Differential Glycosylation Levels in Saliva from Patients with Lung or Breast Cancer: A Preliminary Assessment for Early Diagnostic Purposes
Glycans play a fundamental role in several biological processes, such as cell–cell adhesion, signaling, and recognition. Similarly, abnormal glycosylation is involved in many pathological processes, among which include tumor growth and progression. Several highly glycosylated proteins found in blood...
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Published in | Metabolites Vol. 11; no. 9; p. 566 |
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Main Authors | , , , , , , , , , , , , |
Format | Journal Article |
Language | English |
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24.08.2021
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Abstract | Glycans play a fundamental role in several biological processes, such as cell–cell adhesion, signaling, and recognition. Similarly, abnormal glycosylation is involved in many pathological processes, among which include tumor growth and progression. Several highly glycosylated proteins found in blood are currently used in clinical practice as cancer biomarkers (e.g., CA125, PSA, and CA19-9). The development of novel non-invasive diagnostic procedures would greatly simplify the screening and discovery of pathologies at an early stage, thus also allowing for simpler treatment and a higher success rate. In this observational study carried out on 68 subjects diagnosed with either breast or lung cancer and 34 healthy volunteers, we hydrolyzed the glycoproteins in saliva and quantified the obtained free sugars (fucose, mannose, galactose, glucosamine, and galactosamine) by using high-performance anion-exchange chromatography with pulsed-amperometric detection (HPAEC-PAD). The glycosidic profiles were compared by using multivariate statistical analysis, showing differential glycosylation patterns among the three categories. Furthermore, Receiver Operating Characteristics (ROC) analysis allowed obtaining a reliable and minimally invasive protocol able to discriminate between healthy and pathological subjects. |
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AbstractList | Glycans play a fundamental role in several biological processes, such as cell–cell adhesion, signaling, and recognition. Similarly, abnormal glycosylation is involved in many pathological processes, among which include tumor growth and progression. Several highly glycosylated proteins found in blood are currently used in clinical practice as cancer biomarkers (e.g., CA125, PSA, and CA19-9). The development of novel non-invasive diagnostic procedures would greatly simplify the screening and discovery of pathologies at an early stage, thus also allowing for simpler treatment and a higher success rate. In this observational study carried out on 68 subjects diagnosed with either breast or lung cancer and 34 healthy volunteers, we hydrolyzed the glycoproteins in saliva and quantified the obtained free sugars (fucose, mannose, galactose, glucosamine, and galactosamine) by using high-performance anion-exchange chromatography with pulsed-amperometric detection (HPAEC-PAD). The glycosidic profiles were compared by using multivariate statistical analysis, showing differential glycosylation patterns among the three categories. Furthermore, Receiver Operating Characteristics (ROC) analysis allowed obtaining a reliable and minimally invasive protocol able to discriminate between healthy and pathological subjects. Glycans play a fundamental role in several biological processes, such as cell-cell adhesion, signaling, and recognition. Similarly, abnormal glycosylation is involved in many pathological processes, among which include tumor growth and progression. Several highly glycosylated proteins found in blood are currently used in clinical practice as cancer biomarkers (e.g., CA125, PSA, and CA19-9). The development of novel non-invasive diagnostic procedures would greatly simplify the screening and discovery of pathologies at an early stage, thus also allowing for simpler treatment and a higher success rate. In this observational study carried out on 68 subjects diagnosed with either breast or lung cancer and 34 healthy volunteers, we hydrolyzed the glycoproteins in saliva and quantified the obtained free sugars (fucose, mannose, galactose, glucosamine, and galactosamine) by using high-performance anion-exchange chromatography with pulsed-amperometric detection (HPAEC-PAD). The glycosidic profiles were compared by using multivariate statistical analysis, showing differential glycosylation patterns among the three categories. Furthermore, Receiver Operating Characteristics (ROC) analysis allowed obtaining a reliable and minimally invasive protocol able to discriminate between healthy and pathological subjects.Glycans play a fundamental role in several biological processes, such as cell-cell adhesion, signaling, and recognition. Similarly, abnormal glycosylation is involved in many pathological processes, among which include tumor growth and progression. Several highly glycosylated proteins found in blood are currently used in clinical practice