Glycosylation: Rising Potential for Prostate Cancer Evaluation
Simple Summary Aberrant protein glycosylation is a well-known hallmark of cancer and is associated with differential expression of enzymes such as glycosyltransferases and glycosidases. The altered expression of the enzymes triggers cancer cells to produce glycoproteins with specific cancer-related...
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| Veröffentlicht in: | Cancers 2021-07, Vol.13 (15), p.3726, Article 3726 |
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| description | Simple Summary Aberrant protein glycosylation is a well-known hallmark of cancer and is associated with differential expression of enzymes such as glycosyltransferases and glycosidases. The altered expression of the enzymes triggers cancer cells to produce glycoproteins with specific cancer-related aberrations in glycan structures. Increasing number of data indicate that glycosylation patterns of PSA and other prostate-originated proteins exert a potential to distinguish between benign prostate disease and cancer as well as among different stages of prostate cancer development and aggressiveness. This review summarizes the alterations in glycan sialylation, fucosylation, truncated O-glycans, and LacdiNAc groups outlining their potential applications in non-invasive diagnostic procedures of prostate diseases. Further research is desired to develop more general algorithms exploiting glycobiology data for the improvement of prostate diseases evaluation. Prostate cancer is the second most commonly diagnosed cancer among men. Alterations in protein glycosylation are confirmed to be a reliable hallmark of cancer. Prostate-specific antigen is the biomarker that is used most frequently for prostate cancer detection, although its lack of sensitivity and specificity results in many unnecessary biopsies. A wide range of glycosylation alterations in prostate cancer cells, including increased sialylation and fucosylation, can modify protein function and play a crucial role in many important biological processes in cancer, including cell signalling, adhesion, migration, and cellular metabolism. In this review, we summarize studies evaluating the prostate cancer associated glycosylation related alterations in sialylation, mainly alpha 2,3-sialylation, core fucosylation, branched N-glycans, LacdiNAc group and presence of truncated O-glycans (sTn, sT antigen). Finally, we discuss the great potential to make use of glycans as diagnostic and prognostic biomarkers for prostate cancer. |
| doi_str_mv | 10.3390/cancers13153726 |
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The altered expression of the enzymes triggers cancer cells to produce glycoproteins with specific cancer-related aberrations in glycan structures. Increasing number of data indicate that glycosylation patterns of PSA and other prostate-originated proteins exert a potential to distinguish between benign prostate disease and cancer as well as among different stages of prostate cancer development and aggressiveness. This review summarizes the alterations in glycan sialylation, fucosylation, truncated O-glycans, and LacdiNAc groups outlining their potential applications in non-invasive diagnostic procedures of prostate diseases. Further research is desired to develop more general algorithms exploiting glycobiology data for the improvement of prostate diseases evaluation. Prostate cancer is the second most commonly diagnosed cancer among men. Alterations in protein glycosylation are confirmed to be a reliable hallmark of cancer. Prostate-specific antigen is the biomarker that is used most frequently for prostate cancer detection, although its lack of sensitivity and specificity results in many unnecessary biopsies. A wide range of glycosylation alterations in prostate cancer cells, including increased sialylation and fucosylation, can modify protein function and play a crucial role in many important biological processes in cancer, including cell signalling, adhesion, migration, and cellular metabolism. In this review, we summarize studies evaluating the prostate cancer associated glycosylation related alterations in sialylation, mainly alpha 2,3-sialylation, core fucosylation, branched N-glycans, LacdiNAc group and presence of truncated O-glycans (sTn, sT antigen). Finally, we discuss the great potential to make use of glycans as diagnostic and prognostic biomarkers for prostate cancer.