[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"doc-seo-380218-105":3,"detail-sidebar-cat-0-en-105":81,"doc-detail-380218-en":130},{"code":4,"msg":5,"data":6},0,"ok",{"site_id":7,"language":8,"slug":9,"title":10,"keywords":11,"description":12,"schema_data":13,"social_meta":74,"head_meta":76,"extra_data":78,"updated_unix":80},105,"en","an-update-on-s100a16-in-human-cancer","An Update on S100A16 in Human Cancer","","S100A16 is a calcium-binding S100 protein expressed across human tissues with notably high levels in epithelial-rich areas. mRNA and protein expression of S100A16 often differ across human cancers, and functional studies connect it to tumorigenic processes such as proliferation, differentiation, migration, invasion, and epithelial-mesenchymal transition (EMT). It may act as both tumor-promoter and suppressor. Review also assesses underlying signaling pathways and prognostic biomarker potential.",{"@graph":14,"@context":73},[15,34,56],{"@type":16,"itemListElement":17},"BreadcrumbList",[18,23,27,31],{"item":19,"name":20,"@type":21,"position":22},"https://docshare.wps.com","Home","ListItem",1,{"item":24,"name":25,"@type":21,"position":26},"https://docshare.wps.com/document/","Document",2,{"item":28,"name":29,"@type":21,"position":30},"https://docshare.wps.com/document/healthcare/","Healthcare",3,{"item":32,"name":10,"@type":21,"position":33},"https://docshare.wps.com/document/an-update-on-s100a16-in-human-cancer/380218/",4,{"url":32,"name":10,"@type":35,"image":36,"author":41,"headline":10,"publisher":44,"fileFormat":47,"inLanguage":8,"description":12,"dateModified":48,"datePublished":49,"encodingFormat":47,"isAccessibleForFree":50,"interactionStatistic":51},"DigitalDocument",{"url":37,"@type":38,"width":39,"height":40},"https://docshare.wps.com/thumbnails/an-update-on-s100a16-in-human-cancer/380218.png","ImageObject",300,407,{"name":42,"@type":43},"Sophia Brooks","Person",{"url":19,"name":45,"@type":46},"DocShare","Organization","application/pdf","2026-10-25","2026-09-24",true,{"@type":52,"interactionType":53,"userInteractionCount":55},"InteractionCounter",{"@type":54},"ViewAction",5,{"@type":57,"mainEntity":58},"FAQPage",[59,65,69],{"name":60,"@type":61,"acceptedAnswer":62},"What is S100A16 and where is it expressed?","Question",{"text":63,"@type":64},"S100A16 is a member of the S100 protein family of calcium-binding proteins. It is expressed in many human tissues, with especially high expression in epithelial cell–rich tissues.","Answer",{"name":66,"@type":61,"acceptedAnswer":67},"How is S100A16 linked to cancer biology?",{"text":68,"@type":64},"S100A16 is associated with multiple aspects of tumorigenesis, including cell proliferation, differentiation, migration, invasion, and epithelial-mesenchymal transition (EMT). It has been suggested to have both tumor-promoting and suppressive roles.",{"name":70,"@type":61,"acceptedAnswer":71},"Which pathways or mechanisms are proposed to mediate S100A16 functions?",{"text":72,"@type":64},"S100A16-mediated functions are linked to regulation of signaling pathways and proteins involved in EMT and cancer progression, including PI3K-AKT, p53, MMPs (MMP-1, -2, -9), and JNK/p38, as well as EMT-related proteins such as E-cadherin and vimentin.","https://schema.org",{"og:url":32,"og:type":75,"og:title":10,"og:site_name":45,"og:description":12},"article",{"robots":77,"canonical":32},"index,follow",{"doc_id":79,"site_id":7},380218,1791536401,{"code":4,"msg":82,"data":83},"success",[84,88,92,96,100,105,109,114,119,122,126],{"id":22,"doc_module":4,"doc_module_name":25,"category_name":85,"show_sort_weight":86,"slug":87},"Story & Novel",90,"story-novel",{"id":26,"doc_module":4,"doc_module_name":25,"category_name":89,"show_sort_weight":90,"slug":91},"Literature",80,"literature",{"id":33,"doc_module":4,"doc_module_name":25,"category_name":93,"show_sort_weight":94,"slug":95},"Exam",70,"exam",{"id":55,"doc_module":4,"doc_module_name":25,"category_name":97,"show_sort_weight":98,"slug":99},"Comic",60,"comic",{"id":101,"doc_module":4,"doc_module_name":25,"category_name":102,"show_sort_weight":103,"slug":104},6,"Technology",50,"technology",{"id":106,"doc_module":4,"doc_module_name":25,"category_name":29,"show_sort_weight":107,"slug":108},7,40,"healthcare",{"id":110,"doc_module":4,"doc_module_name":25,"category_name":111,"show_sort_weight":112,"slug":113},8,"Research & Report",30,"research-report",{"id":115,"doc_module":4,"doc_module_name":25,"category_name":116,"show_sort_weight":117,"slug":118},9,"Religion & Spirituality",20,"religion-spirituality",{"id":117,"doc_module":4,"doc_module_name":25,"category_name":120,"show_sort_weight":117,"slug":121},"World Cup","world-cup",{"id":123,"doc_module":4,"doc_module_name":25,"category_name":124,"show_sort_weight":123,"slug":125},10,"Lifestyle","lifestyle",{"id":127,"doc_module":4,"doc_module_name":25,"category_name":128,"show_sort_weight":55,"slug":129},19,"General","general",{"code":4,"msg":82,"data":131},{"doc_id":79,"user_id":132,"nickname":42,"user_avatar":133,"doc_module":4,"category_id":106,"category_name":29,"doc_title":10,"doc_description":12,"doc_content":134,"file_id":135,"file_url":136,"file_type":137,"file_size":138,"view_count":55,"is_deleted":4,"is_public":22,"is_downloadable":22,"audit_status":22,"page_count":139,"language":140,"language_code":8,"site_id":7,"html_lang":8,"table_of_contents":141,"faqs":142,"seo_title":143,"seo_description":12,"update_tm":144,"read_time":112},962084925636,"https://ap-avatar.wpscdn.com/davatar_994ba38a5ba835b3df7d355c54d3ed8d","biomolecules  \nReview  \nAn Update on S100A16 in Human Cancer  \nSuyog Basnet 1, Evan Michael Vallenari 2, Urusha Maharjan 3,4, Sunita Sharma 5, Olaf Schreurs 2 and Dipak Sapkota 2, *  \nCitation: Basnet, S.; Vallenari, E.M.; Maharjan, U.; Sharma, S.; Schreurs, O.; Sapkota, D. An Update on S100A16 in Human Cancer.  \nBiomolecules 2023, 13, 1070 . [https://doi.org/10.3390/](https://doi.org/10.3390/)[ ](https://doi.org/10.3390/)biom13071070  \nAcademic Editors: Wiesława Le´sniakand Anna Filipek  \nReceived: 30 April 2023  \nRevised: 28 June 2023  \nAccepted: 29 June 2023  \nPublished: 3 July 2023  \nCopyright: © 2023 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://](https://)[ ](https://)[creativecommons.org/licenses/by/](creativecommons.org/licenses/by/)[ ](creativecommons.org/licenses/by/)[4.0/](4.0/)) .  \n1 Curida Diatec, 1364 Oslo, Norway  \n2 Department of Oral Biology, Faculty of Dentistry, University of Oslo, 0372 Oslo, Norway  \n3 Department of Biotechnology, Faculty of Applied Ecology, Agricultural Sciences and Biotechnology, Inland Norway University of Applied Sciences, 2317 Hamar, Norway  \n4 Department of Virology, Norwegian Institute of Public Health, 0456 Oslo, Norway  \n5 Christiania Dental Clinic, Malo Dental, 0188 Oslo, Norway  \n* Correspondence: [dipak.sapkota@odont.uio.no](dipak.sapkota@odont.uio.no)  \nAbstract: S100A16 is a member of the S100 protein family. S100A16 is expressed in a variety of human tissues, although at varying levels. S100A16 expression is especially high in tissues rich in epithelial cells. mRNA