Selective binding of nucleotide probes by eosinophilic cationic protein during in situ hybridisation.
Identifieur interne : 002477 ( PubMed/Corpus ); précédent : 002476; suivant : 002478Selective binding of nucleotide probes by eosinophilic cationic protein during in situ hybridisation.
Auteurs : Richard D. Ellis ; Paul Ashwood ; Jonathan J. Powell ; Paul D. Taylor ; Richard Poulsom ; Richard P H. Thompson ; Neville A. PunchardSource :
- The Histochemical journal [ 0018-2214 ]
English descriptors
- KwdEn :
- Antisense Elements (Genetics), Autoradiography, Blood Proteins (metabolism), Chromatography, High Pressure Liquid, Colon (metabolism), Colon (pathology), Colonic Polyps (metabolism), Colonic Polyps (pathology), Coloring Agents, Crohn Disease (metabolism), Crohn Disease (pathology), DNA Probes, Dithiothreitol, Eosinophil Granule Proteins, Eosinophils (metabolism), Exons, Humans, In Situ Hybridization, NF-kappa B (drug effects), NF-kappa B (metabolism), Nucleotides (metabolism), Paraffin Embedding, RNA, Messenger (biosynthesis), Ribonucleases, Sulfhydryl Reagents, Tumor Necrosis Factor-alpha (metabolism).
- MESH :
- chemical , biosynthesis : RNA, Messenger.
- chemical , drug effects : NF-kappa B.
- chemical , metabolism : Blood Proteins, NF-kappa B, Nucleotides, Tumor Necrosis Factor-alpha.
- chemical : Antisense Elements (Genetics), Coloring Agents, DNA Probes, Dithiothreitol, Eosinophil Granule Proteins, Ribonucleases, Sulfhydryl Reagents.
- metabolism : Colon, Colonic Polyps, Crohn Disease, Eosinophils.
- pathology : Colon, Colonic Polyps, Crohn Disease.
- Autoradiography, Chromatography, High Pressure Liquid, Exons, Humans, In Situ Hybridization, Paraffin Embedding.
Abstract
During in situ hybridisation on frozen and paraffin-embedded sections of bowel for IkappaB alpha, oligodeoxyribonucleotide probes were found to bind more avidly to eosinophils than target mRNA. This binding could not be obviated using strategies previously employed to block either binding of long DNA probes (200-mers) to eosinophils in bone marrow smears, or of riboprobes to eosinophils in sections of bowel, without removing specific hybridisation of probes. That this binding could arise through interaction of anionic oligodeoxyribonucleotides with eosinophil cationic protein, which has an unusually high pI, and is abundant in cytoplasmic granules of eosinophils, was demonstrated in vitro using real-time biomolecular interaction analysis with a BiacoreX instrument. Finally, a relationship between probe hydrophobicity, measured by reverse phase ion-pair high performance liquid chromatography, and in situ binding of individual probes to eosinophils was demonstrated. Effective tissue penetration by hydrophobic probes and subsequent strong probe-eosinophilic cationic protein interactions therefore may confound the interpretation of in situ hybridisation performed with oligonucleotide probes in eosinophil-containing tissues, such as bowel and nasal polyps.
