Type IX Collagen Turnover Is Altered in Patients with Solid Tumors
The fibrotic tumor microenvironment, characterized by its intricate extracellular matrix (ECM), consists of many collagens with diverse functions and unexplored biomarker potential. Type IX collagen is a member of the low-abundance collagen family known as the fibril-associated collagen with interru...
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| Veröffentlicht in: | Cancers 2024-06, Vol.16 (11), p.2035 |
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| creator | Port, Helena He, Yi Karsdal, Morten A Madsen, Emilie A Bay-Jensen, Anne-Christine Willumsen, Nicholas Holm Nielsen, Signe |
| description | The fibrotic tumor microenvironment, characterized by its intricate extracellular matrix (ECM), consists of many collagens with diverse functions and unexplored biomarker potential. Type IX collagen is a member of the low-abundance collagen family known as the fibril-associated collagen with interrupted triple helices (FACITs) and is found mostly in cartilage. Its role in the tumor microenvironment remains unexplored. To investigate the biomarker potential of a type IX collagen in cancer, an immuno-assay was developed (PRO-C9) and technical assay performance was evaluated for the assessment of serum. PRO-C9 levels were measured in serum samples from 259 patients with various solid tumor types compared to serum levels from 73 healthy controls. PRO-C9 levels were significantly elevated in patients with solid tumors including bladder, breast, colorectal, gastric, head and neck, lung, melanoma, ovarian, pancreatic, and renal compared to levels in healthy controls (
< 0.05-
< 0.0001). PRO-C9 could discriminate between patients with cancer and healthy controls, with the area under the receiver operating characteristic values ranging from 0.58 to 0.86 (
< 0.3-
< 0.0001), indicating potential diagnostic utility. This study suggests that type IX collagen turnover is altered in patients with solid tumors and demonstrates the feasibility of using PRO-C9 as a non-invasive serum-based biomarker with relevance in multiple cancer types. Furthermore, these results underscore the potential utility of PRO-C9 to better elucidate the biology of FACITs in cancers. |
| doi_str_mv | 10.3390/cancers16112035 |
| format | Article |
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< 0.05-
< 0.0001). PRO-C9 could discriminate between patients with cancer and healthy controls, with the area under the receiver operating characteristic values ranging from 0.58 to 0.86 (
< 0.3-
< 0.0001), indicating potential diagnostic utility. This study suggests that type IX collagen turnover is altered in patients with solid tumors and demonstrates the feasibility of using PRO-C9 as a non-invasive serum-based biomarker with relevance in multiple cancer types. Furthermore, these results underscore the potential utility of PRO-C9 to better elucidate the biology of FACITs in cancers.</description><identifier>ISSN: 2072-6694</identifier><identifier>EISSN: 2072-6694</identifier><identifier>DOI: 10.3390/cancers16112035</identifier><identifier>PMID: 38893155</identifier><language>eng</language><publisher>Switzerland: MDPI AG</publisher><subject>Biomarkers ; Cancer ; Cancer research ; Cloning ; Collagen ; Collagen (type IX) ; Complications and side effects ; Development and progression ; Extracellular matrix ; Health aspects ; Hemoglobin ; Homeostasis ; Immunoassay ; Medical prognosis ; Medical research ; Melanoma ; Metastases ; Monoclonal antibodies ; Peptides ; Protein biosynthesis ; Proteins ; Serum levels ; Solid tumors ; Temperature ; Tumor microenvironment ; Tumors</subject><ispartof>Cancers, 2024-06, Vol.16 (11), p.2035</ispartof><rights>COPYRIGHT 2024 MDPI AG</rights><rights>2024 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/). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2024 by the authors. 