and protein levels of S100A16 have been reported to be differentially expressed in the majority of human cancers. Functionally, S100A16 has been linked to several aspects of tumorigenesis, for example, cell proliferation, differentiation, migration, invasion, and epithelial-mesenchymal transition (EMT) . Accordingly, S100A16 has been suggested to have both tumour-promoting and suppressive roles in human cancers. S100A16-mediated cellular functions are suggested to be mediated by the regulation of various signaling pathways/proteins including EMT-related proteins E-cadherin and Vimentin, PI3K-AKT, p53, MMP1-1, MMP-2, MMP-9, JNK/p38, etc. In addition to the functional roles, expression of S100A16 has been suggested to have prognostic potential in various cancer types. The aims of this review are to summarise the expression profile, identify common molecular partners and functional roles, and explore the prognostic potential of S100A16 in human cancers.  \nKeywords: S100; EMT; prognosis; biomarkers; proliferation; invasion  \n1. Introduction  \nS100A16 is one of the members of the S100 family of calcium-binding proteins. The S100 protein family consists of 25 known members [1] . The S100A16 gene was originally isolated from an astrocytoma cell line. The S100A16 protein is a small acidic protein comprising 103 amino acids with a molecular weight of 11,801.4 Da and the isoelectric point (pI) of 6.28 [2] . This protein is highly conserved in mammals and is ubiquitously expressed in various human tissues [3] . Similar to other S100 proteins, S100A16 contains two EF-hand motifs consisting of a helix-loop-helix structural domain, where the N-terminal domain is interconnected with the C-terminal domain by a “hinge” linker (Figure 1) . The two EF-hand motifs are the Ca2+ and Zn2+ binding sites of S100A6 protein. S100A16 binds to Zn2+ with a relatively low affinity at a site different from the Ca2+ binding site on the S100A16 protein [4,5] . S100A16 has several unique characteristics compared to other S100 proteins. One of the important features is the presence of only one functional Ca2+ binding site in the C-terminal EF-hand, composed of 12 amino acids per protein monomer [2,5] . The N-terminal EF-hand of S100A16 is comprised of 15 amino acids instead of 14, and it lacks the conserv","cbCaiqJI74xA6orq","https://ap.wps.com/l/cbCaiqJI74xA6orq","pdf",1877031,12,"English","# Abstract\n# Keywords\n# 1. Introduction\n## S100A16 structure and binding features\n## S100A16 cellular functions and molecular interactions\n# Figure 1","[{\"question\":\"What is S100A16 and where is it expressed?\",\"answer\":\"S100A16 is a member of the S100 protein family of calcium-binding proteins. It is expressed in many human tissues, with especially high expression in epithelial cell–rich tissues.\"},{\"question\":\"How is S100A16 linked to cancer biology?\",\"answer\":\"S100A16 is associated with multiple aspects of tumorigenesis, including cell proliferation, differentiation, migration, invasion, and epithelial-mesenchymal transition (EMT). It has been suggested to have both tumor-promoting and suppressive roles.\"},{\"question\":\"Which pathways or mechanisms are proposed to mediate S100A16 functions?\",\"answer\":\"S100A16-mediated functions are linked to regulation of signaling pathways and proteins involved in EMT and cancer progression, including PI3K-AKT, p53, MMPs (MMP-1, -2, -9), and JNK/p38, as well as EMT-related proteins such as E-cadherin and vimentin.\"}]","An Update on S100A16 in Human Cancer | PDF",1790239261]