Evolutionary trends of neurofilament proteins in fish.
Identifieur interne : 000685 ( PubMed/Checkpoint ); précédent : 000684; suivant : 000686Evolutionary trends of neurofilament proteins in fish.
Auteurs : C. Mencarelli [Italie] ; B. Magi ; B. Marzocchi ; M. Contorni ; V. PalliniSource :
- Comparative biochemistry and physiology. B, Comparative biochemistry [ 0305-0491 ] ; 1991.
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Neurofilament Proteins.
- chemical , immunology : Epitopes, Neurofilament Proteins.
- chemistry : Ganglia.
- Amino Acid Sequence, Animals, Antibody Specificity, Biological Evolution, Brain Chemistry, Cross Reactions, Fishes, Immunoblotting, Molecular Sequence Data.
Abstract
1. Neurofilament complement was studied in an early chordate (Ciona intestinalis) and six fish species by immunoblot with antisera specific for each of the three mammalian NF subunits. 2. The anti-NF-H and anti-NF-M antisera were characterized as strictly specific for phosphorylated epitopes located in the carboxyterminal domain. 3. The NF-L subunit is absent in primitive chordates and appears first in fish; it can be identified on the basis of its apparent mol. wt, its reactivity with the anti-IFA antibody and with polyclonal antibodies raised to the NF-L subunit of mammals. 4. Primitive chordate neurofilaments are constituted by a single polypeptide of ca 160,000 mol. wt exhibiting only M-type phosphorylation-dependent epitopes. 5. Primitive fish (Acipenser transmontanus, Salmo gairdneri, Scorpaena porcus, Serranus scriba) possess only a single high mol. wt NF subunit reacting with both anti-NF-H and anti-NF-M antiserum while more recent species (Mugil saliens, Perca fluviatilis) possess two high mol. wt NF subunits which are immunologically distinct as to their phosphorylation structures. 6. The existence in some fish species of two high mol. wt NF polypeptides suggests that the process of gene duplication and diversification supposed to have given rise to the two high mol. wt NF subunits of mammals and birds has occurred repeatedly in vertebrate evolution, and may be regarded as a case of convergent evolution.
PubMed: 1723670
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Contorni</name></author><author><name sortKey="Pallini, V" sort="Pallini, V" uniqKey="Pallini V" first="V" last="Pallini">V. 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B, Comparative biochemistry</title><idno type="ISSN">0305-0491</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibody Specificity</term><term>Biological Evolution</term><term>Brain Chemistry</term><term>Cross Reactions</term><term>Epitopes (immunology)</term><term>Fishes</term><term>Ganglia (chemistry)</term><term>Immunoblotting</term><term>Molecular Sequence Data</term><term>Neurofilament Proteins (chemistry)</term><term>Neurofilament Proteins (immunology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Neurofilament Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Epitopes</term><term>Neurofilament Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Ganglia</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Antibody Specificity</term><term>Biological Evolution</term><term>Brain Chemistry</term><term>Cross Reactions</term><term>Fishes</term><term>Immunoblotting</term><term>Molecular Sequence Data</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">1. Neurofilament complement was studied in an early chordate (Ciona intestinalis) and six fish species by immunoblot with antisera specific for each of the three mammalian NF subunits. 2. The anti-NF-H and anti-NF-M antisera were characterized as strictly specific for phosphorylated epitopes located in the carboxyterminal domain. 3. The NF-L subunit is absent in primitive chordates and appears first in fish; it can be identified on the basis of its apparent mol. wt, its reactivity with the anti-IFA antibody and with polyclonal antibodies raised to the NF-L subunit of mammals. 4. Primitive chordate neurofilaments are constituted by a single polypeptide of ca 160,000 mol. wt exhibiting only M-type phosphorylation-dependent epitopes. 5. Primitive fish (Acipenser transmontanus, Salmo gairdneri, Scorpaena porcus, Serranus scriba) possess only a single high mol. wt NF subunit reacting with both anti-NF-H and anti-NF-M antiserum while more recent species (Mugil saliens, Perca fluviatilis) possess two high mol. wt NF subunits which are immunologically distinct as to their phosphorylation structures. 6. The existence in some fish species of two high mol. wt NF polypeptides suggests that the process of gene duplication and diversification supposed to have given rise to the two high mol. wt NF subunits of mammals and birds has occurred repeatedly in vertebrate evolution, and may be regarded as a case of convergent evolution.