Post-translational modifications in tumor biomarkers: the next challenge for aptamers?
Advances in proteomics have fueled the search for novel cancer biomarkers with higher selectivity. Differential expression of low abundant proteins has been the usual way of finding those biomarkers. The existence of a selective receptor for each biomarker is compulsory for their use in diagnostic/p...
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| Veröffentlicht in: | Analytical and bioanalytical chemistry 2018-03, Vol.410 (8), p.2059-2065 |
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| creator | Díaz-Fernández, Ana Miranda-Castro, Rebeca de-los-Santos-Álvarez, Noemí Lobo-Castañón, María Jesús |
| description | Advances in proteomics have fueled the search for novel cancer biomarkers with higher selectivity. Differential expression of low abundant proteins has been the usual way of finding those biomarkers. The existence of a selective receptor for each biomarker is compulsory for their use in diagnostic/prognostic assays. Antibodies are the receptors of choice in most cases although aptamers are becoming familiar because of their facile and reproducible synthesis, chemical stability as well as comparable affinity and selectivity. In recent years, it has been reported that the pattern of post-translational modifications, altered under neoplastic disease, is a better predictive biomarker than the total protein level. Among others, abnormal glycosylation is attracting great attention. Lectins and antibodies are being used for identification and detection of the carbohydrate moiety with low level of discrimination among various glycoproteins. Such level of selectivity is critical to bring next-generation biomarkers to the clinic. Aptamers that can be rationally tailored for a certain molecule domain can become the golden receptor to specifically detect aberrant glycosylation at each protein or even at each glycosylation site, providing new diagnostic tools for early detection of cancer.
Graphical abstract
Aptamers may specifically differentiate normal from aberrant glycoproteins |
| doi_str_mv | 10.1007/s00216-018-0861-9 |
| format | Article |
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Graphical abstract
Aptamers may specifically differentiate normal from aberrant glycoproteins</description><identifier>ISSN: 1618-2642</identifier><identifier>EISSN: 1618-2650</identifier><identifier>DOI: 10.1007/s00216-018-0861-9</identifier><identifier>PMID: 29353432</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer Berlin Heidelberg</publisher><subject>Aberration ; Analytical Chemistry ; Antibodies ; Aptamers ; Biochemistry ; Biological markers ; Biomarkers ; Cancer ; Carbohydrates ; Characterization and Evaluation of Materials ; Chemical synthesis ; Chemistry ; Chemistry and Materials Science ; Diagnostic software ; Diagnostic systems ; Feature Article ; Food Science ; Genetic aspects ; Glycoproteins ; Glycosylation ; Health aspects ; Laboratory Medicine ; Lectins ; Low level ; Monitoring/Environmental Analysis ; Post-translation ; Post-translational modifications ; Proteins ; Proteomics ; Receptors ; Selectivity ; Translation ; Tumors</subject><ispartof>Analytical and bioanalytical chemistry, 2018-03, Vol.410 (8), p.2059-2065</ispartof><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2018</rights><rights>COPYRIGHT 2018 Springer</rights><rights>Analytical and Bioanalytical Chemistry is a copyright of Springer, (2018). All Rights Reserved.</rights><rights>Springer-Verlag GmbH Germany, part of Springer Nature 2018.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c547t-80d453720f72d37872328a9e79c16cefe5be9f53f4807d60624574001283ef7d3</citedby><cites>FETCH-LOGICAL-c547t-80d453720f72d37872328a9e79c16cefe5be9f53f4807d60624574001283ef7d3</cites><orcidid>0000-0002-2964-9490</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s00216-018-0861-9$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s00216-018-0861-9$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27923,27924,41487,42556,51318</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29353432$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Díaz-Fernández, Ana</creatorcontrib><creatorcontrib>Miranda-Castro, Rebeca</creatorcontrib><creatorcontrib>de-los-Santos-Álvarez, Noemí</creatorcontrib><creatorcontrib>Lobo-Castañón, María Jesús</creatorcontrib><title>Post-translational modifications in tumor biomarkers: the next challenge for aptamers?</title><title>Analytical and bioanalytical chemistry</title><addtitle>Anal Bioanal Chem</addtitle><addtitle>Anal Bioanal Chem</addtitle><description>Advances in proteomics have fueled the search for novel cancer biomarkers with higher selectivity. Differential expression of low abundant proteins has been the usual way of finding those biomarkers. The existence of a selective receptor for each biomarker is compulsory for their use in diagnostic/prognostic assays. Antibodies are the receptors of choice in most cases although aptamers are becoming familiar because of their facile and reproducible synthesis, chemical stability as well as comparable affinity and selectivity. In recent years, it has been reported that the pattern of post-translational modifications, altered under neoplastic disease, is a better predictive biomarker than the total protein level. Among others, abnormal glycosylation is attracting great attention. Lectins and antibodies are being used for identification and detection of the carbohydrate moiety with low level of discrimination among various glycoproteins. Such level of selectivity is critical to bring next-generation biomarkers to the clinic. Aptamers that can be rationally tailored for a certain molecule domain can become the golden receptor to specifically detect aberrant glycosylation at each protein or even at each glycosylation site, providing new diagnostic tools for early detection of cancer.