DOI: 10.1023/a:1020942531028
PubMed: 12495221
Links to Exploration step
pubmed:12495221Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Selective binding of nucleotide probes by eosinophilic cationic protein during in situ hybridisation.</title><author><name sortKey="Ellis, Richard D" sort="Ellis, Richard D" uniqKey="Ellis R" first="Richard D" last="Ellis">Richard D. Ellis</name><affiliation><nlm:affiliation>Gastrointestinal Laboratory, The Rayne Institute, St. Thomas' Hospital, London, SE1 7EH, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Ashwood, Paul" sort="Ashwood, Paul" uniqKey="Ashwood P" first="Paul" last="Ashwood">Paul Ashwood</name></author><author><name sortKey="Powell, Jonathan J" sort="Powell, Jonathan J" uniqKey="Powell J" first="Jonathan J" last="Powell">Jonathan J. Powell</name></author><author><name sortKey="Taylor, Paul D" sort="Taylor, Paul D" uniqKey="Taylor P" first="Paul D" last="Taylor">Paul D. Taylor</name></author><author><name sortKey="Poulsom, Richard" sort="Poulsom, Richard" uniqKey="Poulsom R" first="Richard" last="Poulsom">Richard Poulsom</name></author><author><name sortKey="Thompson, Richard P H" sort="Thompson, Richard P H" uniqKey="Thompson R" first="Richard P H" last="Thompson">Richard P H. Thompson</name></author><author><name sortKey="Punchard, Neville A" sort="Punchard, Neville A" uniqKey="Punchard N" first="Neville A" last="Punchard">Neville A. Punchard</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="????"><PubDate><MedlineDate>2002 Mar-Apr</MedlineDate></PubDate></date><idno type="RBID">pubmed:12495221</idno><idno type="pmid">12495221</idno><idno type="doi">10.1023/a:1020942531028</idno><idno type="wicri:Area/PubMed/Corpus">002477</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002477</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Selective binding of nucleotide probes by eosinophilic cationic protein during in situ hybridisation.</title><author><name sortKey="Ellis, Richard D" sort="Ellis, Richard D" uniqKey="Ellis R" first="Richard D" last="Ellis">Richard D. Ellis</name><affiliation><nlm:affiliation>Gastrointestinal Laboratory, The Rayne Institute, St. Thomas' Hospital, London, SE1 7EH, UK.</nlm:affiliation></affiliation></author><author><name sortKey="Ashwood, Paul" sort="Ashwood, Paul" uniqKey="Ashwood P" first="Paul" last="Ashwood">Paul Ashwood</name></author><author><name sortKey="Powell, Jonathan J" sort="Powell, Jonathan J" uniqKey="Powell J" first="Jonathan J" last="Powell">Jonathan J. Powell</name></author><author><name sortKey="Taylor, Paul D" sort="Taylor, Paul D" uniqKey="Taylor P" first="Paul D" last="Taylor">Paul D. Taylor</name></author><author><name sortKey="Poulsom, Richard" sort="Poulsom, Richard" uniqKey="Poulsom R" first="Richard" last="Poulsom">Richard Poulsom</name></author><author><name sortKey="Thompson, Richard P H" sort="Thompson, Richard P H" uniqKey="Thompson R" first="Richard P H" last="Thompson">Richard P H. Thompson</name></author><author><name sortKey="Punchard, Neville A" sort="Punchard, Neville A" uniqKey="Punchard N" first="Neville A" last="Punchard">Neville A. Punchard</name></author></analytic><series><title level="j">The Histochemical journal</title><idno type="ISSN">0018-2214</idno></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antisense Elements (Genetics)</term><term>Autoradiography</term><term>Blood Proteins (metabolism)</term><term>Chromatography, High Pressure Liquid</term><term>Colon (metabolism)</term><term>Colon (pathology)</term><term>Colonic Polyps (metabolism)</term><term>Colonic Polyps (pathology)</term><term>Coloring Agents</term><term>Crohn Disease (metabolism)</term><term>Crohn Disease (pathology)</term><term>DNA Probes</term><term>Dithiothreitol</term><term>Eosinophil Granule Proteins</term><term>Eosinophils (metabolism)</term><term>Exons</term><term>Humans</term><term>In Situ Hybridization</term><term>NF-kappa B (drug effects)</term><term>NF-kappa B (metabolism)</term><term>Nucleotides (metabolism)</term><term>Paraffin Embedding</term><term>RNA, Messenger (biosynthesis)</term><term>Ribonucleases</term><term>Sulfhydryl Reagents</term><term>Tumor Necrosis Factor-alpha (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="drug effects" xml:lang="en"><term>NF-kappa B</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Blood Proteins</term><term>NF-kappa B</term><term>Nucleotides</term><term>Tumor Necrosis Factor-alpha</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antisense Elements (Genetics)</term><term>Coloring Agents</term><term>DNA Probes</term><term>Dithiothreitol</term><term>Eosinophil Granule Proteins</term><term>Ribonucleases</term><term>Sulfhydryl Reagents</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Colon</term><term>Colonic Polyps</term><term>Crohn