Imaging mass spectrometry analysis of renal amyloidosis biopsies reveals protein co-localization with amyloid deposits.
Identifieur interne : 000254 ( PubMed/Checkpoint ); précédent : 000253; suivant : 000255Imaging mass spectrometry analysis of renal amyloidosis biopsies reveals protein co-localization with amyloid deposits.
Auteurs : Rita Casadonte [Allemagne] ; Mark Kriegsmann ; Sören-Oliver Deininger ; Kerstin Amann ; Rainer Paape ; Eckhard Belau ; Detlev Suckau ; Jens Fuchser ; Janine Beckmann ; Michael Becker ; Jörg KriegsmannSource :
- Analytical and bioanalytical chemistry [ 1618-2650 ] ; 2015.
English descriptors
- KwdEn :
- Amyloid (analysis), Amyloidosis (diagnosis), Amyloidosis (pathology), Apolipoproteins E (analysis), Humans, Immunoglobulin Light Chains (analysis), Kidney (pathology), Plaque, Amyloid (diagnosis), Plaque, Amyloid (pathology), Serum Amyloid A Protein (analysis), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Tandem Mass Spectrometry, Vitronectin (analysis).
- MESH :
- chemical , analysis : Amyloid, Apolipoproteins E, Immunoglobulin Light Chains, Serum Amyloid A Protein, Vitronectin.
- diagnosis : Amyloidosis, Plaque, Amyloid.
- pathology : Amyloidosis, Kidney, Plaque, Amyloid.
- Humans, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Tandem Mass Spectrometry.
Abstract
Amyloidosis is a heterogeneous group of protein misfolding diseases characterized by deposition of amyloid proteins. The kidney is frequently affected, especially by immunoglobulin light chain (AL) and serum amyloid A (SAA) amyloidosis as the most common subgroups. Current diagnosis relies on histopathological examination, Congo red staining, or electron microscopy. Subtyping is done by immunohistochemistry; however, commercially available antibodies lack specificity. The purpose of this study was to identify and map amyloid proteins in formalin-fixed paraffin-embedded tissue sections using matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis in an integrated workflow. Renal amyloidosis and non-amyloidosis biopsies were processed for histological and MS analysis. Mass spectra corresponding to the congophilic areas were directly linked to the histological and MS images for correlation studies. Peptides for SAA and AL were detected by MALDI IMS associated to Congo red-positive areas. Sequence determination of amyloid peptides by LC-MS/MS analysis provided protein distribution and identification. Serum amyloid P component, apolipoprotein E, and vitronectin proteins were identified in both AA and AL amyloidosis, showing a strong correlation with Congo red-positive regions. Our findings highlight the utility of MALDI IMS as a new method to type amyloidosis in histopathological routine material and characterize amyloid-associated proteins that may provide insights into the pathogenetic process of amyloid formation.
DOI: 10.1007/s00216-015-8689-z
PubMed: 25935672
Affiliations:
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first="Sören-Oliver" last="Deininger">Sören-Oliver Deininger</name></author><author><name sortKey="Amann, Kerstin" sort="Amann, Kerstin" uniqKey="Amann K" first="Kerstin" last="Amann">Kerstin Amann</name></author><author><name sortKey="Paape, Rainer" sort="Paape, Rainer" uniqKey="Paape R" first="Rainer" last="Paape">Rainer Paape</name></author><author><name sortKey="Belau, Eckhard" sort="Belau, Eckhard" uniqKey="Belau E" first="Eckhard" last="Belau">Eckhard Belau</name></author><author><name sortKey="Suckau, Detlev" sort="Suckau, Detlev" uniqKey="Suckau D" first="Detlev" last="Suckau">Detlev Suckau</name></author><author><name sortKey="Fuchser, Jens" sort="Fuchser, Jens" uniqKey="Fuchser J" first="Jens" last="Fuchser">Jens Fuchser</name></author><author><name sortKey="Beckmann, Janine" sort="Beckmann, Janine" uniqKey="Beckmann J" first="Janine" last="Beckmann">Janine Beckmann</name></author><author><name sortKey="Becker, Michael" sort="Becker, Michael" uniqKey="Becker M" first="Michael" last="Becker">Michael Becker</name></author><author><name sortKey="Kriegsmann, Jorg" sort="Kriegsmann, Jorg" uniqKey="Kriegsmann J" first="Jörg" last="Kriegsmann">Jörg Kriegsmann</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2015">2015</date><idno type="RBID">pubmed:25935672</idno><idno type="pmid">25935672</idno><idno type="doi">10.1007/s00216-015-8689-z</idno><idno type="wicri:Area/PubMed/Corpus">000248</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000248</idno><idno type="wicri:Area/PubMed/Curation">000248</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">000248</idno><idno type="wicri:Area/PubMed/Checkpoint">000248</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">000248</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Imaging mass spectrometry analysis of renal amyloidosis biopsies reveals protein co-localization with amyloid deposits.