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1723670</PMID><DateCreated><Year>1992</Year><Month>03</Month><Day>18</Day></DateCreated><DateCompleted><Year>1992</Year><Month>03</Month><Day>18</Day></DateCompleted><DateRevised><Year>2010</Year><Month>11</Month><Day>18</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0305-0491</ISSN><JournalIssue CitedMedium="Print"><Volume>100</Volume><Issue>4</Issue><PubDate><Year>1991</Year></PubDate></JournalIssue><Title>Comparative biochemistry and physiology. B, Comparative biochemistry</Title><ISOAbbreviation>Comp. Biochem. Physiol., B</ISOAbbreviation></Journal><ArticleTitle>Evolutionary trends of neurofilament proteins in fish.</ArticleTitle><Pagination><MedlinePgn>733-40</MedlinePgn></Pagination><Abstract><AbstractText>1. Neurofilament complement was studied in an early chordate (Ciona intestinalis) and six fish species by immunoblot with antisera specific for each of the three mammalian NF subunits. 2. The anti-NF-H and anti-NF-M antisera were characterized as strictly specific for phosphorylated epitopes located in the carboxyterminal domain. 3. The NF-L subunit is absent in primitive chordates and appears first in fish; it can be identified on the basis of its apparent mol. wt, its reactivity with the anti-IFA antibody and with polyclonal antibodies raised to the NF-L subunit of mammals. 4. Primitive chordate neurofilaments are constituted by a single polypeptide of ca 160,000 mol. wt exhibiting only M-type phosphorylation-dependent epitopes. 5. Primitive fish (Acipenser transmontanus, Salmo gairdneri, Scorpaena porcus, Serranus scriba) possess only a single high mol. wt NF subunit reacting with both anti-NF-H and anti-NF-M antiserum while more recent species (Mugil saliens, Perca fluviatilis) possess two high mol. wt NF subunits which are immunologically distinct as to their phosphorylation structures. 6. The existence in some fish species of two high mol. wt NF polypeptides suggests that the process of gene duplication and diversification supposed to have given rise to the two high mol. wt NF subunits of mammals and birds has occurred repeatedly in vertebrate evolution, and may be regarded as a case of convergent evolution.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Mencarelli</LastName><ForeName>C</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Evolutionary Biology, University of Siena, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Magi</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Marzocchi</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Contorni</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Pallini</LastName><ForeName>V</ForeName><Initials>V</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Comp Biochem Physiol B</MedlineTA><NlmUniqueID>2984730R</NlmUniqueID><ISSNLinking>0305-0491</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000939">Epitopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016900">Neurofilament Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000918" MajorTopicYN="N">Antibody Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005075" MajorTopicYN="Y">Biological Evolution</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001923" MajorTopicYN="N">Brain Chemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003429" MajorTopicYN="N">Cross Reactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005399" MajorTopicYN="Y">Fishes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005724" MajorTopicYN="N">Ganglia</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015151" MajorTopicYN="N">Immunoblotting</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016900" MajorTopicYN="Y">Neurofilament Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1723670</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li></country></list><tree><noCountry><name sortKey="Contorni, M" sort="Contorni, M" uniqKey="Contorni M" first="M" last="Contorni">M. Contorni</name><name sortKey="Magi, B" sort="Magi, B" uniqKey="Magi B" first="B" last="Magi">B. Magi</name><name sortKey="Marzocchi, B" sort="Marzocchi, B" uniqKey="Marzocchi B" first="B" last="Marzocchi">B. Marzocchi</name><name sortKey="Pallini, V" sort="Pallini, V" uniqKey="Pallini V" first="V" last="Pallini">V. Pallini</name></noCountry><country name="Italie"><noRegion><name sortKey="Mencarelli, C" sort="Mencarelli, C" uniqKey="Mencarelli C" first="C" last="Mencarelli">C. Mencarelli</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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