Quantitative determination of human IgA subclasses and their Fc‐glycosylation patterns in plasma by using a peptide analogue internal standard and ultra‐high‐performance liquid chromatography/triple quadrupole mass spectrometry
Rationale Glycosylation on immunoglobulins is important for the immune function. In this study, we developed and validated a method for the absolute quantification of IgA subclasses and relative quantification of IgA‐Fc glycopeptides by using affinity purification and ultrahigh‐performance liquid ch...
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| Veröffentlicht in: | Rapid communications in mass spectrometry 2020-04, Vol.34 (S1), p.e8606-n/a |
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| creator | Chen, Hsiao‐Fan Shiao, Ching‐Ya Wu, Mei‐Yi Lin, Yen‐Chung Chen, Hsi‐Hsien Chang, Wei‐Chiao Wu, Mai‐Szu Kao, Chih‐Chin Tsai, I‐Lin |
| description | Rationale
Glycosylation on immunoglobulins is important for the immune function. In this study, we developed and validated a method for the absolute quantification of IgA subclasses and relative quantification of IgA‐Fc glycopeptides by using affinity purification and ultrahigh‐performance liquid chromatography/tandem mass spectrometry (UHPLC/MS/MS). Only micro‐volumes of plasma were required from each sample and we also applied the method to discover IgA and IgA‐glycopeptide profiles in patients with chronic kidney diseases and IgA nephropathy.
Methods
Peptide M affinity beads were used to purify IgA, and a cost‐effective peptide analogue was added as internal standard. With an efficient on‐bead digestion process, purified samples were analyzed by UHPLC/MS/MS in multiple reaction monitoring mode.
Results
Correlation coefficients were greater than 0.999 for the IgA1 and IgA2 calibration curves and greater than 0.994 for glycopeptide regression curves. Intraday and interday precisions for IgA1 and IgA2 were |
| doi_str_mv | 10.1002/rcm.8606 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_2313360594</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2313360594</sourcerecordid><originalsourceid>FETCH-LOGICAL-c3836-d3ba8334dfa53bcc87390c7bdd4a8f1af9765226560a7ee41452c21b69d87eb63</originalsourceid><addsrcrecordid>eNp1kd9q1UAQh4Mo9lgFn0AWvPEm7W422SSXpVgtVETR6zDZnSRbNtmc_aPkzkfwGb3zLdzTUxUEr2YGvvkY5pdlzxk9Y5QW507OZ42g4kG2Y7Stc1pw9jDb0bZiecna5iR74v0tpYxVBX2cnXBW06qqxS77-SHCEnSAoL8gURjQzXpJk12IHcgUZ1jI9XhBfOylAe_RE1gUCRNqR67kj2_fR7NJ6zdzXFohJMfiiU59WpiB9BuJXi8jAbLiGrTCpABjx4iJOtBgiA9JC07d2aMJDpJ60uOUyopusC5dIpEYvY9aETk5O0Owo4N12s6D06tBso-gXFxtaud0K_ErypBADG57mj0awHh8dl9Ps89Xrz9dvs1v3r-5vry4ySVvuMgV76HhvFQDVLyXsql5S2XdK1VCMzAY2lpURSEqQaFGLFlZFbJgvWhVU2Mv-Gn26uhdnd1H9KGbtZdoDCxoo-9SNJwLWrVlQl_-g97aePjGgWrKUtBaNH-F0lnvHQ7d6vQMbusY7Q7xdyn-7hB_Ql_cC2M_o_oD_s47AfkR-KoNbv8VdR8v390JfwEHWcOb</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2384460768</pqid></control><display><type>article</type><title>Quantitative determination of human IgA subclasses and their Fc‐glycosylation patterns in plasma by using a peptide analogue internal standard and ultra‐high‐performance liquid chromatography/triple quadrupole mass spectrometry</title><source>Wiley Online Library - AutoHoldings Journals</source><source>MEDLINE</source><creator>Chen, Hsiao‐Fan ; Shiao, Ching‐Ya ; Wu, Mei‐Yi ; Lin, Yen‐Chung ; Chen, Hsi‐Hsien ; Chang, Wei‐Chiao ; Wu, Mai‐Szu ; Kao, Chih‐Chin ; Tsai, I‐Lin</creator><creatorcontrib>Chen, Hsiao‐Fan ; Shiao, Ching‐Ya ; Wu, Mei‐Yi ; Lin, Yen‐Chung ; Chen, Hsi‐Hsien ; Chang, Wei‐Chiao ; Wu, Mai‐Szu ; Kao, Chih‐Chin ; Tsai, I‐Lin</creatorcontrib><description>Rationale
Glycosylation on immunoglobulins is important for the immune function. In this study, we developed and validated a method for the absolute quantification of IgA subclasses and relative quantification of IgA‐Fc glycopeptides by using affinity purification and ultrahigh‐performance liquid chromatography/tandem mass spectrometry (UHPLC/MS/MS). Only micro‐volumes of plasma were required from each sample and we also applied the method to discover IgA and IgA‐glycopeptide profiles in patients with chronic kidney diseases and IgA nephropathy.
