Single base oligodeoxyguanosine upregulates Fas ligand release by nonspecific cytotoxic cells.
Identifieur interne : 002387 ( PubMed/Curation ); précédent : 002386; suivant : 002388Single base oligodeoxyguanosine upregulates Fas ligand release by nonspecific cytotoxic cells.
Auteurs : Harjeet Kaur [États-Unis] ; Liliana Jaso-Friedmann ; Donald L. EvansSource :
- Developmental and comparative immunology [ 0145-305X ] ; 2004.
Descripteurs français
- KwdFr :
- ADN bactérien (génétique), ADN bactérien (immunologie), ADN bactérien (physiologie), Animaux, Apoptose (immunologie), Cellules HL-60, Cellules K562, Cytotoxicité immunologique (immunologie), Désoxyguanosine (immunologie), Femelle, Fragmentation de l'ADN (immunologie), Glycoprotéines membranaires (biosynthèse), Glycoprotéines membranaires (immunologie), Glycoprotéines membranaires (métabolisme), Humains, Ligand de Fas, Mâle, Oligonucléotides (immunologie), Poissons-chats (immunologie), Régulation positive.
- MESH :
- biosynthèse : Glycoprotéines membranaires.
- génétique : ADN bactérien.
- immunologie : ADN bactérien, Apoptose, Cytotoxicité immunologique, Désoxyguanosine, Fragmentation de l'ADN, Glycoprotéines membranaires, Oligonucléotides, Poissons-chats.
- métabolisme : Glycoprotéines membranaires.
- physiologie : ADN bactérien.
- Animaux, Cellules HL-60, Cellules K562, Femelle, Humains, Ligand de Fas, Mâle, Régulation positive.
English descriptors
- KwdEn :
- Animals, Apoptosis (immunology), Catfishes (immunology), Cytotoxicity, Immunologic (immunology), DNA Fragmentation (immunology), DNA, Bacterial (genetics), DNA, Bacterial (immunology), DNA, Bacterial (physiology), Deoxyguanosine (immunology), Fas Ligand Protein, Female, HL-60 Cells, Humans, K562 Cells, Male, Membrane Glycoproteins (biosynthesis), Membrane Glycoproteins (immunology), Membrane Glycoproteins (metabolism), Oligonucleotides (immunology), Up-Regulation, fas Receptor (immunology).
- MESH :
- chemical , biosynthesis : Membrane Glycoproteins.
- chemical , genetics : DNA, Bacterial.
- immunology : Apoptosis, Catfishes, Cytotoxicity, Immunologic, DNA Fragmentation, DNA, Bacterial, Deoxyguanosine, Membrane Glycoproteins, Oligonucleotides, fas Receptor.
- chemical , metabolism : Membrane Glycoproteins.
- chemical , physiology : DNA, Bacterial.
- Animals, Fas Ligand Protein, Female, HL-60 Cells, Humans, K562 Cells, Male, Up-Regulation.
Abstract
Nonspecific cytotoxic cells (NCC) are a type of teleost NK-like cell. In the present study a novel stimulus secretion model is described for catfish NCC utilizing single base oligodeoxyguanosine. Binding of guanosine 20-mers (dG20) to NCC up-regulated expression of cytosolic FasL detected by an anti-human FasL monoclonal antibody (mab). In vitro treatment of purified NCC with dG20 produced a 7-fold increase in expression of soluble Fas ligand (sFasL) after 3 h. Antibody binding to NCC was saturable and approximately 30-35% of total NCC were positive for sFasL expression. The teleost FasL equivalent produced programmed cell death of appropriate FasR positive targets. Supernatants from dG20 activated NCC produced hypoploidy and annexin-V binding by FasR bearing HL-60 cells. Treatment of activated supernatants with immobilized anti-FasL mab neutralized these activities. These studies demonstrated that an NK like cell (NCC) produces and secretes sFasL following binding by single base oligodeoxyguanosine.
