ChloroquineV1, Istex, Corpus, bibRecord, 002020

Immunotoxins

Identifieur interne : 002020 ( Istex/Corpus ); précédent : 002019; suivant : 002021

Immunotoxins

Auteurs : Oliver W. Press

Source :

Biotherapy [ 0921-299X ] ; 1991-01-01.

RBID : ISTEX:AAC720C9C73B4CA832F3DB749A3DE1FBEDFA3123

English descriptors

KwdEn :
- immunotherapy, immunotoxins, monoclonal antibodies, ricin, tumor immunology.
Teeft :
- Ammonium chloride, Antibody moiety, Antitumor effects, Biol chem, Blue sepharose, Bone marrow transplantation, Breast cancer, Cancer research, Cancer therapy, Casellas, Cell lymphomas, Cell surface, Chain conjugate, Chain immunotoxin, Clinical trials, Cytosol, Cytotoxic, Cytotoxic activity, Cytotoxic potency, Cytotoxicity, Deglycosylated ricin, Different epitopes, Diphtheria toxin, Disulfide, Disulfide bond, Endocytosis, Epitope, Experimental cell research, Free moab, Host disease, Hydrophobic regions, Immunol, Immunotoxin, Immunotoxin synthesis, Immunotoxins, Intact ricin, Intracellular, Irreversible inactivation, Jansen, Kinetic studies, Moab, Moabs, Moiety, Monoclonal, Monoclonal antibodies, Monoclonal antibody, Nude mouse model, Protein synthesis, Pseudomonas, Pseudomonas exotoxin, Rapid clearance, Reagent, Ribosome, Ricin, Ricin immunotoxin, Ricin immunotoxins, Similar rates, Toxin, Toxin moiety, Trans golgi reticulum, Translocation, Tumor cells, Tumor masses, Variable efficacy, Various concentrations, Vitetta, Vivo, Vivo efficacy, Vivo therapy.

Abstract

Abstract: Immunotoxins (ITs) are chimeric molecules constructed by covalently conjugating monoclonal antibodies (MoAbs) to plant or bacterial toxins (e.g. ricin or pseudomonas exotoxin). The antibody moiety allows specific targeting of ITs to tumor-associated antigens, while the toxin moiety is responsible for cell killing by irreversible inactivation of protein synthesis. Since ITs must reach the cytosol to kill cells, the rates of endocytosis, the pathways of intracellular routing, and the rates of translocation to the cytoplasm are important determinants of the efficacy of an IT. Promisingin vitro andin vivo IT results have been reported by many groups, and phase I clinical trials in cancer patients are currently underway.

Url:

