affected by addition of phosphatidylserine/diacylglycerol, or the staurosporine analogue Roche Compound 3, but it was partly inhibited by a protein kinase C pseudosubstrate peptide. Gel filtration analysis revealed an apparent molecular mass of 41 kDa for the enzyme. Therefore, at least two novel MBP‐phosphorylating enzymes distinct from Mapk are preferentially activated following fertilization and early embryogenesis of the sea star. J. Cell. Biochem. 75:272–287, 1999. © 1999 Wiley‐Liss, Inc.</abstract><qualityIndicators><score>8</score><pdfVersion>1.2</pdfVersion><pdfPageSize>612 x 792 pts (letter)</pdfPageSize><refBibsNative>true</refBibsNative><abstractCharCount>1917</abstractCharCount><pdfWordCount>7172</pdfWordCount><pdfCharCount>44040</pdfCharCount><pdfPageCount>16</pdfPageCount><abstractWordCount>279</abstractWordCount></qualityIndicators><title>Characterization of fertilization‐modulated myelin basic protein kinases from sea star: Regulation of Mapk</title><genre><json:string>article</json:string></genre><host><title>Journal of Cellular Biochemistry</title><language><json:string>unknown</json:string></language><doi><json:string>10.1002/(ISSN)1097-4644</json:string></doi><issn><json:string>0730-2312</json:string></issn><eissn><json:string>1097-4644</json:string></eissn><publisherId><json:string>JCB</json:string></publisherId><volume>75</volume><issue>2</issue><pages><first>272</first><last>287</last><total>16</total></pages><genre><json:string>journal</json:string></genre><subject><json:item><value>Research Article</value></json:item></subject></host><categories><wos><json:string>science</json:string><json:string>cell biology</json:string><json:string>biochemistry & molecular biology</json:string></wos><scienceMetrix><json:string>health sciences</json:string><json:string>biomedical research</json:string><json:string>biochemistry & molecular biology</json:string></scienceMetrix><inist><json:string>sciences appliquees, technologies et medecines</json:string><json:string>sciences biologiques et medicales</json:string><json:string>sciences biologiques fondamentales et appliquees. psychologie</json:string></inist></categories><publicationDate>1999</publicationDate><copyrightDate>1999</copyrightDate><doi><json:string>10.1002/(SICI)1097-4644(19991101)75:2>272::AID-JCB10>3.0.CO;2-J</json:string></doi><id>D8FE53052A71935886C49B30DD5EF68CFBB96CD0</id><score>1</score><fulltext><json:item><extension>pdf</extension><original>true</original><mimetype>application/pdf</mimetype><uri>https://api.istex.fr/document/D8FE53052A71935886C49B30DD5EF68CFBB96CD0/fulltext/pdf</uri></json:item><json:item><extension>zip</extension><original>false</original><mimetype>application/zip</mimetype><uri>https://api.istex.fr/document/D8FE53052A71935886C49B30DD5EF68CFBB96CD0/fulltext/zip</uri></json:item><istex:fulltextTEI uri="https://api.istex.fr/document/D8FE53052A71935886C49B30DD5EF68CFBB96CD0/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a" type="main" xml:lang="en">Characterization of fertilization‐modulated myelin basic protein kinases from sea star: Regulation of Mapk</title></titleStmt><publicationStmt><authority>ISTEX</authority><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><availability><p>Copyright © 1999 Wiley‐Liss, Inc.</p></availability><date>1999</date></publicationStmt><notesStmt><note>Medical Research Council of Canada (MRCC)</note></notesStmt><sourceDesc><biblStruct type="inbook"><analytic><title level="a" type="main" xml:lang="en">Characterization of fertilization‐modulated myelin basic protein kinases from sea star: Regulation of Mapk</title><author xml:id="author-1"><persName><forename type="first">Diana L.</forename><surname>Lefebvre</surname></persName><affiliation>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</affiliation></author><author xml:id="author-2"><persName><forename type="first">David L.</forename><surname>Charest</surname></persName><affiliation>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</affiliation></author><author xml:id="author-3"><persName><forename type="first">Arthur</forename><surname>Yee</surname></persName><affiliation>Kinetek Pharmaceuticals, Inc., Vancouver, British Columbia V6P 6P2, Canada</affiliation></author><author xml:id="author-4"><persName><forename type="first">Bruce J.