Disease</term><term>Eosinophils</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Colon</term><term>Colonic Polyps</term><term>Crohn Disease</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Autoradiography</term><term>Chromatography, High Pressure Liquid</term><term>Exons</term><term>Humans</term><term>In Situ Hybridization</term><term>Paraffin Embedding</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">During in situ hybridisation on frozen and paraffin-embedded sections of bowel for IkappaB alpha, oligodeoxyribonucleotide probes were found to bind more avidly to eosinophils than target mRNA. This binding could not be obviated using strategies previously employed to block either binding of long DNA probes (200-mers) to eosinophils in bone marrow smears, or of riboprobes to eosinophils in sections of bowel, without removing specific hybridisation of probes. That this binding could arise through interaction of anionic oligodeoxyribonucleotides with eosinophil cationic protein, which has an unusually high pI, and is abundant in cytoplasmic granules of eosinophils, was demonstrated in vitro using real-time biomolecular interaction analysis with a BiacoreX instrument. Finally, a relationship between probe hydrophobicity, measured by reverse phase ion-pair high performance liquid chromatography, and in situ binding of individual probes to eosinophils was demonstrated. Effective tissue penetration by hydrophobic probes and subsequent strong probe-eosinophilic cationic protein interactions therefore may confound the interpretation of in situ hybridisation performed with oligonucleotide probes in eosinophil-containing tissues, such as bowel and nasal polyps.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12495221</PMID><DateCompleted><Year>2003</Year><Month>05</Month><Day>21</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0018-2214</ISSN><JournalIssue CitedMedium="Print"><Volume>34</Volume><Issue>3-4</Issue><PubDate><MedlineDate>2002 Mar-Apr</MedlineDate></PubDate></JournalIssue><Title>The Histochemical journal</Title><ISOAbbreviation>Histochem. J.</ISOAbbreviation></Journal><ArticleTitle>Selective binding of nucleotide probes by eosinophilic cationic protein during in situ hybridisation.</ArticleTitle><Pagination><MedlinePgn>153-60</MedlinePgn></Pagination><Abstract><AbstractText>During in situ hybridisation on frozen and paraffin-embedded sections of bowel for IkappaB alpha, oligodeoxyribonucleotide probes were found to bind more avidly to eosinophils than target mRNA. This binding could not be obviated using strategies previously employed to block either binding of long DNA probes (200-mers) to eosinophils in bone marrow smears, or of riboprobes to eosinophils in sections of bowel, without removing specific hybridisation of probes. That this binding could arise through interaction of anionic oligodeoxyribonucleotides with eosinophil cationic protein, which has an unusually high pI, and is abundant in cytoplasmic granules of eosinophils, was demonstrated in vitro using real-time biomolecular interaction analysis with a BiacoreX instrument. Finally, a relationship between probe hydrophobicity, measured by reverse phase ion-pair high performance liquid chromatography, and in situ binding of individual probes to eosinophils was demonstrated. Effective tissue penetration by hydrophobic probes and subsequent strong probe-eosinophilic cationic protein interactions therefore may confound the interpretation of in situ hybridisation performed with oligonucleotide probes in eosinophil-containing tissues, such as bowel and nasal polyps.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ellis</LastName><ForeName>Richard D</ForeName><Initials>RD</Initials><AffiliationInfo><Affiliation>Gastrointestinal Laboratory, The Rayne Institute, St. Thomas' Hospital, London, SE1 7EH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ashwood</LastName><ForeName>Paul</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Powell</LastName><ForeName>Jonathan J</ForeName><Initials>JJ</Initials></Author><Author ValidYN="Y"><LastName>Taylor</LastName><ForeName>Paul D</ForeName><Initials>PD</Initials></Author><Author ValidYN="Y"><LastName>Poulsom</LastName><ForeName>Richard</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Thompson</LastName><ForeName>Richard P H</ForeName><Initials>RP</Initials></Author><Author ValidYN="Y"><LastName>Punchard</LastName><ForeName>Neville A</ForeName><Initials>NA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Histochem J</MedlineTA><NlmUniqueID>0163161</NlmUniqueID><ISSNLinking>0018-2214</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D016375">Antisense Elements (Genetics)</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001798">Blood 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