DOI: 10.1016/j.dci.2003.09.015
PubMed: 15177111
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Evans</name></author></analytic><series><title level="j">Developmental and comparative immunology</title><idno type="ISSN">0145-305X</idno><imprint><date when="2004" type="published">2004</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Apoptosis (immunology)</term><term>Catfishes (immunology)</term><term>Cytotoxicity, Immunologic (immunology)</term><term>DNA Fragmentation (immunology)</term><term>DNA, Bacterial (genetics)</term><term>DNA, Bacterial (immunology)</term><term>DNA, Bacterial (physiology)</term><term>Deoxyguanosine (immunology)</term><term>Fas Ligand Protein</term><term>Female</term><term>HL-60 Cells</term><term>Humans</term><term>K562 Cells</term><term>Male</term><term>Membrane Glycoproteins (biosynthesis)</term><term>Membrane Glycoproteins (immunology)</term><term>Membrane Glycoproteins (metabolism)</term><term>Oligonucleotides (immunology)</term><term>Up-Regulation</term><term>fas Receptor (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN bactérien (génétique)</term><term>ADN bactérien (immunologie)</term><term>ADN bactérien (physiologie)</term><term>Animaux</term><term>Apoptose (immunologie)</term><term>Cellules HL-60</term><term>Cellules K562</term><term>Cytotoxicité immunologique (immunologie)</term><term>Désoxyguanosine (immunologie)</term><term>Femelle</term><term>Fragmentation de l'ADN (immunologie)</term><term>Glycoprotéines membranaires (biosynthèse)</term><term>Glycoprotéines membranaires (immunologie)</term><term>Glycoprotéines membranaires (métabolisme)</term><term>Humains</term><term>Ligand de Fas</term><term>Mâle</term><term>Oligonucléotides (immunologie)</term><term>Poissons-chats (immunologie)</term><term>Régulation positive</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Membrane Glycoproteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA, Bacterial</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Glycoprotéines membranaires</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>ADN bactérien</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>ADN bactérien</term><term>Apoptose</term><term>Cytotoxicité immunologique</term><term>Désoxyguanosine</term><term>Fragmentation de l'ADN</term><term>Glycoprotéines membranaires</term><term>Oligonucléotides</term><term>Poissons-chats</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Apoptosis</term><term>Catfishes</term><term>Cytotoxicity, Immunologic</term><term>DNA Fragmentation</term><term>DNA, Bacterial</term><term>Deoxyguanosine</term><term>Membrane Glycoproteins</term><term>Oligonucleotides</term><term>fas Receptor</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glycoprotéines membranaires</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>ADN bactérien</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>DNA, Bacterial</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Fas Ligand Protein</term><term>Female</term><term>HL-60 Cells</term><term>Humans</term><term>K562 Cells</term><term>Male</term><term>Up-Regulation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cellules HL-60</term><term>Cellules K562</term><term>Femelle</term><term>Humains</term><term>Ligand de Fas</term><term>Mâle</term><term>Régulation positive</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nonspecific cytotoxic cells (NCC) are a type of teleost NK-like cell. In the present study a novel stimulus secretion model is described for catfish NCC utilizing single base oligodeoxyguanosine. Binding of guanosine 20-mers (dG20) to NCC up-regulated expression of cytosolic FasL detected by an anti-human FasL monoclonal antibody (mab). In vitro treatment of purified NCC with dG20 produced a 7-fold increase in expression of soluble Fas ligand (sFasL) after 3 h. Antibody binding to NCC was saturable and approximately 30-35% of total NCC were positive for sFasL expression. The teleost FasL equivalent produced programmed cell death of appropriate FasR positive targets. Supernatants from dG20 activated NCC produced hypoploidy and annexin-V binding by FasR bearing HL-60 cells. Treatment of activated supernatants with immobilized anti-FasL mab neutralized these activities. These studies demonstrated that an NK like cell (NCC) produces and secretes sFasL following binding by single base oligodeoxyguanosine.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">15177111</PMID><DateCompleted><Year>2004</Year><Month>10</Month><Day>12</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0145-305X</ISSN><JournalIssue CitedMedium="Print"><Volume>28</Volume><Issue>6</Issue><PubDate><Year>2004</Year><Month>May</Month><Day>17</Day></PubDate></JournalIssue><Title>Developmental and comparative immunology</Title><ISOAbbreviation>Dev. Comp. Immunol.</ISOAbbreviation></Journal><ArticleTitle>Single base oligodeoxyguanosine upregulates Fas ligand release by nonspecific cytotoxic cells.</ArticleTitle><Pagination><MedlinePgn>571-9</MedlinePgn></Pagination><Abstract><AbstractText>Nonspecific cytotoxic cells (NCC) are a type of teleost NK-like cell. In the present study a novel stimulus secretion model is described for catfish NCC utilizing single base oligodeoxyguanosine. Binding of guanosine 20-mers (dG20) to NCC up-regulated expression of cytosolic FasL detected by an anti-human FasL monoclonal antibody (mab). In vitro treatment of purified NCC with dG20 produced a 7-fold increase in expression of soluble Fas ligand (sFasL) after 3 h. Antibody binding to NCC was saturable and approximately 30-35% of total NCC were positive for sFasL expression. The teleost FasL equivalent produced programmed cell death of appropriate FasR positive targets. Supernatants from dG20 activated NCC produced hypoploidy and annexin-V binding by FasR bearing HL-60 cells. Treatment of activated supernatants with immobilized anti-FasL mab neutralized these activities. These studies demonstrated that an NK like cell (NCC) produces and secretes sFasL following binding by single base oligodeoxyguanosine.</AbstractText><CopyrightInformation>Copyright 2003 Elsevier Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kaur</LastName><ForeName>Harjeet</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Chemical Engineering, North Carolina State University, Raleigh, NC, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jaso-Friedmann</LastName><ForeName>Liliana</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Evans</LastName><ForeName>Donald L</ForeName><Initials>DL</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Dev Comp Immunol</MedlineTA><NlmUniqueID>7708205</NlmUniqueID><ISSNLinking>0145-305X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004269">DNA, Bacterial</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C505661">FASLG protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D053222">Fas Ligand Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009841">Oligonucleotides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019014">fas Receptor</NameOfSubstance></Chemical><Chemical><RegistryNumber>G9481N71RO</RegistryNumber><NameOfSubstance UI="D003849">Deoxyguanosine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017209" MajorTopicYN="N">Apoptosis</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002397" MajorTopicYN="N">Catfishes</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D003602" MajorTopicYN="N">Cytotoxicity, Immunologic</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D053938" MajorTopicYN="N">DNA Fragmentation</DescriptorName><QualifierName UI="Q000276" 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MajorTopicYN="N">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2003</Year><Month>06</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2003</Year><Month>09</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2003</Year><Month>09</Month><Day>19</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2004</Year><Month>6</Month><Day>5</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>10</Month><Day>13</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2004</Year><Month>6</Month><Day>5</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">15177111</ArticleId><ArticleId IdType="doi">10.1016/j.dci.2003.09.015</ArticleId><ArticleId 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