</forename><surname>Crawford</surname></persName><affiliation>Department of Anatomy, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</affiliation></author><author xml:id="author-5"><persName><forename type="first">Steven L.</forename><surname>Pelech</surname></persName><affiliation>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</affiliation><affiliation>Department of Medicine, 2nd Floor, Koerner Pavilion, 2211 Wesbrook Mall, University of British Columbia, Vancouver, B.C., Canada, V6T 1Z3.</affiliation></author></analytic><monogr><title level="j">Journal of Cellular Biochemistry</title><title level="j" type="abbrev">J. Cell. Biochem.</title><idno type="pISSN">0730-2312</idno><idno type="eISSN">1097-4644</idno><idno type="DOI">10.1002/(ISSN)1097-4644</idno><imprint><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="1999-11-01"></date><biblScope unit="volume">75</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="272">272</biblScope><biblScope unit="page" to="287">287</biblScope></imprint></monogr><idno type="istex">D8FE53052A71935886C49B30DD5EF68CFBB96CD0</idno><idno type="DOI">10.1002/(SICI)1097-4644(19991101)75:2<272::AID-JCB10>3.0.CO;2-J</idno><idno type="ArticleID">JCB10</idno></biblStruct></sourceDesc></fileDesc><profileDesc><creation><date>1999</date></creation><langUsage><language ident="en">en</language></langUsage><abstract xml:lang="en"><p>The myelin basic protein (MBP)‐phosphorylating enzymes present during maturation and early embryogenesis of the sea star (Pisaster ochraceus) were investigated. The major maturation‐activated MBP kinase (p45 Mapk) was molecularly cloned based on tryptic sequence information obtained with the purified enzyme and shown to be highly related to human Erk1 with 76% amino acid identity. Kinase assays and immunoblotting studies revealed that Mapk remained highly active until 12 h post‐fertilization (PF), after which it declined. By 4 days PF, Mapk protein was no longer detectable. At 3 h PF, about half of the detectable MBP phosphotransferase activity could be attributed to a 75 kDa protein kinase that was distinct from Mapk. Like Mapk, this protein phosphorylated MBP mostly on threonine residues, but it failed to phosphorylate a peptide (APRTPGGRR) based upon the Thr‐97 MAP kinase phosphorylation site in MBP. Rather, it phosphorylated a peptide (AAQKRPSQRTKYLA) patterned after the N‐terminus of MBP. Our studies also showed a dramatic increase in MBP phosphotransferase activity occurred by 4 days PF that arose from a third kinase that phosphorylated MBP solely on serine residues. This kinase exhibited the following substrate substrate preference: AAQKRPSQRTKYLA, peptide substrate for S6 kinases (AKRRRLSSLRASTSKSESSQK) > MBP > histone H1 > prota‐mine > casein > APRTPGGRR. This kinase was not appreciably affected by addition of phosphatidylserine/diacylglycerol, or the staurosporine analogue Roche Compound 3, but it was partly inhibited by a protein kinase C pseudosubstrate peptide. Gel filtration analysis revealed an apparent molecular mass of 41 kDa for the enzyme. Therefore, at least two novel MBP‐phosphorylating enzymes distinct from Mapk are preferentially activated following fertilization and early embryogenesis of the sea star. J. Cell. Biochem. 75:272–287, 1999. © 1999 Wiley‐Liss, Inc.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>keywords</head><item><term>MAP kinase</term></item><item><term>sea star</term></item><item><term>oocyte maturation</term></item><item><term>fertilization</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>article-category</head><item><term>Research Article</term></item></list></keywords></textClass></profileDesc><revisionDesc><change when="1999-02-26">Received</change><change when="1999-05-07">Registration</change><change when="1999-11-01">Published</change></revisionDesc></teiHeader></istex:fulltextTEI><json:item><extension>txt</extension><original>false</original><mimetype>text/plain</mimetype><uri>https://api.istex.fr/document/D8FE53052A71935886C49B30DD5EF68CFBB96CD0/fulltext/txt</uri></json:item></fulltext><metadata><istex:metadataXml wicri:clean="Wiley, elements deleted: body"><istex:xmlDeclaration>version="1.0" encoding="UTF-8" standalone="yes"</istex:xmlDeclaration><istex:document><component version="2.0" type="serialArticle" xml:lang="en"><header><publicationMeta level="product"><publisherInfo><publisherName>John Wiley & Sons, Inc.