Methods
Peptide M affinity beads were used to purify IgA, and a cost‐effective peptide analogue was added as internal standard. With an efficient on‐bead digestion process, purified samples were analyzed by UHPLC/MS/MS in multiple reaction monitoring mode.
Results
Correlation coefficients were greater than 0.999 for the IgA1 and IgA2 calibration curves and greater than 0.994 for glycopeptide regression curves. Intraday and interday precisions for IgA1 and IgA2 were <1.6% and <5.1% RSD, respectively. Intraday and interday accuracies ranged from 102.6 to 114.9% and 103.5 to 113.5% for IgA1 and IgA2, respectively. Stabilities of IgA1 and IgA2 at −80°C for 7 to 15 days ranged from 96.0 to 109.4%, respectively. The Pearson's correlation coefficient was 0.916 when comparing the IgA quantification results of the 30 clinical samples by using ELISAs and the developed UHPLC/MS/MS method. Compared with healthy controls, IgA and IgA‐glycopeptides showed different profiles in patients with chronic kidney diseases and IgA nephropathy.
Conclusions
The developed method showed good validation results, and the absolute quantification results of IgA correlated with those from ELISA. The pilot application study showed that IgA and IgA‐glycopeptides can be potential biomarker candidates for kidney diseases, and more clinical sample applications are worth investigating.</description><identifier>ISSN: 0951-4198</identifier><identifier>EISSN: 1097-0231</identifier><identifier>DOI: 10.1002/rcm.8606</identifier><identifier>PMID: 31705576</identifier><language>eng</language><publisher>England: Wiley Subscription Services, Inc</publisher><subject>Affinity ; Beads ; Biomarkers ; Chromatography ; Chromatography, High Pressure Liquid - methods ; Chromatography, High Pressure Liquid - standards ; Correlation coefficients ; Glycopeptides ; Glycosylation ; Humans ; Immunoglobulin A - analysis ; Immunoglobulin A - blood ; Immunoglobulin Fc Fragments - analysis ; Immunoglobulin Fc Fragments - blood ; Immunoglobulins ; Kidney diseases ; Limit of Detection ; Liquid chromatography ; Mass spectrometry ; Peptides ; Quadrupoles ; Quality Control ; Reference Standards ; Regression analysis ; Scientific imaging ; Spectroscopy ; Tandem Mass Spectrometry - methods ; Tandem Mass Spectrometry - standards</subject><ispartof>Rapid communications in mass spectrometry, 2020-04, Vol.34 (S1), p.e8606-n/a</ispartof><rights>2019 John Wiley & Sons, Ltd.</rights><rights>2020 John Wiley & Sons, Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3836-d3ba8334dfa53bcc87390c7bdd4a8f1af9765226560a7ee41452c21b69d87eb63</citedby><cites>FETCH-LOGICAL-c3836-d3ba8334dfa53bcc87390c7bdd4a8f1af9765226560a7ee41452c21b69d87eb63</cites><orcidid>0000-0002-3951-5197 ; 0000-0003-3194-2204</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Frcm.8606$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Frcm.8606$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31705576$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, Hsiao‐Fan</creatorcontrib><creatorcontrib>Shiao, Ching‐Ya</creatorcontrib><creatorcontrib>Wu, Mei‐Yi</creatorcontrib><creatorcontrib>Lin, Yen‐Chung</creatorcontrib><creatorcontrib>Chen, Hsi‐Hsien</creatorcontrib><creatorcontrib>Chang, Wei‐Chiao</creatorcontrib><creatorcontrib>Wu, Mai‐Szu</creatorcontrib><creatorcontrib>Kao, Chih‐Chin</creatorcontrib><creatorcontrib>Tsai, I‐Lin</creatorcontrib><title>Quantitative determination of human IgA subclasses and their Fc‐glycosylation patterns in plasma by using a peptide analogue internal standard and ultra‐high‐performance liquid chromatography/triple quadrupole mass spectrometry</title><title>Rapid communications in mass spectrometry</title><addtitle>Rapid Commun Mass Spectrom</addtitle><description>Rationale
