Monoclonal antibodies selective for low molecular weight neurofilaments.
Identifieur interne : 000137 ( Ncbi/Merge ); précédent : 000136; suivant : 000138Monoclonal antibodies selective for low molecular weight neurofilaments.
Auteurs : Niklas Norgren [Suède] ; Jan-Erik Karlsson ; Lars Rosengren ; Torgny StigbrandSource :
- Hybridoma and hybridomics [ 1536-8599 ] ; 2002.
Descripteurs français
- KwdFr :
- Animaux, Anticorps monoclonaux (métabolisme), Axones (métabolisme), Banque de gènes, Banque de peptides, Bovins, Cartographie peptidique, Cartographie épitopique, Chymotrypsine (), Conformation des protéines, Hybridomes (métabolisme), Liaison aux protéines, Macaca, Neurones (métabolisme), Peptides (), Peptides (métabolisme), Souris, Souris de lignée BALB C, Structure tertiaire des protéines, Technique de Western, Test ELISA, Épitopes.
- MESH :
- métabolisme : Anticorps monoclonaux, Axones, Hybridomes, Neurones, Peptides.
- Animaux, Banque de gènes, Banque de peptides, Bovins, Cartographie peptidique, Cartographie épitopique, Chymotrypsine, Conformation des protéines, Liaison aux protéines, Macaca, Peptides, Souris, Souris de lignée BALB C, Structure tertiaire des protéines, Technique de Western, Test ELISA, Épitopes.
English descriptors
- KwdEn :
- Animals, Antibodies, Monoclonal (metabolism), Axons (metabolism), Blotting, Western, Cattle, Chymotrypsin (chemistry), Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Epitopes, Gene Library, Hybridomas (metabolism), Macaca, Mice, Mice, Inbred BALB C, Neurons (metabolism), Peptide Library, Peptide Mapping, Peptides (chemistry), Peptides (metabolism), Protein Binding, Protein Conformation, Protein Structure, Tertiary.
- MESH :
- chemical , chemistry : Chymotrypsin, Peptides.
- chemical , metabolism : Antibodies, Monoclonal, Peptides.
- metabolism : Axons, Hybridomas, Neurons.
- Animals, Blotting, Western, Cattle, Enzyme-Linked Immunosorbent Assay, Epitope Mapping, Epitopes, Gene Library, Macaca, Mice, Mice, Inbred BALB C, Peptide Library, Peptide Mapping, Protein Binding, Protein Conformation, Protein Structure, Tertiary.
Abstract
Neurofilaments are necessary for the maintenance of axonal caliber and structural organization of nerve cells. The low molecular weight form of neurofilament, the neurofilament light protein, which serves as the core of the filament, was used as immunogen for generation of hybridomas with selective reactivity with this form of the filament. Six hybridomas, out of approximately 100 tested clones, were highly discriminatory. All involved epitopes were localized to the rod region of the antigen, as determined by alpha-chymotrypsin digestion of the purified filament and enzymatic peptide mapping. Synthetic peptides (20 mers) covering the entire rod region did not react with the antibodies. A phage display peptide library was used to identify four consensus sequences for the antibodies. The results indicate that all epitopes were of conformational type. Pair-wise BIAcore data furthermore indicated that the epitopes were independent. The access to such specific reagents is a prerequisite for further elucidation of the biology of the low molecular weight form of neurofilaments proteins.
