¿Qué se te perdió aquí? Metaloproteasas de matriz en el núcleo celular
Palabras clave:
Metaloproteasas, núcleo celular, enzimas, biomoléculas, “degradoma”Resumen
Las enzimas capaces de cortar una proteína reciben el nombre de proteasas. Estas biomoléculas regulan una amplia variedad de procesos a nivel celular y de todo el organismo, ya sea por la degradación completa de su sustrato, por el procesamiento específico y limitado del mismo, o bien por el rasurado (shedding en inglés) de ectodominios y liberación de péptidos que pueden desempeñar una función diferente (Pardo et al., 2008). Las proteasas se encuentran en los tres dominios de la vida: archaea, eubacteria y eukarya. Dada su importancia, se ha denominado como “degradoma” al conjunto de proteasas que se expresan en un momento en parti- cular en una célula, tejido u organismo (López-Otín y Overall, 2002). Se clasifican de acuerdo con el aminoácido de su sitio activo en cisteínproteasas, aspartilproteasas, serínproteasas, treonínproteasas, glutamilproteasas y metaloproteasas (Ugalde et al., 2010).
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Afratis, N.A., Selman, M., Pardo, A., et al. (2018). Emerging insights into the role of matrix metalloproteases as therapeutic targets in fibrosis. Matrix Biol. 68-69:167-179.
Aquino-Gálvez, A., y González-Ávila, G. (2010). El papel del factor inducible por hipoxia 1 (HIF-1) en la fibrosis pulmonar idiopática. Neumol Cir Torax. 69(3):170-177.
Cuadrado, E., Rosell, A., y Borrell-Pages, M., (2009). Matrix metalloproteinase-13 is activated and is found in the nucleus of neural cells after cerebral ischemia. J Cereb Blood Flow Metab. 29:398-410.
Eguchi, T., Kubota, S., Kawata, K., et al. (2008). Novel transcription-factor-like function of human matrix metalloproteinase 3 regulating the CTGF⁄CCN2 gene. Mol Cell Biol. 28:2391-2413.
Gaffney, J., Solomonov, I., Zehorai, E., et al. (2015). Multilevel regulation of matrix metalloproteinases in tissue homeostasis indicates their molecular specificity in vivo. Matrix Biol. 44-46:191-9.
Hadler-Olsen, E., Fadnes, B., Sylte, I., et al. (2011). Regulation of matrix metalloproteinase activity in health and disease. FEBS Journal. 278: 28-45.
Herrera, I., Cisneros, J., Maldonado, M., et al. (2013). Matrix metalloproteinase (MMP)-1 induces lung alveolar epithelial cell migration and proliferation, protects from apoptosis, and represses mitochondrial oxygen consumption. J Biol Chem. 288:25964-25975.
Ip, Y.C., Cheung, S.T., y Fan, S.T. (2007). Atypical localization of membrane type 1-matrix metalloproteinase in the nucleus is associated with aggressive features of hepatocellular carcinoma. Mol Carcinog. 46:225–230.
Jara, P., Calyeca, J., Romero, Y., et al. (2015). Matrix metalloproteinase (MMP)-19-deficient fibroblasts display a profibrotic phenotype. Am J Physiol Lung Cell Mol Physiol. 308(6):L511-22.
Kwan, J.A., Schulze, C.J., Wang W., et al. (2004). Matrix metalloproteinase-2 (MMP-2) is present in the nucleus of cardiac myocytes and is capable of cleaving poly (ADP-ribose) polymerase (PARP) in vitro. The FASEB Journal. 1: 690-692.
López-Otín, C., y Overall, C.M. (2002). Protease degradomics: a new challenge for proteomics. Nat Rev Mol Cell Biol 3. 509-519.
Maldonado, M., Salgado-Aguayo, A., Herrera I., et al. (2018). Upregulation and Nuclear Location of MMP28 in Alveolar Epithelium of Idiopathic Pulmonary Fibrosis. Am J Respir Cell Mol Biol. 59(1):77-86.
Marchant, D.J., Bellac, C.L., Moraes, T.J., et al. (2014). A new transcriptional role for matrix metalloproteinase-12 in antiviral immunity. Nature Med. 20:493-502.
Pardo, A., Cabrera, S., Maldonado, M., et al. (2016). Role of matrix metalloproteinases in the pathogenesis of idiopathic pulmonary fibrosis. Respir Res. 17:23.
Pardo, A., Selman, M., y Kaminski, N. (2008). Approaching the degradome in idiopathic pulmonary fibrosis. Int. J. Biochem. Cell Biol. 40:1141-1155.
Plácido, L., Romero, Y., Maldonado, M., et al. (2021). Loss of MT1- MMP in alveolar epithelial cells exacerbates pulmonary fibrosis. Int. J. Mol. Sci. 22:Aceptado.
Raeeszadeh-Sarmazdeh, M., Do, L.D., y Hritz, B.G. (2020). Metalloproteinases and Their Inhibitors: Potential for the Development of New Therapeutics. Cells. 9(5):1313.
Rawlings, N.D., Barrett, A.J., Thomas, P.D., et al. (2018). The MEROPS database of proteolytic enzymes, their substrates and inhibitors in 2017 and a comparison with peptidases in the PANTHER database. Nucleic Acids Res. 46:D624-D632.
Shimizu-Hirota, R., Xiong, W., Baxter, B.T., et al. (2012). MT1-MMP regulates the PI3Kδ•Mi-2/NuRD-dependent control of macrophage immune function. Genes Dev. 26:395-413.
Si-Tayeb, K., Monvoisin, A., Mazzocco, C., et al. (2006). Matrix metalloproteinase 3 is present in the cell nucleus and is involved in apoptosis. Am J Pathol. 169(4):1390-1401.
Tzouvelekis, A., Harokopos, A., Paparountas, T., et al. (2007). Comparative Expression Profiling in Pulmonary Fibrosis Suggests a Role of Hypoxia-inducible Factor-1a in Disease Pathogenesis. Am J RespirCrit Care Med. 176:1108-1119.
Ugalde, A.P., Ordóñez, G.R., Quirós, P.M., et al. (2010). Metalloproteases and the Degradome. En: Clark I. (eds) Matrix Metalloproteinase Protocols. Methods in Molecular Biology (Methods and Protocols). Vol 622. Humana Press: Totowa, NJ. https://doi.org/10.1007/978-1-60327-299-5
Xie, Y., Mustafa, A., Yerzhan, A., et al. (2017). Nuclear matrix metalloproteinases: functions resemble the evolution from the intracellular to the extracellular compartment. Cell death discovery. 3:17036.
Yang, Y., Candelario-Jalil, E., Thompson, J.F., et al. (2010). Increased intranuclear matrix metalloproteinase activity in neurons interferes with oxidative DNA repair in focal cerebral ischemia. J Neurochem. 112:134-149.