Glycosylation on immunoglobulins is important for the immune function. In this study, we developed and validated a method for the absolute quantification of IgA subclasses and relative quantification of IgA‐Fc glycopeptides by using affinity purification and ultrahigh‐performance liquid chromatography/tandem mass spectrometry (UHPLC/MS/MS). Only micro‐volumes of plasma were required from each sample and we also applied the method to discover IgA and IgA‐glycopeptide profiles in patients with chronic kidney diseases and IgA nephropathy.
Methods
Peptide M affinity beads were used to purify IgA, and a cost‐effective peptide analogue was added as internal standard. With an efficient on‐bead digestion process, purified samples were analyzed by UHPLC/MS/MS in multiple reaction monitoring mode.
Results
Correlation coefficients were greater than 0.999 for the IgA1 and IgA2 calibration curves and greater than 0.994 for glycopeptide regression curves. Intraday and interday precisions for IgA1 and IgA2 were <1.6% and <5.1% RSD, respectively. Intraday and interday accuracies ranged from 102.6 to 114.9% and 103.5 to 113.5% for IgA1 and IgA2, respectively. Stabilities of IgA1 and IgA2 at −80°C for 7 to 15 days ranged from 96.0 to 109.4%, respectively. The Pearson's correlation coefficient was 0.916 when comparing the IgA quantification results of the 30 clinical samples by using ELISAs and the developed UHPLC/MS/MS method. Compared with healthy controls, IgA and IgA‐glycopeptides showed different profiles in patients with chronic kidney diseases and IgA nephropathy.
Conclusions
The developed method showed good validation results, and the absolute quantification results of IgA correlated with those from ELISA. The pilot application study showed that IgA and IgA‐glycopeptides can be potential biomarker candidates for kidney diseases, and more clinical sample applications are worth investigating.</description><subject>Affinity</subject><subject>Beads</subject><subject>Biomarkers</subject><subject>Chromatography</subject><subject>Chromatography, High Pressure Liquid - methods</subject><subject>Chromatography, High Pressure Liquid - standards</subject><subject>Correlation coefficients</subject><subject>Glycopeptides</subject><subject>Glycosylation</subject><subject>Humans</subject><subject>Immunoglobulin A - analysis</subject><subject>Immunoglobulin A - blood</subject><subject>Immunoglobulin Fc Fragments - analysis</subject><subject>Immunoglobulin Fc Fragments - blood</subject><subject>Immunoglobulins</subject><subject>Kidney diseases</subject><subject>Limit of Detection</subject><subject>Liquid chromatography</subject><subject>Mass spectrometry</subject><subject>Peptides</subject><subject>Quadrupoles</subject><subject>Quality Control</subject><subject>Reference Standards</subject><subject>Regression analysis</subject><subject>Scientific imaging</subject><subject>Spectroscopy</subject><subject>Tandem Mass Spectrometry - methods</subject><subject>Tandem Mass Spectrometry - standards</subject><issn>0951-4198</issn><issn>1097-0231</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2020</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kd9q1UAQh4Mo9lgFn0AWvPEm7W422SSXpVgtVETR6zDZnSRbNtmc_aPkzkfwGb3zLdzTUxUEr2YGvvkY5pdlzxk9Y5QW507OZ42g4kG2Y7Stc1pw9jDb0bZiecna5iR74v0tpYxVBX2cnXBW06qqxS77-SHCEnSAoL8gURjQzXpJk12IHcgUZ1jI9XhBfOylAe_RE1gUCRNqR67kj2_fR7NJ6zdzXFohJMfiiU59WpiB9BuJXi8jAbLiGrTCpABjx4iJOtBgiA9JC07d2aMJDpJ60uOUyopusC5dIpEYvY9aETk5O0Owo4N12s6D06tBso-gXFxtaud0K_ErypBADG57mj0awHh8dl9Ps89Xrz9dvs1v3r-5vry4ySVvuMgV76HhvFQDVLyXsql5S2XdK1VCMzAY2lpURSEqQaFGLFlZFbJgvWhVU2Mv-Gn26uhdnd1H9KGbtZdoDCxoo-9SNJwLWrVlQl_-g97aePjGgWrKUtBaNH-F0lnvHQ7d6vQMbusY7Q7xdyn-7hB_Ql_cC2M_o_oD_s47AfkR-KoNbv8VdR8v390JfwEHWcOb</recordid><startdate>202004</startdate><enddate>202004</enddate><creator>Chen, Hsiao‐Fan</creator><creator>Shiao, Ching‐Ya</creator><creator>Wu, Mei‐Yi</creator><creator>Lin, Yen‐Chung</creator><creator>Chen, Hsi‐Hsien</creator><creator>Chang, Wei‐Chiao</creator><creator>Wu, Mai‐Szu</creator><creator>Kao, Chih‐Chin</creator><creator>Tsai, I‐Lin</creator><general>Wiley Subscription Services, Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7SR</scope><scope>7U5</scope><scope>8BQ</scope><scope>8FD</scope><scope>JG9</scope><scope>JQ2</scope><scope>L7M</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0002-3951-5197</orcidid><orcidid>https://orcid.org/0000-0003-3194-2204</orcidid></search><sort><creationdate>202004</creationdate><title>Quantitative determination of human IgA subclasses and their Fc‐glycosylation patterns in plasma by using a peptide analogue internal standard and ultra‐high‐performance liquid chromatography/triple quadrupole mass spectrometry</title><author>Chen, Hsiao‐Fan ; Shiao, Ching‐Ya ; Wu, Mei‐Yi ; Lin, Yen‐Chung ; Chen, Hsi‐Hsien ; Chang, Wei‐Chiao ; Wu, Mai‐Szu ; Kao, Chih‐Chin ; Tsai, I‐Lin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3836-d3ba8334dfa53bcc87390c7bdd4a8f1af9765226560a7ee41452c21b69d87eb63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2020</creationdate><topic>Affinity</topic><topic>Beads</topic><topic>Biomarkers</topic><topic>Chromatography</topic><topic>Chromatography, High Pressure Liquid - methods</topic><topic>Chromatography, High Pressure Liquid - standards</topic><topic>Correlation coefficients</topic><topic>Glycopeptides</topic><topic>Glycosylation</topic><topic>Humans</topic><topic>Immunoglobulin A - analysis</topic><topic>Immunoglobulin A - blood</topic><topic>Immunoglobulin Fc Fragments - analysis</topic><topic>Immunoglobulin Fc Fragments - blood</topic><topic>Immunoglobulins</topic><topic>Kidney diseases</topic><topic>Limit of Detection</topic><topic>Liquid chromatography</topic><topic>Mass spectrometry</topic><topic>Peptides</topic><topic>Quadrupoles</topic><topic>Quality Control</topic><topic>Reference Standards</topic><topic>Regression analysis</topic><topic>Scientific imaging</topic><topic>Spectroscopy</topic><topic>Tandem Mass Spectrometry - methods</topic><topic>Tandem Mass Spectrometry - standards</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chen, Hsiao‐Fan</creatorcontrib><creatorcontrib>Shiao, Ching‐Ya</creatorcontrib><creatorcontrib>Wu, Mei‐Yi</creatorcontrib><creatorcontrib>Lin, Yen‐Chung</creatorcontrib><creatorcontrib>Chen, Hsi‐Hsien</creatorcontrib><creatorcontrib>Chang, Wei‐Chiao</creatorcontrib><creatorcontrib>Wu, Mai‐Szu</creatorcontrib><creatorcontrib>Kao, Chih‐Chin</creatorcontrib><creatorcontrib>Tsai, I‐Lin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Engineered Materials Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>Technology Research Database</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</collection><jtitle>Rapid communications in mass spectrometry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chen, Hsiao‐Fan</au><au>Shiao, Ching‐Ya</au><au>Wu, Mei‐Yi</au><au>Lin, Yen‐Chung</au><au>Chen, Hsi‐Hsien</au><au>Chang, Wei‐Chiao</au><au>Wu, Mai‐Szu</au><au>Kao, Chih‐Chin</au><au>Tsai, I‐Lin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Quantitative determination of human IgA subclasses and their Fc‐glycosylation patterns in plasma by using a peptide analogue internal standard and ultra‐high‐performance liquid chromatography/triple quadrupole mass spectrometry</atitle><jtitle>Rapid communications in mass spectrometry</jtitle><addtitle>Rapid Commun Mass Spectrom</addtitle><date>2020-04</date><risdate>2020</risdate><volume>34</volume><issue>S1</issue><spage>e8606</spage><epage>n/a</epage><pages>e8606-n/a</pages><issn>0951-4198</issn><eissn>1097-0231</eissn><abstract>Rationale