</publisherName><publisherLoc>New York</publisherLoc></publisherInfo><doi registered="yes">10.1002/(ISSN)1097-4644</doi><issn type="print">0730-2312</issn><issn type="electronic">1097-4644</issn><idGroup><id type="product" value="JCB"></id></idGroup><titleGroup><title type="main" xml:lang="en" sort="JOURNAL OF CELLULAR BIOCHEMISTRY">Journal of Cellular Biochemistry</title><title type="short">J. Cell. Biochem.</title></titleGroup></publicationMeta><publicationMeta level="part" position="20"><doi origin="wiley" registered="yes">10.1002/(SICI)1097-4644(19991101)75:2<>1.0.CO;2-D</doi><numberingGroup><numbering type="journalVolume" number="75">75</numbering><numbering type="journalIssue">2</numbering></numberingGroup><coverDate startDate="1999-11-01">1 November 1999</coverDate></publicationMeta><publicationMeta level="unit" type="article" position="10" status="forIssue"><doi origin="wiley" registered="yes">10.1002/(SICI)1097-4644(19991101)75:2<272::AID-JCB10>3.0.CO;2-J</doi><idGroup><id type="unit" value="JCB10"></id></idGroup><countGroup><count type="pageTotal" number="16"></count></countGroup><titleGroup><title type="articleCategory">Research Article</title><title type="tocHeading1">ARTICLES</title></titleGroup><copyright ownership="publisher">Copyright © 1999 Wiley‐Liss, Inc.</copyright><eventGroup><event type="manuscriptReceived" date="1999-02-26"></event><event type="manuscriptAccepted" date="1999-05-07"></event><event type="firstOnline" date="1999-09-27"></event><event type="publishedOnlineFinalForm" date="1999-09-27"></event><event type="xmlConverted" agent="Converter:JWSART34_TO_WML3G version:2.3.2 mode:FullText source:HeaderRef result:HeaderRef" date="2010-03-06"></event><event type="xmlConverted" agent="Converter:WILEY_ML3G_TO_WILEY_ML3GV2 version:3.8.8" date="2014-01-29"></event><event type="xmlConverted" agent="Converter:WML3G_To_WML3G version:4.1.7 mode:FullText,remove_FC" date="2014-10-24"></event></eventGroup><numberingGroup><numbering type="pageFirst">272</numbering><numbering type="pageLast">287</numbering></numberingGroup><correspondenceTo>Department of Medicine, 2nd Floor, Koerner Pavilion, 2211 Wesbrook Mall, University of British Columbia, Vancouver, B.C., Canada, V6T 1Z3.</correspondenceTo><linkGroup><link type="toTypesetVersion" href="file:JCB.JCB10.pdf"></link></linkGroup></publicationMeta><contentMeta><countGroup><count type="figureTotal" number="8"></count><count type="tableTotal" number="0"></count><count type="referenceTotal" number="26"></count><count type="wordTotal" number="8332"></count></countGroup><titleGroup><title type="main" xml:lang="en">Characterization of fertilization‐modulated myelin basic protein kinases from sea star: Regulation of Mapk</title><title type="short" xml:lang="en">MBP Kinases During Sea Star Fertilization and Embryogenesis</title></titleGroup><creators><creator xml:id="au1" creatorRole="author" affiliationRef="#af1"><personName><givenNames>Diana L.</givenNames><familyName>Lefebvre</familyName></personName></creator><creator xml:id="au2" creatorRole="author" affiliationRef="#af1"><personName><givenNames>David L.</givenNames><familyName>Charest</familyName></personName></creator><creator xml:id="au3" creatorRole="author" affiliationRef="#af3"><personName><givenNames>Arthur</givenNames><familyName>Yee</familyName></personName></creator><creator xml:id="au4" creatorRole="author" affiliationRef="#af2"><personName><givenNames>Bruce J.</givenNames><familyName>Crawford</familyName></personName></creator><creator xml:id="au5" creatorRole="author" affiliationRef="#af1" corresponding="yes"><personName><givenNames>Steven L.