First bioelectronic immunoplatform for quantitative secretomic analysis of total and metastasis-driven glycosylated haptoglobin
The glycosylation status of proteins is increasingly used as biomarker to improve the reliability in the diagnosis and prognosis of diseases as relevant as cancer. This feeds the need for tools that allow its simple and reliable analysis and are compatible with applicability in the clinic. With this...
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| Veröffentlicht in: | Analytical and bioanalytical chemistry 2023-05, Vol.415 (11), p.2045-2057 |
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| creator | Muñoz-San Martín, Cristina Montero-Calle, Ana Garranzo-Asensio, María Gamella, Maria Pérez-Ginés, Víctor Pedrero, María Pingarrón, José M. Barderas, Rodrigo de-los-Santos-Álvarez, Noemí Lobo-Castañón, María Jesús Campuzano, Susana |
| description | The glycosylation status of proteins is increasingly used as biomarker to improve the reliability in the diagnosis and prognosis of diseases as relevant as cancer. This feeds the need for tools that allow its simple and reliable analysis and are compatible with applicability in the clinic. With this objective in mind, this work reports the first bioelectronic immunoplatforms described to date for the determination of glycosylated haptoglobin (Hp) and the simultaneous determination of total and glycosylated Hp. The bioelectronic immunoplatform is based on the implementation of non-competitive bioassays using two different antibodies or an antibody and a lectin on the surface of commercial magnetic microcarriers. The resulting bioconjugates are labeled with the horseradish peroxidase (HRP) enzyme, and after their magnetic capture on disposable electroplatforms, the amperometric transduction using the H
2
O
2
/hydroquinone (HQ) system allows the single or multiple detection. The developed immunoplatform achieves limits of detection (LODs) of 0.07 and 0.46 ng mL
−1
for total and glycosylated Hp in buffer solution, respectively. The immunoplatform allows accurate determination using simple and relatively short protocols (approx. 75 min) of total and glycosylated Hp in the secretomes of in vitro–cultured colorectal cancer (CRC) cells with different metastatic potentials, which is not feasible, due to lack of sensitivity, by means of some commercial ELISA kits and Western blot methodology.
Graphical abstract |
| doi_str_mv | 10.1007/s00216-022-04397-6 |
| format | Article |
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2
O
2
/hydroquinone (HQ) system allows the single or multiple detection. The developed immunoplatform achieves limits of detection (LODs) of 0.07 and 0.46 ng mL
−1
for total and glycosylated Hp in buffer solution, respectively. The immunoplatform allows accurate determination using simple and relatively short protocols (approx. 75 min) of total and glycosylated Hp in the secretomes of in vitro–cultured colorectal cancer (CRC) cells with different metastatic potentials, which is not feasible, due to lack of sensitivity, by means of some commercial ELISA kits and Western blot methodology.
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2
O
2
/hydroquinone (HQ) system allows the single or multiple detection. The developed immunoplatform achieves limits of detection (LODs) of 0.07 and 0.46 ng mL
−1
for total and glycosylated Hp in buffer solution, respectively. The immunoplatform allows accurate determination using simple and relatively short protocols (approx. 75 min) of total and glycosylated Hp in the secretomes of in vitro–cultured colorectal cancer (CRC) cells with different metastatic potentials, which is not feasible, due to lack of sensitivity, by means of some commercial ELISA kits and Western blot methodology.
Graphical abstract</description><subject>Analysis</subject><subject>Analytical Chemistry</subject><subject>Analytical Nanoscience and Nanotechnology</subject><subject>Angiogenesis</subject><subject>Antibodies</subject><subject>Bioassays</subject><subject>Biochemistry</subject><subject>Bioelectricity</subject><subject>Biomarkers</subject><subject>Biosensing Techniques - methods</subject><subject>Biosensors</subject><subject>Buffer solutions</subject><subject>Cancer</subject><subject>Characterization and Evaluation of Materials</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Colorectal cancer</subject><subject>Colorectal carcinoma</subject><subject>Electrical measurement</subject><subject>Enzyme-Linked Immunosorbent Assay</subject><subject>Extracellular matrix</subject><subject>Food Science</subject><subject>Glycoproteins</subject><subject>Glycosylation</subject><subject>Haptoglobin</subject><subject>Haptoglobins</subject><subject>Horseradish peroxidase</subject><subject>Humans</subject><subject>Hydrogen Peroxide</subject><subject>Hydroquinone</subject><subject>Immunoassay</subject><subject>Laboratory Medicine</subject><subject>Lectins</subject><subject>Metastases</subject><subject>Metastasis</subject><subject>Methods</subject><subject>Monitoring/Environmental Analysis</subject><subject>Neoplasms</subject><subject>Paper in Forefront</subject><subject>Peroxidase</subject><subject>Properties</subject><subject>Proteins</subject><subject>Reproducibility