Glycosylation on immunoglobulins is important for the immune function. In this study, we developed and validated a method for the absolute quantification of IgA subclasses and relative quantification of IgA‐Fc glycopeptides by using affinity purification and ultrahigh‐performance liquid chromatography/tandem mass spectrometry (UHPLC/MS/MS). Only micro‐volumes of plasma were required from each sample and we also applied the method to discover IgA and IgA‐glycopeptide profiles in patients with chronic kidney diseases and IgA nephropathy.
Methods
Peptide M affinity beads were used to purify IgA, and a cost‐effective peptide analogue was added as internal standard. With an efficient on‐bead digestion process, purified samples were analyzed by UHPLC/MS/MS in multiple reaction monitoring mode.
Results
Correlation coefficients were greater than 0.999 for the IgA1 and IgA2 calibration curves and greater than 0.994 for glycopeptide regression curves. Intraday and interday precisions for IgA1 and IgA2 were <1.6% and <5.1% RSD, respectively. Intraday and interday accuracies ranged from 102.6 to 114.9% and 103.5 to 113.5% for IgA1 and IgA2, respectively. Stabilities of IgA1 and IgA2 at −80°C for 7 to 15 days ranged from 96.0 to 109.4%, respectively. The Pearson's correlation coefficient was 0.916 when comparing the IgA quantification results of the 30 clinical samples by using ELISAs and the developed UHPLC/MS/MS method. Compared with healthy controls, IgA and IgA‐glycopeptides showed different profiles in patients with chronic kidney diseases and IgA nephropathy.
Conclusions
The developed method showed good validation results, and the absolute quantification results of IgA correlated with those from ELISA. The pilot application study showed that IgA and IgA‐glycopeptides can be potential biomarker candidates for kidney diseases, and more clinical sample applications are worth investigating.</abstract><cop>England</cop><pub>Wiley Subscription Services, Inc</pub><pmid>31705576</pmid><doi>10.1002/rcm.8606</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0002-3951-5197</orcidid><orcidid>https://orcid.org/0000-0003-3194-2204</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Affinity Beads Biomarkers Chromatography Chromatography, High Pressure Liquid - methods Chromatography, High Pressure Liquid - standards Correlation coefficients Glycopeptides Glycosylation Humans Immunoglobulin A - analysis Immunoglobulin A - blood Immunoglobulin Fc Fragments - analysis Immunoglobulin Fc Fragments - blood Immunoglobulins Kidney diseases Limit of Detection Liquid chromatography Mass spectrometry Peptides Quadrupoles Quality Control Reference Standards Regression analysis Scientific imaging Spectroscopy Tandem Mass Spectrometry - methods Tandem Mass Spectrometry - standards |
| title | Quantitative determination of human IgA subclasses and their Fc‐glycosylation patterns in plasma by using a peptide analogue internal standard and ultra‐high‐performance liquid chromatography/triple quadrupole mass spectrometry |
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