</givenNames><familyName>Pelech</familyName></personName><contactDetails><email>spelech@home.com</email></contactDetails></creator></creators><affiliationGroup><affiliation xml:id="af1" countryCode="CA" type="organization"><unparsedAffiliation>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</unparsedAffiliation></affiliation><affiliation xml:id="af2" countryCode="CA" type="organization"><unparsedAffiliation>Department of Anatomy, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</unparsedAffiliation></affiliation><affiliation xml:id="af3" countryCode="CA" type="organization"><unparsedAffiliation>Kinetek Pharmaceuticals, Inc., Vancouver, British Columbia V6P 6P2, Canada</unparsedAffiliation></affiliation></affiliationGroup><keywordGroup xml:lang="en" type="author"><keyword xml:id="kwd1">MAP kinase</keyword><keyword xml:id="kwd2">sea star</keyword><keyword xml:id="kwd3">oocyte maturation</keyword><keyword xml:id="kwd4">fertilization</keyword></keywordGroup><fundingInfo><fundingAgency>Medical Research Council of Canada (MRCC)</fundingAgency></fundingInfo><abstractGroup><abstract type="main" xml:lang="en"><title type="main">Abstract</title><p>The myelin basic protein (MBP)‐phosphorylating enzymes present during maturation and early embryogenesis of the sea star (<i>Pisaster ochraceus</i>) were investigated. The major maturation‐activated MBP kinase (p45 Mapk) was molecularly cloned based on tryptic sequence information obtained with the purified enzyme and shown to be highly related to human Erk1 with 76% amino acid identity. Kinase assays and immunoblotting studies revealed that Mapk remained highly active until 12 h post‐fertilization (PF), after which it declined. By 4 days PF, Mapk protein was no longer detectable. At 3 h PF, about half of the detectable MBP phosphotransferase activity could be attributed to a 75 kDa protein kinase that was distinct from Mapk. Like Mapk, this protein phosphorylated MBP mostly on threonine residues, but it failed to phosphorylate a peptide (APRTPGGRR) based upon the Thr‐97 MAP kinase phosphorylation site in MBP. Rather, it phosphorylated a peptide (AAQKRPSQRTKYLA) patterned after the N‐terminus of MBP. Our studies also showed a dramatic increase in MBP phosphotransferase activity occurred by 4 days PF that arose from a third kinase that phosphorylated MBP solely on serine residues. This kinase exhibited the following substrate substrate preference: AAQKRPSQRTKYLA, peptide substrate for S6 kinases (AKRRRLSSLRASTSKSESSQK) > MBP > histone H1 > prota‐mine > casein > APRTPGGRR. This kinase was not appreciably affected by addition of phosphatidylserine/diacylglycerol, or the staurosporine analogue Roche Compound 3, but it was partly inhibited by a protein kinase C pseudosubstrate peptide. Gel filtration analysis revealed an apparent molecular mass of 41 kDa for the enzyme. Therefore, at least two novel MBP‐phosphorylating enzymes distinct from Mapk are preferentially activated following fertilization and early embryogenesis of the sea star. J. Cell. Biochem. 75:272–287, 1999. © 1999 Wiley‐Liss, Inc.</p></abstract></abstractGroup></contentMeta></header></component></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Characterization of fertilization‐modulated myelin basic protein kinases from sea star: Regulation of Mapk</title></titleInfo><titleInfo type="abbreviated" lang="en"><title>MBP Kinases During Sea Star Fertilization and Embryogenesis</title></titleInfo><titleInfo type="alternative" contentType="CDATA" lang="en"><title>Characterization of fertilization‐modulated myelin basic protein kinases from sea star: Regulation of Mapk</title></titleInfo><name type="personal"><namePart type="given">Diana L.</namePart><namePart type="family">Lefebvre</namePart><affiliation>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">David L.</namePart><namePart type="family">Charest</namePart><affiliation>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Arthur</namePart><namePart type="family">Yee</namePart><affiliation>Kinetek Pharmaceuticals, Inc., Vancouver, British Columbia V6P 6P2, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Bruce J.</namePart><namePart type="family">Crawford</namePart><affiliation>Department of Anatomy, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Steven L.</namePart><namePart type="family">Pelech</namePart><affiliation>Department of Medicine, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada</affiliation><affiliation>Department of Medicine, 2nd Floor, Koerner Pavilion, 2211 Wesbrook Mall, University of British Columbia, Vancouver, B.C., Canada, V6T 1Z3.