as cancer biomarkers (e.g., CA125, PSA, and CA19-9). The development of novel non-invasive diagnostic procedures would greatly simplify the screening and discovery of pathologies at an early stage, thus also allowing for simpler treatment and a higher success rate. In this observational study carried out on 68 subjects diagnosed with either breast or lung cancer and 34 healthy volunteers, we hydrolyzed the glycoproteins in saliva and quantified the obtained free sugars (fucose, mannose, galactose, glucosamine, and galactosamine) by using high-performance anion-exchange chromatography with pulsed-amperometric detection (HPAEC-PAD). The glycosidic profiles were compared by using multivariate statistical analysis, showing differential glycosylation patterns among the three categories. Furthermore, Receiver Operating Characteristics (ROC) analysis allowed obtaining a reliable and minimally invasive protocol able to discriminate between healthy and pathological subjects. |
Author | Romano, Pietrina Maffia, Michele Di Renzo, Nicola Neglia, Cosimo Ragusa, Andrea Piscitelli, Prisco Lenucci, Marcello Salvatore Pitotti, Elena Surico, Giammarco Civino, Emanuela Vergara, Daniele Distante, Alessandro Romano, Giampiero Diego |
AuthorAffiliation | 3 Medical Oncology Unit, “Vito Fazzi” Hospital, 73100 Lecce, Italy; info@isbem.it (P.R.); oncologia.polecce@ausl.le.it (G.D.R.); direnzo.ematolecce@gmail.com (N.D.R.); repol@ausl.le.it (G.S.) 1 Department of Biological and Environmental Sciences and Technologies, Campus Ecotekne, University of Salento, via Monteroni, 73100 Lecce, Italy; marcello.lenucci@unisalento.it (M.S.L.); emanuela.civino@unisalento.it (E.C.); daniele.vergara@unisalento.it (D.V.) 2 CNR-Nanotec, Institute of Nanotechnology, via Monteroni, 73100 Lecce, Italy 5 Euro Mediterranean Scientific Biomedical Institute (ISBEM), 72100 Brindisi, Italy; neglia@isbem.it (C.N.); distante@isbem.it (A.D.) 4 Local Health Authority ASL Lecce, 73100 Lecce, Italy; proteomica.polecce@ausl.le.it (E.P.); piscitelli@unescochairnapoli.it (P.P.) |
AuthorAffiliation_xml | – name: 4 Local Health Authority ASL Lecce, 73100 Lecce, Italy; proteomica.polecce@ausl.le.it (E.P.); piscitelli@unescochairnapoli.it (P.P.) – name: 5 Euro Mediterranean Scientific Biomedical Institute (ISBEM), 72100 Brindisi, Italy; neglia@isbem.it (C.N.); distante@isbem.it (A.D.) – name: 2 CNR-Nanotec, Institute of Nanotechnology, via Monteroni, 73100 Lecce, Italy – name: 3 Medical Oncology Unit, “Vito Fazzi” Hospital, 73100 Lecce, Italy; info@isbem.it (P.R.); oncologia.polecce@ausl.le.it (G.D.R.); direnzo.ematolecce@gmail.com (N.D.R.); repol@ausl.le.it (G.S.) – name: 1 Department of Biological and Environmental Sciences and Technologies, Campus Ecotekne, University of Salento, via Monteroni, 73100 Lecce, Italy; marcello.lenucci@unisalento.it (M.S.L.); emanuela.civino@unisalento.it (E.C.); daniele.vergara@unisalento.it (D.V.) |
Author_xml | – sequence: 1 givenname: Andrea orcidid: 0000-0002-2198-6185 surname: Ragusa fullname: Ragusa, Andrea – sequence: 2 givenname: Pietrina surname: Romano fullname: Romano, Pietrina – sequence: 3 givenname: Marcello Salvatore orcidid: 0000-0002-6493-9549 surname: Lenucci fullname: Lenucci, Marcello Salvatore – sequence: 4 givenname: Emanuela surname: Civino fullname: Civino, Emanuela – sequence: 5 givenname: Daniele orcidid: 0000-0002-2396-7674 surname: Vergara fullname: Vergara, Daniele – sequence: 6 givenname: Elena surname: Pitotti fullname: Pitotti, Elena – sequence: 7 givenname: Cosimo surname: Neglia fullname: Neglia, Cosimo – sequence: 8 givenname: Alessandro surname: Distante fullname: Distante, Alessandro – sequence: 9 givenname: Giampiero Diego surname: Romano fullname: Romano, Giampiero Diego – sequence: 10 givenname: Nicola surname: Di Renzo fullname: Di Renzo, Nicola – sequence: 11 givenname: Giammarco surname: Surico fullname: Surico, Giammarco – sequence: 12 givenname: Prisco surname: Piscitelli fullname: Piscitelli, Prisco – sequence: 13 givenname: Michele orcidid: 0000-0003-0665-4534 surname: Maffia fullname: Maffia, Michele |
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Snippet | Glycans play a fundamental role in several biological processes, such as cell–cell adhesion, signaling, and recognition. Similarly, abnormal glycosylation is... Glycans play a fundamental role in several biological processes, such as cell-cell adhesion, signaling, and recognition. Similarly, abnormal glycosylation is... |
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SubjectTerms | Anion-exchange chromatography Biomarkers Biopsy Body mass index Breast cancer Cancer therapies Carbohydrates Cell adhesion Chromatography Clinical medicine D-Galactosamine early diagnosis Galactose Glucosamine glycomics glycoprotein Glycoproteins Glycosylation HPEAC-PAD Lung cancer Mannose Medical prognosis Mortality Patients Polysaccharides Proteins Saliva Statistical analysis |
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Title | Differential Glycosylation Levels in Saliva from Patients with Lung or Breast Cancer: A Preliminary Assessment for Early Diagnostic Purposes |
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