</title><author><name sortKey="Casadonte, Rita" sort="Casadonte, Rita" uniqKey="Casadonte R" first="Rita" last="Casadonte">Rita Casadonte</name><affiliation wicri:level="1"><nlm:affiliation>Proteopath GmbH, Max-Planck-Str. 17, 54296, Trier, Germany.</nlm:affiliation><country xml:lang="fr">Allemagne</country><wicri:regionArea>Proteopath GmbH, Max-Planck-Str. 17, 54296, Trier</wicri:regionArea><wicri:noRegion>54296, Trier</wicri:noRegion><wicri:noRegion>54296, Trier</wicri:noRegion><wicri:noRegion>Trier</wicri:noRegion></affiliation></author><author><name sortKey="Kriegsmann, Mark" sort="Kriegsmann, Mark" uniqKey="Kriegsmann M" first="Mark" last="Kriegsmann">Mark Kriegsmann</name></author><author><name sortKey="Deininger, Soren Oliver" sort="Deininger, Soren Oliver" uniqKey="Deininger S" first="Sören-Oliver" last="Deininger">Sören-Oliver Deininger</name></author><author><name sortKey="Amann, Kerstin" sort="Amann, Kerstin" uniqKey="Amann K" first="Kerstin" last="Amann">Kerstin Amann</name></author><author><name sortKey="Paape, Rainer" sort="Paape, Rainer" uniqKey="Paape R" first="Rainer" last="Paape">Rainer Paape</name></author><author><name sortKey="Belau, Eckhard" sort="Belau, Eckhard" uniqKey="Belau E" first="Eckhard" last="Belau">Eckhard Belau</name></author><author><name sortKey="Suckau, Detlev" sort="Suckau, Detlev" uniqKey="Suckau D" first="Detlev" last="Suckau">Detlev Suckau</name></author><author><name sortKey="Fuchser, Jens" sort="Fuchser, Jens" uniqKey="Fuchser J" first="Jens" last="Fuchser">Jens Fuchser</name></author><author><name sortKey="Beckmann, Janine" sort="Beckmann, Janine" uniqKey="Beckmann J" first="Janine" last="Beckmann">Janine Beckmann</name></author><author><name sortKey="Becker, Michael" sort="Becker, Michael" uniqKey="Becker M" first="Michael" last="Becker">Michael Becker</name></author><author><name sortKey="Kriegsmann, Jorg" sort="Kriegsmann, Jorg" uniqKey="Kriegsmann J" first="Jörg" last="Kriegsmann">Jörg Kriegsmann</name></author></analytic><series><title level="j">Analytical and bioanalytical chemistry</title><idno type="eISSN">1618-2650</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amyloid (analysis)</term><term>Amyloidosis (diagnosis)</term><term>Amyloidosis (pathology)</term><term>Apolipoproteins E (analysis)</term><term>Humans</term><term>Immunoglobulin Light Chains (analysis)</term><term>Kidney (pathology)</term><term>Plaque, Amyloid (diagnosis)</term><term>Plaque, Amyloid (pathology)</term><term>Serum Amyloid A Protein (analysis)</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term><term>Tandem Mass Spectrometry</term><term>Vitronectin (analysis)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Amyloid</term><term>Apolipoproteins E</term><term>Immunoglobulin Light Chains</term><term>Serum Amyloid A Protein</term><term>Vitronectin</term></keywords><keywords scheme="MESH" qualifier="diagnosis" xml:lang="en"><term>Amyloidosis</term><term>Plaque, Amyloid</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Amyloidosis</term><term>Kidney</term><term>Plaque, Amyloid</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term><term>Tandem Mass Spectrometry</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Amyloidosis is a heterogeneous group of protein misfolding diseases characterized by deposition of amyloid proteins. The kidney is frequently affected, especially by immunoglobulin light chain (AL) and serum amyloid A (SAA) amyloidosis as the most common subgroups. Current diagnosis relies on histopathological examination, Congo red staining, or electron microscopy. Subtyping is done by immunohistochemistry; however, commercially available antibodies lack specificity. The purpose of this study was to identify and map amyloid proteins in