{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMatrix metalloproteinase‐2 (MMP2) is a zinc‐dependent protease that plays a pivotal role in remodeling the extracellular matrix (ECM) under normal as well as stress‐induced conditions. In physiological settings MMP2 contributes to embryonic development, angiogenesis, and tissue repair by precisely degrading ECM proteins. Endothelial cells, for example, can shed MMP2‐containing vesicles to locally regulate vessel formation and promote coordinated capillary morphogenesis. In addition, intracellular roles of MMP2 have been uncovered in cardiac myocytes—where its proteolytic activity on sarcomeric proteins is implicated in ischemia/reperfusion injury—and in the clearance of extracellular amyloid‐beta by astrocytes, emphasizing its importance in maintaining tissue homeostasis. Moreover, MMP2 sensitivity is being exploited for stimulus‐responsive drug delivery strategies that aim to improve tumor targeting and intracellular drug release."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, MMP2 is frequently hijacked to promote tumor progression and metastasis. Its expression and proteolytic activity facilitate cancer cell invasion by degrading basement membranes and ECM barriers, thereby enhancing both the intravasation of primary tumor cells and their colonization at distant sites. Various studies have demonstrated that MMP2 up‐regulation—often stimulated by pro‐inflammatory cytokines, growth factors, and transcriptional regulators such as TGFβ or Snail—contributes to enhanced tumor cell adhesion, migration, and angiogenesis in malignancies ranging from breast and ovarian carcinomas to non‐small cell lung cancer and even retinoblastoma. In addition, epigenetic changes (for instance, those induced by histone deacetylase inhibitors) as well as paracrine interactions within the tumor microenvironment further modulate MMP2 expression. Collectively, these findings have established MMP2 as a key target not only for prognostic evaluation but also for therapeutic intervention in cancer."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in normal tissue remodeling and cancer, aberrant MMP2 activity is increasingly recognized in a variety of vascular, inflammatory, and fibrotic disorders. Elevated MMP2 has been associated with adverse vascular remodeling in coronary aneurysms and atherosclerotic plaques, as well as with abnormal ECM turnover in conditions such as Crohn’s disease and endometriosis. In addition, MMP2 facilitates leukocyte extravasation by cleaving junctional proteins in the blood–tissue barrier, a mechanism implicated in both central nervous system infiltration by hematologic malignancies and in the chronic inflammation observed in obesity. Together, these studies highlight the multifaceted contribution of MMP2 to pathological ECM degradation and underscore its potential as a diagnostic and therapeutic target in diverse non‐cancerous conditions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "29"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Giulia Taraboletti, Sandra D'Ascenzo, Patrizia Borsotti, et al. 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