Graphical abstract
Aptamers may specifically differentiate normal from aberrant glycoproteins</description><subject>Aberration</subject><subject>Analytical Chemistry</subject><subject>Antibodies</subject><subject>Aptamers</subject><subject>Biochemistry</subject><subject>Biological markers</subject><subject>Biomarkers</subject><subject>Cancer</subject><subject>Carbohydrates</subject><subject>Characterization and Evaluation of Materials</subject><subject>Chemical synthesis</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Diagnostic software</subject><subject>Diagnostic systems</subject><subject>Feature Article</subject><subject>Food Science</subject><subject>Genetic aspects</subject><subject>Glycoproteins</subject><subject>Glycosylation</subject><subject>Health aspects</subject><subject>Laboratory Medicine</subject><subject>Lectins</subject><subject>Low level</subject><subject>Monitoring/Environmental Analysis</subject><subject>Post-translation</subject><subject>Post-translational 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Bioanal Chem</stitle><addtitle>Anal Bioanal Chem</addtitle><date>2018-03-01</date><risdate>2018</risdate><volume>410</volume><issue>8</issue><spage>2059</spage><epage>2065</epage><pages>2059-2065</pages><issn>1618-2642</issn><eissn>1618-2650</eissn><abstract>Advances in proteomics have fueled the search for novel cancer biomarkers with higher selectivity. Differential expression of low abundant proteins has been the usual way of finding those biomarkers. The existence of a selective receptor for each biomarker is compulsory for their use in diagnostic/prognostic assays. Antibodies are the receptors of choice in most cases although aptamers are becoming familiar because of their facile and reproducible synthesis, chemical stability as well as comparable affinity and selectivity. In recent years, it has been reported that the pattern of post-translational modifications, altered under neoplastic disease, is a better predictive biomarker than the total protein level. Among others, abnormal glycosylation is attracting great attention. Lectins and antibodies are being used for identification and detection of the carbohydrate moiety with low level of discrimination among various glycoproteins. Such level of selectivity is critical to bring next-generation biomarkers to the clinic. Aptamers that can be rationally tailored for a certain molecule domain can become the golden receptor to specifically detect aberrant glycosylation at each protein or even at each glycosylation site, providing new diagnostic tools for early detection of cancer.
Graphical abstract
Aptamers may specifically differentiate normal from aberrant glycoproteins</abstract><cop>Berlin/Heidelberg</cop><pub>Springer Berlin Heidelberg</pub><pmid>29353432</pmid><doi>10.1007/s00216-018-0861-9</doi><tpages>7</tpages><orcidid>https://orcid.org/0000-0002-2964-9490</orcidid><oa>free_for_read</oa></addata></record> |
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| ispartof | Analytical and bioanalytical chemistry, 2018-03, Vol.410 (8), p.2059-2065 |
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| subjects | Aberration Analytical Chemistry Antibodies Aptamers Biochemistry Biological markers Biomarkers Cancer Carbohydrates Characterization and Evaluation of Materials Chemical synthesis Chemistry Chemistry and Materials Science Diagnostic software Diagnostic systems Feature Article Food Science Genetic aspects Glycoproteins Glycosylation Health aspects Laboratory Medicine Lectins Low level Monitoring/Environmental Analysis Post-translation Post-translational modifications Proteins Proteomics Receptors Selectivity Translation Tumors |
| title | Post-translational modifications in tumor biomarkers: the next challenge for aptamers? |
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