</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="article" displayLabel="article"></genre><originInfo><publisher>John Wiley & Sons, Inc.</publisher><place><placeTerm type="text">New York</placeTerm></place><dateIssued encoding="w3cdtf">1999-11-01</dateIssued><dateCaptured encoding="w3cdtf">1999-02-26</dateCaptured><dateValid encoding="w3cdtf">1999-05-07</dateValid><copyrightDate encoding="w3cdtf">1999</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><physicalDescription><internetMediaType>text/html</internetMediaType><extent unit="figures">8</extent><extent unit="references">26</extent><extent unit="words">8332</extent></physicalDescription><abstract lang="en">The myelin basic protein (MBP)‐phosphorylating enzymes present during maturation and early embryogenesis of the sea star (Pisaster ochraceus) were investigated. The major maturation‐activated MBP kinase (p45 Mapk) was molecularly cloned based on tryptic sequence information obtained with the purified enzyme and shown to be highly related to human Erk1 with 76% amino acid identity. Kinase assays and immunoblotting studies revealed that Mapk remained highly active until 12 h post‐fertilization (PF), after which it declined. By 4 days PF, Mapk protein was no longer detectable. At 3 h PF, about half of the detectable MBP phosphotransferase activity could be attributed to a 75 kDa protein kinase that was distinct from Mapk. Like Mapk, this protein phosphorylated MBP mostly on threonine residues, but it failed to phosphorylate a peptide (APRTPGGRR) based upon the Thr‐97 MAP kinase phosphorylation site in MBP. Rather, it phosphorylated a peptide (AAQKRPSQRTKYLA) patterned after the N‐terminus of MBP. Our studies also showed a dramatic increase in MBP phosphotransferase activity occurred by 4 days PF that arose from a third kinase that phosphorylated MBP solely on serine residues. This kinase exhibited the following substrate substrate preference: AAQKRPSQRTKYLA, peptide substrate for S6 kinases (AKRRRLSSLRASTSKSESSQK) > MBP > histone H1 > prota‐mine > casein > APRTPGGRR. This kinase was not appreciably affected by addition of phosphatidylserine/diacylglycerol, or the staurosporine analogue Roche Compound 3, but it was partly inhibited by a protein kinase C pseudosubstrate peptide. Gel filtration analysis revealed an apparent molecular mass of 41 kDa for the enzyme. Therefore, at least two novel MBP‐phosphorylating enzymes distinct from Mapk are preferentially activated following fertilization and early embryogenesis of the sea star. J. Cell. Biochem. 75:272–287, 1999. © 1999 Wiley‐Liss, Inc.</abstract><note type="funding">Medical Research Council of Canada (MRCC)</note><subject lang="en"><genre>keywords</genre><topic>MAP kinase</topic><topic>sea star</topic><topic>oocyte maturation</topic><topic>fertilization</topic></subject><relatedItem type="host"><titleInfo><title>Journal of Cellular Biochemistry</title></titleInfo><titleInfo type="abbreviated"><title>J. Cell. Biochem.</title></titleInfo><genre type="journal">journal</genre><subject><genre>article-category</genre><topic>Research Article</topic></subject><identifier type="ISSN">0730-2312</identifier><identifier type="eISSN">1097-4644</identifier><identifier type="DOI">10.1002/(ISSN)1097-4644</identifier><identifier type="PublisherID">JCB</identifier><part><date>1999</date><detail type="volume"><caption>vol.</caption><number>75</number></detail><detail type="issue"><caption>no.</caption><number>2</number></detail><extent unit="pages"><start>272</start><end>287</end><total>16</total></extent></part></relatedItem><identifier type="istex">D8FE53052A71935886C49B30DD5EF68CFBB96CD0</identifier><identifier type="DOI">10.1002/(SICI)1097-4644(19991101)75:2<272::AID-JCB10>3.0.CO;2-J</identifier><identifier type="ArticleID">JCB10</identifier><accessCondition type="use and reproduction" contentType="copyright">Copyright © 1999 Wiley‐Liss, Inc.</accessCondition><recordInfo><recordContentSource>WILEY</recordContentSource><recordOrigin>John Wiley & Sons, Inc.</recordOrigin></recordInfo></mods></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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