[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"doc-seo-331887-105":3,"detail-sidebar-cat-0-en-105":81,"doc-detail-331887-en":131},{"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","parkin-inhibits-proliferation-and-migration-of-bladder-cancer-via-ubiquitinating-catalase","Parkin inhibits proliferation and migration of bladder cancer via ubiquitinating Catalase","","Parkin (PRKN) is known for its role in mitophagy in Parkinson’s disease, but its function in bladder cancer (BLCA) remained unclear. This study analyzed PRKN expression across human BLCA cohorts and found low PRKN levels, with Parkin acting as a tumor suppressor. Mechanistically, Parkin inhibited BLCA cell proliferation and migration in a mitophagy-independent manner by directly binding and regulating the antioxidant enzyme Catalase to control intracellular ROS. Catalase knockdown increased ROS and suppressed growth and migration, whereas Catalase upregulation had the opposite effect. Parkin upregulation partially restored these outcomes, and USP30 deubiquitinated and stabilized Catalase, identifying a potential therapeutic target.",{"@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/research-report/","Research & Report",3,{"item":32,"name":10,"@type":21,"position":33},"https://docshare.wps.com/document/parkin-inhibits-proliferation-and-migration-of-bladder-cancer-via-ubiquitinating-catalase/331887/",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/parkin-inhibits-proliferation-and-migration-of-bladder-cancer-via-ubiquitinating-catalase/331887.png","ImageObject",300,407,{"name":42,"@type":43},"Anda","Person",{"url":19,"name":45,"@type":46},"DocShare","Organization","application/pdf","2026-10-26","2026-09-21",true,{"@type":52,"interactionType":53,"userInteractionCount":55},"InteractionCounter",{"@type":54},"ViewAction",11,{"@type":57,"mainEntity":58},"FAQPage",[59,65,69],{"name":60,"@type":61,"acceptedAnswer":62},"What role does Parkin play in bladder cancer cells?","Question",{"text":63,"@type":64},"PRKN expression is low in BLCA, and Parkin suppresses BLCA cell proliferation and migration. This effect occurs in a mitophagy-independent manner.","Answer",{"name":66,"@type":61,"acceptedAnswer":67},"How does Parkin influence Catalase and reactive oxygen species (ROS)?",{"text":68,"@type":64},"Parkin binds to Catalase and affects its regulation, which changes intracellular ROS levels during cancer progression. Higher ROS suppress proliferation and migration, while lower ROS promotes growth and migration.",{"name":70,"@type":61,"acceptedAnswer":71},"What is the relationship between USP30 and Catalase stability in this study?",{"text":72,"@type":64},"USP30, a known Parkin substrate, can deubiquitinate and stabilize Catalase. This provides a mechanistic link between Parkin signaling and ROS regulation in BLCA.","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},331887,1790193148,{"code":4,"msg":82,"data":83},"success",[84,88,92,96,101,106,111,115,120,123,127],{"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":97,"doc_module":4,"doc_module_name":25,"category_name":98,"show_sort_weight":99,"slug":100},5,"Comic",60,"comic",{"id":102,"doc_module":4,"doc_module_name":25,"category_name":103,"show_sort_weight":104,"slug":105},6,"Technology",50,"technology",{"id":107,"doc_module":4,"doc_module_name":25,"category_name":108,"show_sort_weight":109,"slug":110},7,"Healthcare",40,"healthcare",{"id":112,"doc_module":4,"doc_module_name":25,"category_name":29,"show_sort_weight":113,"slug":114},8,30,"research-report",{"id":116,"doc_module":4,"doc_module_name":25,"category_name":117,"show_sort_weight":118,"slug":119},9,"Religion & Spirituality",20,"religion-spirituality",{"id":118,"doc_module":4,"doc_module_name":25,"category_name":121,"show_sort_weight":118,"slug":122},"World Cup","world-cup",{"id":124,"doc_module":4,"doc_module_name":25,"category_name":125,"show_sort_weight":124,"slug":126},10,"Lifestyle","lifestyle",{"id":128,"doc_module":4,"doc_module_name":25,"category_name":129,"show_sort_weight":97,"slug":130},19,"General","general",{"code":4,"msg":82,"data":132},{"doc_id":79,"user_id":133,"nickname":42,"user_avatar":134,"doc_module":4,"category_id":112,"category_name":29,"doc_title":10,"doc_description":12,"doc_content":135,"file_id":136,"file_url":137,"file_type":138,"file_size":139,"view_count":55,"is_deleted":4,"is_public":22,"is_downloadable":22,"audit_status":22,"page_count":140,"language":141,"language_code":8,"site_id":7,"html_lang":8,"table_of_contents":142,"faqs":143,"seo_title":144,"seo_description":12,"update_tm":145,"read_time":109,"preview_page_count":4},962075006959,"https://ap-avatar.wpscdn.com/avatar/e0002397efbe92a78e?