</description><identifier>ISSN: 2072-6694</identifier><identifier>EISSN: 2072-6694</identifier><identifier>DOI: 10.3390/cancers13153726</identifier><identifier>PMID: 34359624</identifier><language>eng</language><publisher>BASEL: Mdpi</publisher><subject>Androgens ; Antigens ; Biomarkers ; Biopsy ; Cancer therapies ; Cell migration ; Chemical elements ; Enzymes ; FDA approval ; Federal regulation ; Glycoproteins ; Glycosylation ; Growth factors ; Homeostasis ; Hyperplasia ; Inflammation ; Life Sciences & Biomedicine ; Ligands ; Lymphocytes ; Magnetic resonance imaging ; Metastasis ; N-glycans ; Oncology ; Oxidation ; Polysaccharides ; Prostate cancer ; Prostate-specific antigen ; Proteins ; Review ; Science & Technology ; Tumors</subject><ispartof>Cancers, 2021-07, Vol.13 (15), p.3726, Article 3726</ispartof><rights>2021 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). 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The altered expression of the enzymes triggers cancer cells to produce glycoproteins with specific cancer-related aberrations in glycan structures. Increasing number of data indicate that glycosylation patterns of PSA and other prostate-originated proteins exert a potential to distinguish between benign prostate disease and cancer as well as among different stages of prostate cancer development and aggressiveness. This review summarizes the alterations in glycan sialylation, fucosylation, truncated O-glycans, and LacdiNAc groups outlining their potential applications in non-invasive diagnostic procedures of prostate diseases. Further research is desired to develop more general algorithms exploiting glycobiology data for the improvement of prostate diseases evaluation. Prostate cancer is the second most commonly diagnosed cancer among men. Alterations in protein glycosylation are confirmed to be a reliable hallmark of cancer. Prostate-specific antigen is the biomarker that is used most frequently for prostate cancer detection, although its lack of sensitivity and specificity results in many unnecessary biopsies. A wide range of glycosylation alterations in prostate cancer cells, including increased sialylation and fucosylation, can modify protein function and play a crucial role in many important biological processes in cancer, including cell signalling, adhesion, migration, and cellular metabolism. In this review, we summarize studies evaluating the prostate cancer associated glycosylation related alterations in sialylation, mainly alpha 2,3-sialylation, core fucosylation, branched N-glycans, LacdiNAc group and presence of truncated O-glycans (sTn, sT antigen). Finally, we discuss the great potential to make use of glycans as diagnostic and prognostic biomarkers for prostate cancer.</description><subject>Androgens</subject><subject>Antigens</subject><subject>Biomarkers</subject><subject>Biopsy</subject><subject>Cancer therapies</subject><subject>Cell migration</subject><subject>Chemical elements</subject><subject>Enzymes</subject><subject>FDA approval</subject><subject>Federal regulation</subject><subject>Glycoproteins</subject><subject>Glycosylation</subject><subject>Growth factors</subject><subject>Homeostasis</subject><subject>Hyperplasia</subject><subject>Inflammation</subject><subject>Life Sciences & Biomedicine</subject><subject>Ligands</subject><subject>Lymphocytes</subject><subject>Magnetic resonance imaging</subject><subject>Metastasis</subject><subject>N-glycans</subject><subject>Oncology</subject><subject>Oxidation</subject><subject>Polysaccharides</subject><subject>Prostate cancer</subject><subject>Prostate-specific antigen</subject><subject>Proteins</subject><subject>Review</subject><subject>Science & Technology</subject><subject>Tumors</subject><issn>2072-6694</issn><issn>2072-6694</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>HGBXW</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqNkUtLAzEUhYMoKtq12wE3glTznsSFIIMvKCii65BJMzUyndQkU-m_N31Q1JXZ5ML9zrk3OQCcIHhBiISXRnfGhogIYqTEfAccYljiIeeS7v6oD8Agxg-YDyGo5OU-OCCUMMkxPQTX9-3C-LhodXK-uypeXHTdpHj2yXbJ6bZofCieg49JJ1tUq4nF7Vy3_UpwDPYa3UY72NxH4O3u9rV6GI6e7h-rm9HQECnSkAgtqYScwBrlWlsJIdWI4TFlDFpZIylqLGRTN6ZBY0xqWja0ZFLrMcW2Jkfgeu076-upHZu8XNCtmgU31WGhvHbqd6dz72ri50oQyiAV2eBsYxD8Z29jUlMXjW1b3VnfR4UZk5QggWlGT_-gH74PXX7ekhIlzhDP1OWaMvlzYrDNdhkE1TIe9SeerDhfK75s7ZtonM39rSrHwwUSjPJlUijT4v905dIqjsr3XSLf0vujMw</recordid><startdate>20210724</startdate><enddate>20210724</enddate><creator>Kaluza, Anna</creator><creator>Szczykutowicz, Justyna</creator><creator>Ferens-Sieczkowska, Miroslawa</creator><general>Mdpi</general><general>MDPI AG</general><general>MDPI</general><scope>BLEPL</scope><scope>DTL</scope><scope>HGBXW</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7T5</scope><scope>7TO</scope><scope>7XB</scope><scope>8FE</scope><scope>8FH</scope><scope>8FK</scope><scope>8G5</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-0161-3012</orcidid><orcidid>https://orcid.org/0000-0001-6746-6591</orcidid><orcidid>https://orcid.org/0000-0001-8578-7487</orcidid></search><sort><creationdate>20210724</creationdate><title>Glycosylation: Rising Potential for Prostate Cancer Evaluation</title><author>Kaluza, Anna ; 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The altered expression of the enzymes triggers cancer cells to produce glycoproteins with specific cancer-related aberrations in glycan structures. Increasing number of data indicate that glycosylation patterns of PSA and other prostate-originated proteins exert a potential to distinguish between benign prostate disease and cancer as well as among different stages of prostate cancer development and aggressiveness. This review summarizes the alterations in glycan sialylation, fucosylation, truncated O-glycans, and LacdiNAc groups outlining their potential applications in non-invasive diagnostic procedures of prostate diseases. Further research is desired to develop more general algorithms exploiting glycobiology data for the improvement of prostate diseases evaluation. Prostate cancer is the second most commonly diagnosed cancer among men. Alterations in protein glycosylation are confirmed to be a reliable hallmark of cancer. Prostate-specific antigen is the biomarker that is used most frequently for prostate cancer detection, although its lack of sensitivity and specificity results in many unnecessary biopsies. A wide range of glycosylation alterations in prostate cancer cells, including increased sialylation and fucosylation, can modify protein function and play a crucial role in many important biological processes in cancer, including cell signalling, adhesion, migration, and cellular metabolism. In this review, we summarize studies evaluating the prostate cancer associated glycosylation related alterations in sialylation, mainly alpha 2,3-sialylation, core fucosylation, branched N-glycans, LacdiNAc group and presence of truncated O-glycans (sTn, sT antigen). Finally, we discuss the great potential to make use of glycans as diagnostic and prognostic biomarkers for prostate cancer.</abstract><cop>BASEL</cop><pub>Mdpi</pub><pmid>34359624</pmid><doi>10.3390/cancers13153726</doi><tpages>22</tpages><orcidid>https://orcid.org/0000-0003-0161-3012</orcidid><orcidid>https://orcid.org/0000-0001-6746-6591</orcidid><orcidid>https://orcid.org/0000-0001-8578-7487</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Androgens Antigens Biomarkers Biopsy Cancer therapies Cell migration Chemical elements Enzymes FDA approval Federal regulation Glycoproteins Glycosylation Growth factors Homeostasis Hyperplasia Inflammation Life Sciences & Biomedicine Ligands Lymphocytes Magnetic resonance imaging Metastasis N-glycans Oncology Oxidation Polysaccharides Prostate cancer Prostate-specific antigen Proteins Review Science & Technology Tumors |
| title | Glycosylation: Rising Potential for Prostate Cancer Evaluation |
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