2024</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c443t-79c34fe3d0200b71cd573d910644b4388e251c31caa46018bcc5f50b829b9eda3</cites><orcidid>0000-0001-8903-7800 ; 0000-0002-9716-572X ; 0000-0001-7952-9297 ; 0009-0001-8944-2512</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11171364/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11171364/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38893155$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Port, Helena</creatorcontrib><creatorcontrib>He, Yi</creatorcontrib><creatorcontrib>Karsdal, Morten A</creatorcontrib><creatorcontrib>Madsen, Emilie A</creatorcontrib><creatorcontrib>Bay-Jensen, Anne-Christine</creatorcontrib><creatorcontrib>Willumsen, Nicholas</creatorcontrib><creatorcontrib>Holm Nielsen, Signe</creatorcontrib><title>Type IX Collagen Turnover Is Altered in Patients with Solid Tumors</title><title>Cancers</title><addtitle>Cancers (Basel)</addtitle><description>The fibrotic tumor microenvironment, characterized by its intricate extracellular matrix (ECM), consists of many collagens with diverse functions and unexplored biomarker potential. Type IX collagen is a member of the low-abundance collagen family known as the fibril-associated collagen with interrupted triple helices (FACITs) and is found mostly in cartilage. Its role in the tumor microenvironment remains unexplored. To investigate the biomarker potential of a type IX collagen in cancer, an immuno-assay was developed (PRO-C9) and technical assay performance was evaluated for the assessment of serum. PRO-C9 levels were measured in serum samples from 259 patients with various solid tumor types compared to serum levels from 73 healthy controls. PRO-C9 levels were significantly elevated in patients with solid tumors including bladder, breast, colorectal, gastric, head and neck, lung, melanoma, ovarian, pancreatic, and renal compared to levels in healthy controls (
< 0.05-
< 0.0001). PRO-C9 could discriminate between patients with cancer and healthy controls, with the area under the receiver operating characteristic values ranging from 0.58 to 0.86 (
< 0.3-
< 0.0001), indicating potential diagnostic utility. This study suggests that type IX collagen turnover is altered in patients with solid tumors and demonstrates the feasibility of using PRO-C9 as a non-invasive serum-based biomarker with relevance in multiple cancer types. Furthermore, these results underscore the potential utility of PRO-C9 to better elucidate the biology of FACITs in cancers.</description><subject>Biomarkers</subject><subject>Cancer</subject><subject>Cancer research</subject><subject>Cloning</subject><subject>Collagen</subject><subject>Collagen (type IX)</subject><subject>Complications and side effects</subject><subject>Development and progression</subject><subject>Extracellular matrix</subject><subject>Health aspects</subject><subject>Hemoglobin</subject><subject>Homeostasis</subject><subject>Immunoassay</subject><subject>Medical prognosis</subject><subject>Medical research</subject><subject>Melanoma</subject><subject>Metastases</subject><subject>Monoclonal antibodies</subject><subject>Peptides</subject><subject>Protein biosynthesis</subject><subject>Proteins</subject><subject>Serum levels</subject><subject>Solid tumors</subject><subject>Temperature</subject><subject>Tumor microenvironment</subject><subject>Tumors</subject><issn>2072-6694</issn><issn>2072-6694</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2024</creationdate><recordtype>article</recordtype><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNptkc9rFDEUx4MottSevUnAi5dt8-ZlJpOTrIu2CwUFV_AWMpk325SZZE1mK_3vTWmtbTE55JF8vt-8H4y9BXGCqMWps8FRytAAVALrF-ywEqpaNI2WLx_FB-w45ytRFiKoRr1mB9i2GqGuD9mnzc2O-PonX8VxtFsKfLNPIV5T4uvMl-NMiXruA_9mZ09hzvy3ny_59zj6vqBTTPkNezXYMdPx_XnEfnz5vFmdLy6-nq1Xy4uFkxLnhdIO5UDYi0qIToHra4W9BtFI2cmSEVU1OARnrWwEtJ1z9VCLrq10p6m3eMQ-3vnu9t1EvSvZJDuaXfKTTTcmWm-evgR_abbx2gCAAmxkcfhw75Dirz3l2Uw-OyqFB4r7bFAo0QpQqi3o-2foVSyNKfUVqlHYokT9j9rakYwPQywfu1tTs1RatVqLuirUyX-osnuavIuBBl_unwhO7wQuxZwTDQ9FgjC3ozfPRl8U7x735oH_O2j8AylrqDk</recordid><startdate>20240601</startdate><enddate>20240601</enddate><creator>Port, Helena</creator><creator>He, Yi</creator><creator>Karsdal, Morten A</creator><creator>Madsen, Emilie A</creator><creator>Bay-Jensen, Anne-Christine</creator><creator>Willumsen, Nicholas</creator><creator>Holm Nielsen, Signe</creator><general>MDPI AG</general><general>MDPI</general><scope>NPM</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/0000-0001-8903-7800</orcidid><orcidid>https://orcid.org/0000-0002-9716-572X</orcidid><orcidid>https://orcid.org/0000-0001-7952-9297</orcidid><orcidid>https://orcid.org/0009-0001-8944-2512</orcidid></search><sort><creationdate>20240601</creationdate><title>Type IX Collagen Turnover Is Altered in Patients with Solid Tumors</title><author>Port, Helena ; He, Yi ; Karsdal, Morten A ; Madsen, Emilie A ; Bay-Jensen, Anne-Christine ; Willumsen, Nicholas ; Holm Nielsen, Signe</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-79c34fe3d0200b71cd573d910644b4388e251c31caa46018bcc5f50b829b9eda3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2024</creationdate><topic>Biomarkers</topic><topic>Cancer</topic><topic>Cancer research</topic><topic>Cloning</topic><topic>Collagen</topic><topic>Collagen (type IX)</topic><topic>Complications and side effects</topic><topic>Development and progression</topic><topic>Extracellular matrix</topic><topic>Health aspects</topic><topic>Hemoglobin</topic><topic>Homeostasis</topic><topic>Immunoassay</topic><topic>Medical prognosis</topic><topic>Medical research</topic><topic>Melanoma</topic><topic>Metastases</topic><topic>Monoclonal antibodies</topic><topic>Peptides</topic><topic>Protein biosynthesis</topic><topic>Proteins</topic><topic>Serum levels</topic><topic>Solid tumors</topic><topic>Temperature</topic><topic>Tumor microenvironment</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Port, Helena</creatorcontrib><creatorcontrib>He, Yi</creatorcontrib><creatorcontrib>Karsdal, Morten A</creatorcontrib><creatorcontrib>Madsen, Emilie A</creatorcontrib><creatorcontrib>Bay-Jensen, Anne-Christine</creatorcontrib><creatorcontrib>Willumsen, Nicholas</creatorcontrib><creatorcontrib>Holm Nielsen, Signe</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cancers</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Port, Helena</au><au>He, Yi</au><au>Karsdal, Morten A</au><au>Madsen, Emilie A</au><au>Bay-Jensen, Anne-Christine</au><au>Willumsen, Nicholas</au><au>Holm Nielsen, Signe</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Type IX Collagen Turnover Is Altered in Patients with Solid Tumors</atitle><jtitle>Cancers</jtitle><addtitle>Cancers (Basel)</addtitle><date>2024-06-01</date><risdate>2024</risdate><volume>16</volume><issue>11</issue><spage>2035</spage><pages>2035-</pages><issn>2072-6694</issn><eissn>2072-6694</eissn><abstract>The fibrotic tumor microenvironment, characterized by its intricate extracellular matrix (ECM), consists of many collagens with diverse functions and unexplored biomarker potential. Type IX collagen is a member of the low-abundance collagen family known as the fibril-associated collagen with interrupted triple helices (FACITs) and is found mostly in cartilage. Its role in the tumor microenvironment remains unexplored. To investigate the biomarker potential of a type IX collagen in cancer, an immuno-assay was developed (PRO-C9) and technical assay performance was evaluated for the assessment of serum. PRO-C9 levels were measured in serum samples from 259 patients with various solid tumor types compared to serum levels from 73 healthy controls. PRO-C9 levels were significantly elevated in patients with solid tumors including bladder, breast, colorectal, gastric, head and neck, lung, melanoma, ovarian, pancreatic, and renal compared to levels in healthy controls (
< 0.05-
< 0.0001). PRO-C9 could discriminate between patients with cancer and healthy controls, with the area under the receiver operating characteristic values ranging from 0.58 to 0.86 (
< 0.3-
< 0.0001), indicating potential diagnostic utility. This study suggests that type IX collagen turnover is altered in patients with solid tumors and demonstrates the feasibility of using PRO-C9 as a non-invasive serum-based biomarker with relevance in multiple cancer types. Furthermore, these results underscore the potential utility of PRO-C9 to better elucidate the biology of FACITs in cancers.</abstract><cop>Switzerland</cop><pub>MDPI AG</pub><pmid>38893155</pmid><doi>10.3390/cancers16112035</doi><orcidid>https://orcid.org/0000-0001-8903-7800</orcidid><orcidid>https://orcid.org/0000-0002-9716-572X</orcidid><orcidid>https://orcid.org/0000-0001-7952-9297</orcidid><orcidid>https://orcid.org/0009-0001-8944-2512</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Biomarkers Cancer Cancer research Cloning Collagen Collagen (type IX) Complications and side effects Development and progression Extracellular matrix Health aspects Hemoglobin Homeostasis Immunoassay Medical prognosis Medical research Melanoma Metastases Monoclonal antibodies Peptides Protein biosynthesis Proteins Serum levels Solid tumors Temperature Tumor microenvironment Tumors |
| title | Type IX Collagen Turnover Is Altered in Patients with Solid Tumors |
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