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This study evaluates the presence, activity, and expression of gelatinases A (MMP-2) and B (MMP-9) in human renal carcinoma using Western blot and ELISA for content, with fluorimetric analysis for actual and specific activity, supported by zymograms. MMP-9 shows higher content but lower specific activity, suggesting predominant inactive localization in tumor tissue, while both enzymes’ activity increases with tumor grade.",{"@graph":69,"@context":114},[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":35,"@type":76,"position":81},"https://docshare.wps.com/document/healthcare/",3,{"item":83,"name":65,"@type":76,"position":19},"https://docshare.wps.com/document/higher-content-but-no-specic-activity-in-gelatinase-b-mmp-9-compared-with-gelatinase-a-mmp-2-in-human-renal-carcinoma/381862/",{"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/higher-content-but-no-specic-activity-in-gelatinase-b-mmp-9-compared-with-gelatinase-a-mmp-2-in-human-renal-carcinoma/381862.png","ImageObject",300,407,{"name":92,"@type":93},"Kurz","Person",{"url":74,"name":95,"@type":96},"DocShare","Organization","application/pdf","2026-10-30","2026-09-24",true,{"@type":102,"interactionType":103,"userInteractionCount":34},"InteractionCounter",{"@type":104},"ViewAction",{"@type":106,"mainEntity":107},"FAQPage",[108],{"name":109,"@type":110,"acceptedAnswer":111},"What does the study conclude about MMP-9 versus MMP-2 in renal carcinoma?","Question",{"text":112,"@type":113},"MMP-9 shows higher content but lower specific activity than MMP-2 in both tumor grades, indicating that MMP-9 is largely present in an inactive form in cancer tissue.","Answer","https://schema.org",{"og:url":83,"og:type":116,"og:title":65,"og:site_name":95,"og:description":67},"article",{"robots":118,"canonical":83},"index,follow",{"doc_id":120,"site_id":62},381862,1790763934,{"code":4,"msg":5,"data":123},{"doc_id":120,"user_id":124,"nickname":92,"user_avatar":125,"doc_module":4,"category_id":34,"category_name":35,"doc_title":65,"doc_description":67,"doc_content":126,"file_id":127,"file_url":128,"file_type":129,"file_size":130,"view_count":34,"is_deleted":4,"is_public":8,"is_downloadable":8,"audit_status":8,"page_count":131,"language":132,"language_code":63,"site_id":62,"html_lang":63,"table_of_contents":133,"faqs":134,"seo_title":135,"seo_description":67,"update_tm":136,"read_time":137},2336478945635,"https://ap-avatar.wpscdn.com/davatar_6f874abed73319feea01a86fa6f0fab8","cancers   \nArticle  \nHigher Content but No Specific Activity in Gelatinase B (MMP-9) Compared with Gelatinase A (MMP-2) in Human Renal Carcinoma  \nGrzegorz Młynarczyk 1, *, Monika Gudowska-Sawczuk 2, Barbara Mroczko 2,3, Marta Bruczko-Goralewska 4, Lech Romanowicz 4 and Anna Tokarzewicz 4  \nCitation: Młynarczyk, G.; Gudowska-Sawczuk, M.; Mroczko, B.; Bruczko-Goralewska, M.;  \nRomanowicz, L.; Tokarzewicz, A. Higher Content but No Specific Activity in Gelatinase B (MMP-9) Compared with Gelatinase A (MMP-2) in Human Renal Carcinoma. Cancers 2023, 15, 5475. [https://](https://)  \n[doi.org/10.3390/cancers15225475](doi.org/10.3390/cancers15225475)[ ](doi.org/10.3390/cancers15225475)Academic Editors: Roberta Mazzucchelli and Giovanni Tossetta  \nReceived: 19 October 2023  \nRevised: 8 November 2023  \nAccepted: 18 November 2023  \nPublished: 20 November 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 Department of Urology, Medical University of Białystok, 15-089 Białystok, Poland  \n2 Department of Biochemical Diagnostics, Medical University of Białystok, 15-269 Białystok, Poland; [monika.gudowska-sawczuk@umb.edu.pl](monika.gudowska-sawczuk@umb.edu.pl) (M.G.-S.); [mroczko@umb.edu.pl](mroczko@umb.edu.pl) (B.M.)  \n3 Department of Neurodegeneration Diagnostics, Medical University of Bialystok, 15-269 Białystok, Poland  \n4 Department of Medical Biochemistry, Medical University of Białystok, 15-089 Białystok, Poland; [marta.bruczko-goralewska@umb.edu.pl](marta.bruczko-goralewska@umb.edu.pl) (M.B.-G.); [lech.romanowicz@umb.edu.pl](lech.romanowicz@umb.edu.pl) (L.R.); [anna.tokarzewicz@umb.edu.pl](anna.tokarzewicz@umb.edu.pl) (A.T.)  \n* [Correspondence: mlynarz36@yahoo.pl](Correspondence: mlynarz36@yahoo.pl)  \nSimple Summary: Gelatinases are one of the major groups of matrix metalloproteinases. Gelatinase A which known as matrix metalloproteinase-2 and gelatinase B referred to as matrix metalloproteinase-9 play a crucial role in breaking down gelatin and various components of the extracellular matrix, including denatured collagen. It has been observed that, in cancer gelatinases are often associated with an-giogenesis, tumor invasion and metastasis.Matrix metalloproteinases have been studied for their involvement in the progression of various tumors in recent years. This paper analyses the contribu-tion of gelatinases A and B in human renal carcinoma pathogenesis, showing their opposite action both at the stage of extracellular matrix remodeling and at different stages of renal tumor devel-opment. Based on the obtained results, MMP-9 showed higher content and lower specific activity compared with MMP-2 .  \nAbstract: Gelatinases belong to a group of enzymes known as matrix metalloproteinases (MMPs) . Gelatinases A and B (MMP-2 and MMP-9, respectively) are the enzymes with the highest ability to destroy collagen, primarily type IV collagen, which is an essential component of the base membrane. Hence, it can be assumed that they are involved, among other things, with the metastasis process of cancer. As a result, the objective of this study was to assess the presence, activity, and expression of selected gelatinases in human renal cancer. Healthy (n = 20) and clear-cell kidney cancer tissue samples (G2 n = 10, G3 n = 10) were analyzed. The presence and content of MMPs were measured using the Western blot and ELISA methods, respectively. The activity (actual and specific) was analyzed with a fluorimetric method. The presence of both investigated enzymes was demonstrated in the representative zymogram. MMP-9 showed the most intensive saturation. It has been observed that both gelatinases occur primarily in high molecular complexes in the hum","cbCaivaVHAJqhym5","https://ap.wps.com/l/cbCaivaVHAJqhym5","pdf",2292043,13,"English","# Introduction\n## Background on renal extracellular matrix and gelatinases\n# Abstract\n## Study objective and methods\n## Key findings on MMP-2 and MMP-9","[{\"question\":\"What does the study conclude about MMP-9 versus MMP-2 in renal carcinoma?\",\"answer\":\"MMP-9 shows higher content but lower specific activity than MMP-2 in both tumor grades, indicating that MMP-9 is largely present in an inactive form in cancer tissue.\"}]","Higher Content but No Specific Activity in Gelatinase B (MMP-9) Compared with Gelatinase A (MMP-2) in Human Renal Carcinoma | PDF",1790247501,33]