_k=1776741047341049297","communications biology Article  \n\n| \u003Cbr>[https://doi.org/10.1038/s42003-024-05935-x](https://doi.org/10.1038/s42003-024-05935-x) |  |\n| --- | --- |\n| Parkin inhibits proliferation and migration of bladder cancer via ubiquitinating Catalase\u003Cbr> Check for updates |  |\n| Renjie Zhang1,8, Wenyu Jiang1,8, Gang Wang 2,8, Yi Zhang 3,4, Wei Liu5, Mingxing Li1, Jingtian Yu1, Xin Yan1, Fenfang Zhou6, Wenzhi Du1, Kaiyu Qian 1,2, Yu Xiao 1,2, Tongzu Liu1 , Lingao Ju 2  & Xinghuan Wang 1,7  |  |\n| PRKN is a key gene involved in mitophagy in Parkinson’s disease. However, recent studies have demonstrated that it also plays a role in the development and metastasis of several types of cancers, both in a mitophagy-dependent and mitophagy-independent manner. Despite this, the potential effects and underlying mechanisms of Parkin on bladder cancer(BLCA)remain unknown. Therefore, in this study, we investigated the expression of Parkin in various BLCA cohorts derived from human. Here we show that PRKN expression was low and that PRKN acts as a tumor suppressor by inhibiting the proliferation and migration of BLCA cells in a mitophagy-independent manner. We further identified Catalase as a binding partner and substrate of Parkin, which is an important antioxidant enzyme that regulates intracellular ROS levels during cancer progression. Our data showedthat knockdown of CAT led to increased intracellular ROS levels, which suppressed cell proliferation and migration. Conversely, upregulation of Catalase decreased intracellular ROS levels, promoting cell growth and migration. Importantly, we found that Parkin upregulation partially restored these effects. Moreover, we discovered that USP30, a known Parkin substrate, could deubiquitinate and stabilize Catalase. Overall, our study reveals a novel function of Parkin and identifies a potential therapeutic target in BLCA. |  |\n| As the global population ages, cancer is predicted to become the leading cause of death worldwide by 20301,2. Bladder cancer (BLCA) is projected tobe the fourth most common cancer in men in the United States, with death from BLCA ranking eighth by 20233. BLCA is classified into non-muscleinvasive bladder cancer (NMIBC) and muscle-invasive bladder cancer (MIBC) based on clinical characteristics. NMIBC has a better prognosis but is more prone to relapse, while MIBC diagnosis is often accompanied by distant metastases, leading to a poor prognosis4. The incidence of BLCA is closely related to risk factors such as smoking and exposure to benzidine. Increasing evidence suggests that the imbalance between oxidants and antioxidants may play a pivotal role in the development of BLCA5. | Therefore, gaining a comprehensive understanding of the underlying biological mechanisms of BLCA progression and metastasis is crucial in discovering new therapeutic approaches.\u003Cbr>The ubiquitin protease system (UPS) is a critical epigenetic modification involved in the entire process of tumor development and progression6. Parkin, encoded by the PRKN gene, is an E3 ubiquitin ligase initially identified in autosomal recessive inherited juvenile Parkinson’s disease7. Subsequent research revealed that phosphorylation of Parkin by phosphatase and tensin homolog (PTEN)-induced kinase 1(PINK-1) has aneuroprotective function by removing damaged mitochondria through mitophagy8. In recentyears, increasing studies and reviews have emphasized |\n\n1Department of Urology, Laboratory of Precision Medicine, Zhongnan Hospital of Wuhan University, Wuhan, China. 2Department of Biological Repositories, Human Genetic Resources Preservation Center of Hubei Province, Hubei Key Laboratory of Urological Diseases, Zhongnan Hospital of Wuhan University, Wuhan, China. 3Euler Technology, ZGC Life Sciences Park, Beijing, China. 4Center for Quantitative Biology, School of Life Sciences, Peking University, Beijing, China. 5Department of Urology, Peking University Aerospace Center Hospital, Beijing, China. 6Department of Radiology, Zhongnan Hospit","cbCaiqYRTlGxmxyg","https://ap.wps.com/l/cbCaiqYRTlGxmxyg","pdf",3200134,16,"English","# Background\n# Parkin and PRKN in bladder cancer\n## Oxidative stress and ROS in tumor development\n# Parkin inhibits BLCA proliferation and migration\n## Catalase as a Parkin binding partner and substrate\n# Catalase regulation and ROS control\n## Knockdown and upregulation effects\n# USP30-mediated deubiquitination of Catalase\n# Therapeutic implications for BLCA","[{\"question\":\"What role does Parkin play in bladder cancer cells?\",\"answer\":\"PRKN expression is low in BLCA, and Parkin suppresses BLCA cell proliferation and migration. This effect occurs in a mitophagy-independent manner.\"},{\"question\":\"How does Parkin influence Catalase and reactive oxygen species (ROS)?\",\"answer\":\"Parkin binds to Catalase and affects its regulation, which changes intracellular ROS levels during cancer progression. Higher ROS suppress proliferation and migration, while lower ROS promotes growth and migration.\"},{\"question\":\"What is the relationship between USP30 and Catalase stability in this study?\",\"answer\":\"USP30, a known Parkin substrate, can deubiquitinate and stabilize Catalase. This provides a mechanistic link between Parkin signaling and ROS regulation in BLCA.\"}]","Parkin inhibits proliferation and migration of bladder cancer via ubiquitinating Catalase | PDF",1789995631]