of 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bioelectronic immunoplatform for quantitative secretomic analysis of total and metastasis-driven glycosylated haptoglobin</title><author>Muñoz-San Martín, Cristina ; Montero-Calle, Ana ; Garranzo-Asensio, María ; Gamella, Maria ; Pérez-Ginés, Víctor ; Pedrero, María ; Pingarrón, José M. ; Barderas, Rodrigo ; de-los-Santos-Álvarez, Noemí ; Lobo-Castañón, María Jesús ; Campuzano, Susana</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c542t-3637afd2f9c04cc2f96acabcaf0ad3930e4ec253125e5d4fd3d0ed2b5d8a16c93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Analysis</topic><topic>Analytical Chemistry</topic><topic>Analytical Nanoscience and Nanotechnology</topic><topic>Angiogenesis</topic><topic>Antibodies</topic><topic>Bioassays</topic><topic>Biochemistry</topic><topic>Bioelectricity</topic><topic>Biomarkers</topic><topic>Biosensing Techniques - 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Martín, Cristina</au><au>Montero-Calle, Ana</au><au>Garranzo-Asensio, María</au><au>Gamella, Maria</au><au>Pérez-Ginés, Víctor</au><au>Pedrero, María</au><au>Pingarrón, José M.</au><au>Barderas, Rodrigo</au><au>de-los-Santos-Álvarez, Noemí</au><au>Lobo-Castañón, María Jesús</au><au>Campuzano, Susana</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>First bioelectronic immunoplatform for quantitative secretomic analysis of total and metastasis-driven glycosylated haptoglobin</atitle><jtitle>Analytical and bioanalytical chemistry</jtitle><stitle>Anal Bioanal Chem</stitle><addtitle>Anal Bioanal Chem</addtitle><date>2023-05-01</date><risdate>2023</risdate><volume>415</volume><issue>11</issue><spage>2045</spage><epage>2057</epage><pages>2045-2057</pages><issn>1618-2642</issn><eissn>1618-2650</eissn><abstract>The glycosylation status of proteins is increasingly used as biomarker to improve the reliability in the diagnosis and prognosis of diseases as relevant as cancer. This feeds the need for tools that allow its simple and reliable analysis and are compatible with applicability in the clinic. With this objective in mind, this work reports the first bioelectronic immunoplatforms described to date for the determination of glycosylated haptoglobin (Hp) and the simultaneous determination of total and glycosylated Hp. The bioelectronic immunoplatform is based on the implementation of non-competitive bioassays using two different antibodies or an antibody and a lectin on the surface of commercial magnetic microcarriers. The resulting bioconjugates are labeled with the horseradish peroxidase (HRP) enzyme, and after their magnetic capture on disposable electroplatforms, the amperometric transduction using the H
2
O
2
/hydroquinone (HQ) system allows the single or multiple detection. The developed immunoplatform achieves limits of detection (LODs) of 0.07 and 0.46 ng mL
−1
for total and glycosylated Hp in buffer solution, respectively. The immunoplatform allows accurate determination using simple and relatively short protocols (approx. 75 min) of total and glycosylated Hp in the secretomes of in vitro–cultured colorectal cancer (CRC) cells with different metastatic potentials, which is not feasible, due to lack of sensitivity, by means of some commercial ELISA kits and Western blot methodology.
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| fulltext | fulltext |
| identifier | ISSN: 1618-2642 |
| ispartof | Analytical and bioanalytical chemistry, 2023-05, Vol.415 (11), p.2045-2057 |
| issn | 1618-2642 1618-2650 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10079713 |
| source | MEDLINE; SpringerLink Journals |
| subjects | Analysis Analytical Chemistry Analytical Nanoscience and Nanotechnology Angiogenesis Antibodies Bioassays Biochemistry Bioelectricity Biomarkers Biosensing Techniques - methods Biosensors Buffer solutions Cancer Characterization and Evaluation of Materials Chemistry Chemistry and Materials Science Colorectal cancer Colorectal carcinoma Electrical measurement Enzyme-Linked Immunosorbent Assay Extracellular matrix Food Science Glycoproteins Glycosylation Haptoglobin Haptoglobins Horseradish peroxidase Humans Hydrogen Peroxide Hydroquinone Immunoassay Laboratory Medicine Lectins Metastases Metastasis Methods Monitoring/Environmental Analysis Neoplasms Paper in Forefront Peroxidase Properties Proteins Reproducibility of Results |
| title | First bioelectronic immunoplatform for quantitative secretomic analysis of total and metastasis-driven glycosylated haptoglobin |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T12%3A55%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=First%20bioelectronic%20immunoplatform%20for%20quantitative%20secretomic%20analysis%20of%20total%20and%20metastasis-driven%20glycosylated%20haptoglobin&rft.jtitle=Analytical%20and%20bioanalytical%20chemistry&rft.au=Mu%C3%B1oz-San%20Mart%C3%ADn,%20Cristina&rft.date=2023-05-01&rft.volume=415&rft.issue=11&rft.spage=2045&rft.epage=2057&rft.pages=2045-2057&rft.issn=1618-2642&rft.eissn=1618-2650&rft_id=info:doi/10.1007/s00216-022-04397-6&rft_dat=%3Cgale_pubme%3EA744615711%3C/gale_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2796669407&rft_id=info:pmid/36344668&rft_galeid=A744615711&rfr_iscdi=true |