DOI: 10.1089/15368590252917647
PubMed: 11991817
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pubmed:11991817Le document en format XML
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T" first="Torgny" last="Stigbrand">Torgny Stigbrand</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:11991817</idno><idno type="pmid">11991817</idno><idno type="doi">10.1089/15368590252917647</idno><idno type="wicri:Area/PubMed/Corpus">002509</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002509</idno><idno type="wicri:Area/PubMed/Curation">002509</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002509</idno><idno type="wicri:Area/PubMed/Checkpoint">002362</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">002362</idno><idno type="wicri:Area/Ncbi/Merge">000137</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Monoclonal antibodies selective for low molecular weight neurofilaments.</title><author><name sortKey="Norgren, Niklas" sort="Norgren, Niklas" uniqKey="Norgren N" first="Niklas" last="Norgren">Niklas Norgren</name><affiliation wicri:level="1"><nlm:affiliation>Department of Immunology, University of Umeå, S-90187 Umeå, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Immunology, University of Umeå, S-90187 Umeå</wicri:regionArea><wicri:noRegion>S-90187 Umeå</wicri:noRegion></affiliation></author><author><name sortKey="Karlsson, Jan Erik" sort="Karlsson, Jan Erik" uniqKey="Karlsson J" first="Jan-Erik" last="Karlsson">Jan-Erik Karlsson</name></author><author><name sortKey="Rosengren, Lars" sort="Rosengren, Lars" uniqKey="Rosengren L" first="Lars" last="Rosengren">Lars Rosengren</name></author><author><name sortKey="Stigbrand, Torgny" sort="Stigbrand, Torgny" uniqKey="Stigbrand T" first="Torgny" last="Stigbrand">Torgny Stigbrand</name></author></analytic><series><title level="j">Hybridoma and hybridomics</title><idno type="ISSN">1536-8599</idno><imprint><date when="2002" 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gènes</term><term>Banque de peptides</term><term>Bovins</term><term>Cartographie peptidique</term><term>Cartographie épitopique</term><term>Chymotrypsine ()</term><term>Conformation des protéines</term><term>Hybridomes (métabolisme)</term><term>Liaison aux protéines</term><term>Macaca</term><term>Neurones (métabolisme)</term><term>Peptides ()</term><term>Peptides (métabolisme)</term><term>Souris</term><term>Souris de lignée BALB C</term><term>Structure tertiaire des protéines</term><term>Technique de Western</term><term>Test ELISA</term><term>Épitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chymotrypsin</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antibodies, Monoclonal</term><term>Peptides</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Axons</term><term>Hybridomas</term><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Anticorps monoclonaux</term><term>Axones</term><term>Hybridomes</term><term>Neurones</term><term>Peptides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Blotting, Western</term><term>Cattle</term><term>Enzyme-Linked Immunosorbent Assay</term><term>Epitope Mapping</term><term>Epitopes</term><term>Gene Library</term><term>Macaca</term><term>Mice</term><term>Mice, Inbred BALB C</term><term>Peptide Library</term><term>Peptide Mapping</term><term>Protein Binding</term><term>Protein Conformation</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Banque de gènes</term><term>Banque de peptides</term><term>Bovins</term><term>Cartographie peptidique</term><term>Cartographie épitopique</term><term>Chymotrypsine</term><term>Conformation des protéines</term><term>Liaison aux 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The low molecular weight form of neurofilament, the neurofilament light protein, which serves as the core of the filament, was used as immunogen for generation of hybridomas with selective reactivity with this form of the filament. Six hybridomas, out of approximately 100 tested clones, were highly discriminatory. All involved epitopes were localized to the rod region of the antigen, as determined by alpha-chymotrypsin digestion of the purified filament and enzymatic peptide mapping. Synthetic peptides (20 mers) covering the entire rod region did not react with the antibodies. A phage display peptide library was used to identify four consensus sequences for the antibodies. The results indicate that all epitopes were of conformational type. Pair-wise BIAcore data furthermore indicated that the epitopes were independent. The access to such specific reagents is a prerequisite for further elucidation of the biology of the low molecular weight form of neurofilaments proteins.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11991817</PMID><DateCompleted><Year>2002</Year><Month>10</Month><Day>08</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1536-8599</ISSN><JournalIssue CitedMedium="Print"><Volume>21</Volume><Issue>1</Issue><PubDate><Year>2002</Year><Month>Feb</Month></PubDate></JournalIssue><Title>Hybridoma and hybridomics</Title><ISOAbbreviation>Hybrid. Hybridomics</ISOAbbreviation></Journal><ArticleTitle>Monoclonal antibodies selective for low molecular weight neurofilaments.</ArticleTitle><Pagination><MedlinePgn>53-9</MedlinePgn></Pagination><Abstract><AbstractText>Neurofilaments are necessary for the maintenance of axonal caliber and structural organization of nerve cells. The low molecular weight form of neurofilament, the neurofilament light protein, which serves as the core of the filament, was used as immunogen for generation of hybridomas with selective reactivity with this form of the filament. Six hybridomas, out of approximately 100 tested clones, were highly discriminatory. All involved epitopes were localized to the rod region of the antigen, as determined by alpha-chymotrypsin digestion of the purified filament and enzymatic peptide mapping. Synthetic peptides (20 mers) covering the entire rod region did not react with the antibodies. A phage display peptide library was used to identify four consensus sequences for the antibodies. The results indicate that all epitopes were of conformational type. Pair-wise BIAcore data furthermore indicated that the epitopes were independent. The access to such specific reagents is a prerequisite for further elucidation of the biology of the low molecular weight form of neurofilaments proteins.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Norgren</LastName><ForeName>Niklas</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Immunology, University of Umeå, S-90187 Umeå, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Karlsson</LastName><ForeName>Jan-Erik</ForeName><Initials>JE</Initials></Author><Author ValidYN="Y"><LastName>Rosengren</LastName><ForeName>Lars</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Stigbrand</LastName><ForeName>Torgny</ForeName><Initials>T</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Hybrid 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