https://api.istex.fr/ark:/67375/1BB-HVRBVGD2-D/fulltext.pdf

DOI: 10.1007/BF02175100

Links to Exploration step

ISTEX:AAC720C9C73B4CA832F3DB749A3DE1FBEDFA3123

Le document en format XML

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<ArticleTitle Language="En">Immunotoxins</ArticleTitle>
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<FamilyName>Press</FamilyName>
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<Affiliation ID="Aff1"><OrgDivision>Departments of Medicine and Biological Structure</OrgDivision>
<OrgName>University of Washington and the Fred Hutchinson Cancer Research Center</OrgName>
<OrgAddress><City>Seattle</City>
<State>WA</State>
<Country>USA</Country>
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<Country>USA</Country>
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<Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading>
<Para>Immunotoxins (ITs) are chimeric molecules constructed by covalently conjugating monoclonal antibodies (MoAbs) to plant or bacterial toxins (e.g. ricin or pseudomonas exotoxin). The antibody moiety allows specific targeting of ITs to tumor-associated antigens, while the toxin moiety is responsible for cell killing by irreversible inactivation of protein synthesis. Since ITs must reach the cytosol to kill cells, the rates of endocytosis, the pathways of intracellular routing, and the rates of translocation to the cytoplasm are important determinants of the efficacy of an IT. Promising<Emphasis Type="Italic">in vitro</Emphasis>
 and<Emphasis Type="Italic">in vivo</Emphasis>
 IT results have been reported by many groups, and phase I clinical trials in cancer patients are currently underway.</Para>
</Abstract>
<KeywordGroup Language="En"><Heading>Key words</Heading>
<Keyword>immunotherapy</Keyword>
<Keyword>immunotoxins</Keyword>
<Keyword>monoclonal antibodies</Keyword>
<Keyword>ricin</Keyword>
<Keyword>tumor immunology</Keyword>
</KeywordGroup>
<AbbreviationGroup><Heading>Abbreviations</Heading>
<DefinitionList><DefinitionListEntry><Term>dgA</Term>
<Description><Para>deglycosylated A-chain</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>GVHD</Term>
<Description><Para>graft versus host disease</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>HAMA</Term>
<Description><Para>human anti-mouse antibodies</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>2IT</Term>
<Description><Para>2-iminothiolane</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>IT</Term>
<Description><Para>immunotoxin</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>IT-A</Term>
<Description><Para>A-chain immunotoxin</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>IT-B</Term>
<Description><Para>B-chain immunotoxin</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>MoAb</Term>
<Description><Para>monoclonal antibody</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>RME</Term>
<Description><Para>receptor mediated endocytosis</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>SPDP</Term>
<Description><Para>N-succinimidyl-3-(2-pyridyldithio)-propionate</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>SMPT</Term>
<Description><Para>N-succinimidyl-oxycarbonyl-alpha-methyl-alpha-(2-pyridyldithio)-toluene</Para>
</Description>
</DefinitionListEntry>
<DefinitionListEntry><Term>SPDB</Term>
<Description><Para>N-succinimidyl-3-(2-pyridyldithio)-butyrate</Para>
</Description>
</DefinitionListEntry>
</DefinitionList>
</AbbreviationGroup>
<ArticleNote Type="Misc"><SimplePara>This research was supported in part by a First Independent Research and Training award from the National Institutes of Health (R29 CA 46134-03).</SimplePara>
</ArticleNote>
</ArticleHeader>
<NoBody></NoBody>
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</Issue>
</Volume>
</Journal>
</Publisher>
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<titleInfo type="alternative" contentType="CDATA"><title>Immunotoxins</title>
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<name type="personal" displayLabel="corresp"><namePart type="given">Oliver</namePart>
<namePart type="given">W.</namePart>
<namePart type="family">Press</namePart>
<affiliation>Departments of Medicine and Biological Structure, University of Washington and the Fred Hutchinson Cancer Research Center, Seattle, WA, USA</affiliation>
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<abstract lang="en">Abstract: Immunotoxins (ITs) are chimeric molecules constructed by covalently conjugating monoclonal antibodies (MoAbs) to plant or bacterial toxins (e.g. ricin or pseudomonas exotoxin). The antibody moiety allows specific targeting of ITs to tumor-associated antigens, while the toxin moiety is responsible for cell killing by irreversible inactivation of protein synthesis. Since ITs must reach the cytosol to kill cells, the rates of endocytosis, the pathways of intracellular routing, and the rates of translocation to the cytoplasm are important determinants of the efficacy of an IT. Promisingin vitro andin vivo IT results have been reported by many groups, and phase I clinical trials in cancer patients are currently underway.</abstract>
<subject lang="en"><genre>Key words</genre>
<topic>immunotherapy</topic>
<topic>immunotoxins</topic>
<topic>monoclonal antibodies</topic>
<topic>ricin</topic>
<topic>tumor immunology</topic>
</subject>
<subject><genre>Abbreviations</genre>
<topic>dgA : deglycosylated A-chain</topic>
<topic>GVHD : graft versus host disease</topic>
<topic>HAMA : human anti-mouse antibodies</topic>
<topic>2IT : 2-iminothiolane</topic>
<topic>IT : immunotoxin</topic>
<topic>IT-A : A-chain immunotoxin</topic>
<topic>IT-B : B-chain immunotoxin</topic>
<topic>MoAb : monoclonal antibody</topic>
<topic>RME : receptor mediated endocytosis</topic>
<topic>SPDP : N-succinimidyl-3-(2-pyridyldithio)-propionate</topic>
<topic>SMPT : N-succinimidyl-oxycarbonyl-alpha-methyl-alpha-(2-pyridyldithio)-toluene</topic>
<topic>SPDB : N-succinimidyl-3-(2-pyridyldithio)-butyrate</topic>
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<subject><genre>Medicine & Public Health</genre>
<topic>Immunology</topic>
<topic>Medical Microbiology</topic>
<topic>Hematology</topic>
<topic>Oncology</topic>
</subject>
<identifier type="ISSN">0921-299X</identifier>
<identifier type="eISSN">1573-8280</identifier>
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Immunotoxins

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