Identification of the origin and localization of chorion (egg envelope) proteins in an ancient fish, the white sturgeon, Acipenser transmontanus.
Identifieur interne : 000186 ( PubMed/Curation ); précédent : 000185; suivant : 000187Identification of the origin and localization of chorion (egg envelope) proteins in an ancient fish, the white sturgeon, Acipenser transmontanus.
Auteurs : Kenji Murata [États-Unis] ; Fred S. Conte [États-Unis] ; Elizabeth Mcinnis [États-Unis] ; Tak Hou Fong [États-Unis] ; Gary N. Cherr [États-Unis]Source :
- Biology of reproduction [ 1529-7268 ] ; 2014.
English descriptors
- KwdEn :
- Animals, Biological Evolution, Chorion (physiology), Egg Proteins (biosynthesis), Egg Proteins (metabolism), Extracellular Matrix (metabolism), Female, Fishes (physiology), Glycoproteins (biosynthesis), Glycoproteins (metabolism), Immunohistochemistry, Mumps Vaccine (metabolism), Oocytes (cytology), Oocytes (metabolism), Oogenesis (physiology), Ovarian Follicle (cytology), Ovarian Follicle (metabolism), Ovum (cytology), Ovum (metabolism), Phylogeny.
- MESH :
- chemical , biosynthesis : Egg Proteins, Glycoproteins.
- chemical , metabolism : Egg Proteins, Glycoproteins, Mumps Vaccine.
- cytology : Oocytes, Ovarian Follicle, Ovum.
- metabolism : Extracellular Matrix, Oocytes, Ovarian Follicle, Ovum.
- physiology : Chorion, Fishes, Oogenesis.
- Animals, Biological Evolution, Female, Immunohistochemistry, Phylogeny.
Abstract
In many modern teleost fish, chorion (egg envelope) glycoproteins are synthesized in the liver of females, and the expression of those genes is controlled by endogenous estrogen released from the ovary during maturation. However, among the classical teleosts, such as salmonid, carp, and zebrafish, the chorion glycoproteins are synthesized in the oocyte, as in higher vertebrates. Sturgeon, which are members of the subclass Chondrostei, represent an ancient lineage of ray-finned fishes that differ from other teleosts in that their sperm possess acrosomes, their eggs have numerous micropyles, and early embryo development is similar to that of amphibians. In order to understand the molecular mechanisms of chorion formation and the phylogenetic relationship between sturgeon and other teleosts, we used specific antibodies directed against the primary components of sturgeon chorion glycoproteins, using immunoblotting and immunocytochemistry approaches. The origin of each chorion glycoprotein was determined through analyses of both liver and ovary, and their localization during ovarian development was investigated. Our data indicate that the origin of the major chorion glycoproteins of sturgeon, ChG1, ChG2, and ChG4, derive not only from the oocyte itself but also from follicle cells in the ovary, as well as from hepatocytes. In the follicle cell layer, granulosa cells were found to be the primary source of ChGs during oogenesis in white sturgeon. The unique origins of chorion glycoproteins in sturgeon suggest that sturgeons are an intermediate form in the evolution of the teleost lineage.
DOI: 10.1095/biolreprod.113.116194
PubMed: 24804966
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Cherr</name><affiliation wicri:level="2"><nlm:affiliation>Bodega Marine Laboratory, University of California, Davis, Bodega Bay, California Departments of Environmental Toxicology and Nutrition, University of California, Davis, California.</nlm:affiliation><country>États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Bodega Marine Laboratory, University of California, Davis, Bodega Bay, California Departments of Environmental Toxicology and Nutrition, University of California, Davis</wicri:cityArea></affiliation></author></analytic><series><title level="j">Biology of reproduction</title><idno type="eISSN">1529-7268</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Biological Evolution</term><term>Chorion (physiology)</term><term>Egg Proteins (biosynthesis)</term><term>Egg Proteins (metabolism)</term><term>Extracellular Matrix (metabolism)</term><term>Female</term><term>Fishes (physiology)</term><term>Glycoproteins (biosynthesis)</term><term>Glycoproteins (metabolism)</term><term>Immunohistochemistry</term><term>Mumps Vaccine (metabolism)</term><term>Oocytes (cytology)</term><term>Oocytes (metabolism)</term><term>Oogenesis (physiology)</term><term>Ovarian Follicle (cytology)</term><term>Ovarian Follicle (metabolism)</term><term>Ovum (cytology)</term><term>Ovum (metabolism)</term><term>Phylogeny</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Egg Proteins</term><term>Glycoproteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Egg Proteins</term><term>Glycoproteins</term><term>Mumps Vaccine</term></keywords><keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Oocytes</term><term>Ovarian Follicle</term><term>Ovum</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Extracellular Matrix</term><term>Oocytes</term><term>Ovarian Follicle</term><term>Ovum</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Chorion</term><term>Fishes</term><term>Oogenesis</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Biological Evolution</term><term>Female</term><term>Immunohistochemistry</term><term>Phylogeny</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In many modern teleost fish, chorion (egg envelope) glycoproteins are synthesized in the liver of females, and the expression of those genes is controlled by endogenous estrogen released from the ovary during maturation. However, among the classical teleosts, such as salmonid, carp, and zebrafish, the chorion glycoproteins are synthesized in the oocyte, as in higher vertebrates. Sturgeon, which are members of the subclass Chondrostei, represent an ancient lineage of ray-finned fishes that differ from other teleosts in that their sperm possess acrosomes, their eggs have numerous micropyles, and early embryo development is similar to that of amphibians. In order to understand the molecular mechanisms of chorion formation and the phylogenetic relationship between sturgeon and other teleosts, we used specific antibodies directed against the primary components of sturgeon chorion glycoproteins, using immunoblotting and immunocytochemistry approaches. The origin of each chorion glycoprotein was determined through analyses of both liver and ovary, and their localization during ovarian development was investigated. Our data indicate that the origin of the major chorion glycoproteins of sturgeon, ChG1, ChG2, and ChG4, derive not only from the oocyte itself but also from follicle cells in the ovary, as well as from hepatocytes. In the follicle cell layer, granulosa cells were found to be the primary source of ChGs during oogenesis in white sturgeon. The unique origins of chorion glycoproteins in sturgeon suggest that sturgeons are an intermediate form in the evolution of the teleost lineage.