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HSP47 gene expression was analyzed across gastric cancer cell lines and patient tissues, showing significantly higher HSP47 mRNA and protein levels in cancer and tumors versus normal gastric mucosa. Silencing HSP47 with siRNA reduced proliferation, wound healing, migration, and invasion in gastric cancer cells, alongside decreased MMP-7 expression. HSP47 promoter methylation was detected in low-HSP47 SNU-216 cells and most non-cancerous gastric tissues, indicating epigenetic regulation and supporting HSP47-targeted therapy via promoter methylation.",{"@graph":69,"@context":122},[70,84,105],{"@type":71,"itemListElement":72},"BreadcrumbList",[73,77,79,82],{"item":74,"name":75,"@type":76,"position":8},"https://docshare.wps.com","Home","ListItem",{"item":78,"name":9,"@type":76,"position":14},"https://docshare.wps.com/document/",{"item":80,"name":40,"@type":76,"position":81},"https://docshare.wps.com/document/research-report/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/overexpression-of-heat-shock-protein-47-is-associated-with-increased-proliferation-and-metastasis-in-gastric-cancer/332158/",{"url":83,"name":65,"@type":85,"image":86,"author":91,"headline":65,"publisher":94,"fileFormat":97,"inLanguage":63,"description":67,"dateModified":98,"datePublished":99,"encodingFormat":97,"isAccessibleForFree":100,"interactionStatistic":101},"DigitalDocument",{"url":87,"@type":88,"width":89,"height":90},"https://docshare.wps.com/thumbnails/overexpression-of-heat-shock-protein-47-is-associated-with-increased-proliferation-and-metastasis-in-gastric-cancer/332158.png","ImageObject",300,407,{"name":92,"@type":93},"Violet","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-11-04","2026-09-21",true,{"@type":102,"interactionType":103,"userInteractionCount":52},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108,114,118],{"name":109,"@type":110,"acceptedAnswer":111},"What relationship did the study find between HSP47 and gastric cancer progression?","Question",{"text":112,"@type":113},"HSP47 was significantly overexpressed in gastric cancer cell lines and tumor tissues compared with normal gastric mucosa. 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Genomics & Informatics (2024) 22:6 [https://doi.org/10.1186/s44342-024-00010-7](https://doi.org/10.1186/s44342-024-00010-7)  \nGenomics & Informatics  \n RESEARCH Open Access  \nOverexpression of heat shock protein  \n47 is associated with increased proliferation and metastasis in gastric cancer  \nJieun Lee1, Jung‑Ah Hwang2, Seung‑Hyun Hong2, Seon‑Young Kim3, Donghyeok Seol1, Il Ju Choi4 and Yeon‑Su Lee5*  \nAbstract  \nHere, we investigated that the heat shock protein 47 (HSP47) plays a crucial role in the progression of gastric cancer (GC) . We analyzed HSP47 gene expression in GC cell lines and patient tissues. The HSP47 mRNA and protein expres‑ sion levels were significantly higher in GC cell lines and tumor tissues compared to normal gastric mucosa. Using siRNA to silence the expression of HSP47 in GC cells resulted in a significant reduction in their proliferation, wound healing, migration, and invasion capacities. Additionally, we also showed that the mRNA expression of matrix metal‑ lopeptidase‑7 (MMP‑7), a metastasis‑promoting gene, was significantly reduced in HSP47 siRNA‑transfected GC cells. We confirmed that the HSP47 promoter region was methylated in the SNU‑216 GC cell line expressing low levels of HSP47 and in most non‑cancerous gastric tissues. It means that the expression of HSP47 is regulated by epigenetic regulatory mechanisms. These findings suggest that targeting HSP47, potentially through its promoter methylation, could be a useful new therapeutic strategy for treating GC.  \nKeywords HSP47, SERPINH1, Proliferation, MMP‑7, Promoter methylation  \n1 Introduction  \nGastric cancer (GC) is the fifth most common malignancy and the fourth leading cause of cancer-related deaths in the world [1]. In an effort to identify novel genes related to GC progression that can be used to understand GC development, we previously profiled gene expression in human GC and adjacent normal tissues [2].  \n*Correspondence: Yeon‑Su Lee [yslee2@ncc. re.kr](yslee2@ncc. re.kr)  \n1 Department of Surgery, Seoul National University Bundang Hospital, Seongnam, Republic of Korea  \n2 Genomics Core Facility, Research Core Center, Research Institute, National Cancer Center, Goyang, Republic of Korea  \n3 Enzynomics Co. Ltd, Daejeon, Republic of Korea  \n4 Center for Gastric Cancer, National Cancer Center, Goyang, Republic of Korea  \n5 Rare Cancer Branch, Research Institute, National Cancer Center, Goyang, Republic of Korea  \nOne gene, serpin peptidase inhibitor, clade H, member 1 (SERPINH1), the gene encoding HSP47, was upregulated in gastric tumor tissues.  \nHSP47 belongs to the serine protease inhibitor (serpin) superfamily, but has no protease inhibitor activity [3]. It was originally discovered as a cell surface collagen-binding protein, colligin, and was later shown to be an endoplasmic reticulum (ER) resident protein [4, 5]. HSP47 is a collagen-specific molecular chaperone that promotes the correct folding of type I and IV procollagen and prevents the aggregation of collagen molecules within the ER [6]. Under stress conditions, HSP47 expression is upregulated, and it acts as a molecular chaperone that mitigates cell damage from elevated temperature, heavy metals, and oxidative stress [7]. HSP47 has been identified as being overexpressed in various cancers, including cervical cancer [8], breast cancer [9], glioblastoma [10], and colorectal cancer [11]. In the case of breast cancer,  \n© The Author(s) 2024. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If mat","cbCainsGtDlKNV7a","https://ap.wps.com/l/cbCainsGtDlKNV7a","pdf",2057025,"English","# Abstract\n# 1 Introduction\n## Gastric cancer background and motivation\n# 2 Methods\n## 2.1 Cell lines and cell culture","[{\"question\":\"What relationship did the study find between HSP47 and gastric cancer progression?\",\"answer\":\"HSP47 was significantly overexpressed in gastric cancer cell lines and tumor tissues compared with normal gastric mucosa. The study indicates HSP47 supports progression by influencing proliferation and metastatic behaviors.\"},{\"question\":\"How did silencing HSP47 affect gastric cancer cells?\",\"answer\":\"Using siRNA to silence HSP47 reduced gastric cancer cell proliferation, wound healing, migration, and invasion. It also lowered MMP-7 mRNA levels in transfected cells.\"},{\"question\":\"What evidence supports an epigenetic mechanism for HSP47 regulation?\",\"answer\":\"The HSP47 promoter region was methylated in the SNU-216 cell line with low HSP47 expression and in most non-cancerous gastric tissues. This pattern suggests promoter methylation contributes to HSP47 expression control.\"}]","Overexpression of heat shock protein 47 is associated with increased proliferation and metastasis in gastric cancer | PDF",1789997090,23]