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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pubmed:15177111Le document en format XML
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<author><name sortKey="Jaso Friedmann, Liliana" sort="Jaso Friedmann, Liliana" uniqKey="Jaso Friedmann L" first="Liliana" last="Jaso-Friedmann">Liliana Jaso-Friedmann</name>
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<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>
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<term>Membrane Glycoproteins (immunology)</term>
<term>Membrane Glycoproteins (metabolism)</term>
<term>Oligonucleotides (immunology)</term>
<term>Up-Regulation</term>
<term>fas Receptor (immunology)</term>
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<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>
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<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>
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<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>
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<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>
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<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>
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<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>
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<term>Cellules HL-60</term>
<term>Cellules K562</term>
<term>Femelle</term>
<term>Humains</term>
<term>Ligand de Fas</term>
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<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>
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<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>
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