formalin-fixed paraffin-embedded tissue sections using matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis in an integrated workflow. Renal amyloidosis and non-amyloidosis biopsies were processed for histological and MS analysis. Mass spectra corresponding to the congophilic areas were directly linked to the histological and MS images for correlation studies. Peptides for SAA and AL were detected by MALDI IMS associated to Congo red-positive areas. Sequence determination of amyloid peptides by LC-MS/MS analysis provided protein distribution and identification. Serum amyloid P component, apolipoprotein E, and vitronectin proteins were identified in both AA and AL amyloidosis, showing a strong correlation with Congo red-positive regions. Our findings highlight the utility of MALDI IMS as a new method to type amyloidosis in histopathological routine material and characterize amyloid-associated proteins that may provide insights into the pathogenetic process of amyloid formation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25935672</PMID><DateCreated><Year>2015</Year><Month>06</Month><Day>24</Day></DateCreated><DateCompleted><Year>2016</Year><Month>03</Month><Day>18</Day></DateCompleted><DateRevised><Year>2016</Year><Month>05</Month><Day>12</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1618-2650</ISSN><JournalIssue CitedMedium="Internet"><Volume>407</Volume><Issue>18</Issue><PubDate><Year>2015</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Analytical and bioanalytical chemistry</Title><ISOAbbreviation>Anal Bioanal Chem</ISOAbbreviation></Journal><ArticleTitle>Imaging mass spectrometry analysis of renal amyloidosis biopsies reveals protein co-localization with amyloid deposits.</ArticleTitle><Pagination><MedlinePgn>5323-31</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00216-015-8689-z</ELocationID><Abstract><AbstractText>Amyloidosis is a heterogeneous group of protein misfolding diseases characterized by deposition of amyloid proteins. The kidney is frequently affected, especially by immunoglobulin light chain (AL) and serum amyloid A (SAA) amyloidosis as the most common subgroups. Current diagnosis relies on histopathological examination, Congo red staining, or electron microscopy. Subtyping is done by immunohistochemistry; however, commercially available antibodies lack specificity. The purpose of this study was to identify and map amyloid proteins in formalin-fixed paraffin-embedded tissue sections using matrix-assisted laser desorption/ionization imaging mass spectrometry (MALDI IMS) coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis in an integrated workflow. Renal amyloidosis and non-amyloidosis biopsies were processed for histological and MS analysis. Mass spectra corresponding to the congophilic areas were directly linked to the histological and MS images for correlation studies. Peptides for SAA and AL were detected by MALDI IMS associated to Congo red-positive areas. Sequence determination of amyloid peptides by LC-MS/MS analysis provided protein distribution and identification. Serum amyloid P component, apolipoprotein E, and vitronectin proteins were identified in both AA and AL amyloidosis, showing a strong correlation with Congo red-positive regions. Our findings highlight the utility of MALDI IMS as a new method to type amyloidosis in histopathological routine material and characterize amyloid-associated proteins that may provide insights into the pathogenetic process of amyloid formation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Casadonte</LastName><ForeName>Rita</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Proteopath GmbH, Max-Planck-Str. 17, 54296, Trier, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kriegsmann</LastName><ForeName>Mark</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Deininger</LastName><ForeName>Sören-Oliver</ForeName><Initials>SO</Initials></Author><Author ValidYN="Y"><LastName>Amann</LastName><ForeName>Kerstin</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Paape</LastName><ForeName>Rainer</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Belau</LastName><ForeName>Eckhard</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Suckau</LastName><ForeName>Detlev</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Fuchser</LastName><ForeName>Jens</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Beckmann</LastName><ForeName>Janine</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Becker</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Kriegsmann</LastName><ForeName>Jörg</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>05</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Anal