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24804966</PMID><DateCreated><Year>2014</Year><Month>06</Month><Day>28</Day></DateCreated><DateCompleted><Year>2015</Year><Month>01</Month><Day>23</Day></DateCompleted><DateRevised><Year>2014</Year><Month>06</Month><Day>28</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1529-7268</ISSN><JournalIssue CitedMedium="Internet"><Volume>90</Volume><Issue>6</Issue><PubDate><Year>2014</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Biology of reproduction</Title><ISOAbbreviation>Biol. Reprod.</ISOAbbreviation></Journal><ArticleTitle>Identification of the origin and localization of chorion (egg envelope) proteins in an ancient fish, the white sturgeon, Acipenser transmontanus.</ArticleTitle><Pagination><MedlinePgn>132</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1095/biolreprod.113.116194</ELocationID><Abstract><AbstractText>In many modern teleost fish, chorion (egg envelope) glycoproteins are synthesized in the liver of females, and the expression of those genes is controlled by endogenous estrogen released from the ovary during maturation. However, among the classical teleosts, such as salmonid, carp, and zebrafish, the chorion glycoproteins are synthesized in the oocyte, as in higher vertebrates. Sturgeon, which are members of the subclass Chondrostei, represent an ancient lineage of ray-finned fishes that differ from other teleosts in that their sperm possess acrosomes, their eggs have numerous micropyles, and early embryo development is similar to that of amphibians. In order to understand the molecular mechanisms of chorion formation and the phylogenetic relationship between sturgeon and other teleosts, we used specific antibodies directed against the primary components of sturgeon chorion glycoproteins, using immunoblotting and immunocytochemistry approaches. The origin of each chorion glycoprotein was determined through analyses of both liver and ovary, and their localization during ovarian development was investigated. Our data indicate that the origin of the major chorion glycoproteins of sturgeon, ChG1, ChG2, and ChG4, derive not only from the oocyte itself but also from follicle cells in the ovary, as well as from hepatocytes. In the follicle cell layer, granulosa cells were found to be the primary source of ChGs during oogenesis in white sturgeon. The unique origins of chorion glycoproteins in sturgeon suggest that sturgeons are an intermediate form in the evolution of the teleost lineage.</AbstractText><CopyrightInformation>© 2014 by the Society for the Study of Reproduction, Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Murata</LastName><ForeName>Kenji</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Center for Health and the Environment, University of California, Davis, California kmurata@ucdavis.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Conte</LastName><ForeName>Fred S</ForeName><Initials>FS</Initials><AffiliationInfo><Affiliation>Department of Animal Science, University of California, Davis, California.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>McInnis</LastName><ForeName>Elizabeth</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Department of Animal Science, University of California, Davis, California.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fong</LastName><ForeName>Tak Hou</ForeName><Initials>TH</Initials><AffiliationInfo><Affiliation>Department of Animal Science, University of California, Davis, California.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cherr</LastName><ForeName>Gary N</ForeName><Initials>GN</Initials><AffiliationInfo><Affiliation>Bodega Marine Laboratory, University of California, Davis, Bodega Bay, California Departments of Environmental Toxicology and Nutrition, University of California, Davis, California.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>05</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biol Reprod</MedlineTA><NlmUniqueID>0207224</NlmUniqueID><ISSNLinking>0006-3363</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004527">Egg Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D006023">Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009108">Mumps Vaccine</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C015753">chorion proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005075" MajorTopicYN="Y">Biological Evolution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002823" MajorTopicYN="N">Chorion</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004527" MajorTopicYN="N">Egg Proteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005109" MajorTopicYN="N">Extracellular Matrix</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="N">Fishes</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006023" MajorTopicYN="N">Glycoproteins</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007150" MajorTopicYN="N">Immunohistochemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009108" MajorTopicYN="N">Mumps Vaccine</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009865" MajorTopicYN="N">Oocytes</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009866" MajorTopicYN="N">Oogenesis</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006080" MajorTopicYN="N">Ovarian Follicle</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010063" MajorTopicYN="N">Ovum</DescriptorName><QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">choriogenin</Keyword><Keyword MajorTopicYN="N">chorion</Keyword><Keyword MajorTopicYN="N">chorion proteins</Keyword><Keyword MajorTopicYN="N">egg envelope</Keyword><Keyword MajorTopicYN="N">extracellular matrix</Keyword><Keyword MajorTopicYN="N">fish reproduction</Keyword><Keyword MajorTopicYN="N">gametogenesis</Keyword><Keyword MajorTopicYN="N">oocyte development</Keyword><Keyword MajorTopicYN="N">oogenesis</Keyword><Keyword MajorTopicYN="N">white sturgeon</Keyword><Keyword MajorTopicYN="N">zona pellucida</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>5</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>5</Month><Day>9</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2015</Year><Month>1</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24804966</ArticleId><ArticleId IdType="pii">biolreprod.113.116194</ArticleId><ArticleId IdType="doi">10.1095/biolreprod.113.116194</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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