Palacios Serrato EG, Medina-Abreu KH, Oropeza-Martínez E, Jacinto-Alemán LF, Macías-Silva M, Tecalco-Cruz AC. ADAMTS-8 and kallikrein-related peptidases 10 and 5 proteases also have a tumor suppression role. World J Clin Oncol 2025; 16(11): 110202 [DOI: 10.5306/wjco.v16.i11.110202]
Corresponding Author of This Article
Angeles C Tecalco-Cruz, PhD, Full Professor, Posgrado en Ciencias Genómicas, Universidad Autónoma de la Ciudad de México, Colonia Del Valle, San Lorenzo 290, Mexico City 03100, Mexico. angeles.tecalco@uacm.edu.mx
Research Domain of This Article
Oncology
Article-Type of This Article
Minireviews
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
Nov 24, 2025 (publication date) through Nov 21, 2025
Times Cited of This Article
Times Cited (0)
Journal Information of This Article
Publication Name
World Journal of Clinical Oncology
ISSN
2218-4333
Publisher of This Article
Baishideng Publishing Group Inc, 7041 Koll Center Parkway, Suite 160, Pleasanton, CA 94566, USA
Share the Article
Palacios Serrato EG, Medina-Abreu KH, Oropeza-Martínez E, Jacinto-Alemán LF, Macías-Silva M, Tecalco-Cruz AC. ADAMTS-8 and kallikrein-related peptidases 10 and 5 proteases also have a tumor suppression role. World J Clin Oncol 2025; 16(11): 110202 [DOI: 10.5306/wjco.v16.i11.110202]
World J Clin Oncol. Nov 24, 2025; 16(11): 110202 Published online Nov 24, 2025. doi: 10.5306/wjco.v16.i11.110202
ADAMTS-8 and kallikrein-related peptidases 10 and 5 proteases also have a tumor suppression role
Eva G Palacios Serrato, Karen H Medina-Abreu, Enrique Oropeza-Martínez, Luis Fernando Jacinto-Alemán, Marina Macías-Silva, Angeles C Tecalco-Cruz
Eva G Palacios Serrato, Karen H Medina-Abreu, Enrique Oropeza-Martínez, Angeles C Tecalco-Cruz, Posgrado en Ciencias Genómicas, Universidad Autónoma de la Ciudad de México, Mexico City 03100, Mexico
Luis Fernando Jacinto-Alemán, Departamento de Medicina y Patología, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico
Marina Macías-Silva, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico
Author contributions: Palacios Serrato EG researched, wrote, and integrated the information in the manuscript, tables, and figures; Medina-Abreu KH, Oropeza-Martínez E, and Jacinto-Alemán LF researched and wrote some parts of the manuscript and tables; Macías-Silva M participated in editing and improving the manuscript; Tecalco-Cruz AC designed this research, discussed, and integrated the manuscript; and all authors approved the final manuscript.
Supported by Colegio de Ciencia y Tecnologia de la Universidad Autónoma de la Ciudad de México, No. UACM- CCyT-2025-CON-11.
Conflict-of-interest statement: All the authors report no relevant conflicts of interest for this article.
Open Access: This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: https://creativecommons.org/Licenses/by-nc/4.0/
Corresponding author: Angeles C Tecalco-Cruz, PhD, Full Professor, Posgrado en Ciencias Genómicas, Universidad Autónoma de la Ciudad de México, Colonia Del Valle, San Lorenzo 290, Mexico City 03100, Mexico. angeles.tecalco@uacm.edu.mx
Received: June 3, 2025 Revised: July 2, 2025 Accepted: October 10, 2025 Published online: November 24, 2025 Processing time: 174 Days and 9.6 Hours
Abstract
Proteases are essential for homeostasis, and their primary function is proteolytic in extracellular and intracellular compartments. The deregulation of expression, abundance, and activity of proteases has been related to several pathologies, including cancer. This deregulation contributes to their pro-tumorigenic activity since they participate in the degradation of extracellular matrix components and adhesion molecules, and the activation of growth factors. However, some proteases, such as ADAM metallopeptidase with thrombospondin type 1 motif 8 and kallikrein-related peptidases 5 and 10, have emerged as tumor suppressors due to their antitumoral actions in specific cancer contexts. In this article, we discuss the antitumoral effects of ADAM metallopeptidase with thrombospondin type 1 motif 8, kallikrein-related peptidases 5 and 10 that have been described to date, suggesting their potential use as novel biomarkers and therapeutic targets in cancer.
Core Tip: In this article, we explore the published information on two proteases of the kallikrein family, kallikrein-related peptidases 5 and 10, and one metallopeptidase with a thrombospondin motif, ADAM metallopeptidase with thrombospondin type 1 motif 8, which are suggested to be both tumor suppressors and protumoral factors, depending on cancer context and stage.