Bioanal Chem</MedlineTA><NlmUniqueID>101134327</NlmUniqueID><ISSNLinking>1618-2642</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000682">Amyloid</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001057">Apolipoproteins E</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007147">Immunoglobulin Light Chains</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000685">Serum Amyloid A Protein</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D019096">Vitronectin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000682" MajorTopicYN="N">Amyloid</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="Y">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000686" MajorTopicYN="N">Amyloidosis</DescriptorName><QualifierName UI="Q000175" MajorTopicYN="N">diagnosis</QualifierName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001057" MajorTopicYN="N">Apolipoproteins E</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007147" MajorTopicYN="N">Immunoglobulin Light Chains</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007668" MajorTopicYN="N">Kidney</DescriptorName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D058225" MajorTopicYN="N">Plaque, Amyloid</DescriptorName><QualifierName UI="Q000175" MajorTopicYN="N">diagnosis</QualifierName><QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000685" MajorTopicYN="N">Serum Amyloid A Protein</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019032" MajorTopicYN="N">Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D053719" MajorTopicYN="N">Tandem Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019096" MajorTopicYN="N">Vitronectin</DescriptorName><QualifierName UI="Q000032" MajorTopicYN="N">analysis</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2015</Year><Month>03</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2015</Year><Month>04</Month><Day>09</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2015</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>5</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2015</Year><Month>5</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2016</Year><Month>3</Month><Day>19</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">25935672</ArticleId><ArticleId IdType="doi">10.1007/s00216-015-8689-z</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Allemagne</li></country></list><tree><noCountry><name sortKey="Amann, Kerstin" sort="Amann, Kerstin" uniqKey="Amann K" first="Kerstin" last="Amann">Kerstin Amann</name><name sortKey="Becker, Michael" sort="Becker, Michael" uniqKey="Becker M" first="Michael" last="Becker">Michael Becker</name><name sortKey="Beckmann, Janine" sort="Beckmann, Janine" uniqKey="Beckmann J" first="Janine" last="Beckmann">Janine Beckmann</name><name sortKey="Belau, Eckhard" sort="Belau, Eckhard" uniqKey="Belau E" first="Eckhard" last="Belau">Eckhard Belau</name><name sortKey="Deininger, Soren Oliver" sort="Deininger, Soren Oliver" uniqKey="Deininger S" first="Sören-Oliver" last="Deininger">Sören-Oliver Deininger</name><name sortKey="Fuchser, Jens" sort="Fuchser, Jens" uniqKey="Fuchser J" first="Jens" last="Fuchser">Jens Fuchser</name><name sortKey="Kriegsmann, Jorg" sort="Kriegsmann, Jorg" uniqKey="Kriegsmann J" first="Jörg" last="Kriegsmann">Jörg Kriegsmann</name><name sortKey="Kriegsmann, Mark" sort="Kriegsmann, Mark" uniqKey="Kriegsmann M" first="Mark" last="Kriegsmann">Mark Kriegsmann</name><name sortKey="Paape, Rainer" sort="Paape, Rainer" uniqKey="Paape R" first="Rainer" last="Paape">Rainer Paape</name><name sortKey="Suckau, Detlev" sort="Suckau, Detlev" uniqKey="Suckau D" first="Detlev" last="Suckau">Detlev Suckau</name></noCountry><country name="Allemagne"><noRegion><name sortKey="Casadonte, Rita" sort="Casadonte, Rita" uniqKey="Casadonte R" first="Rita" last="Casadonte">Rita Casadonte</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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