Matrix metalloproteinases (MMPs) are a family of extracellular enzymes that regulate development and physiological processes by degrading extracellular matrix (ECM) components. They play critical roles in cell migration, invasion, proliferation, and apoptosis, and are involved in various developmental processes such as branching morphogenesis, angiogenesis, wound healing, and ECM degradation. MMPs are synthesized as proenzymes and activated by the removal of an amino-terminal propeptide, which is regulated by interactions with a cysteine residue and zinc in the active site. They are inhibited by tissue inhibitors of metalloproteinases (TIMPs). There are over 20 MMPs, divided into subgroups based on their substrates and structural domains. MMPs are essential for cell migration, as they help cells overcome ECM barriers by degrading ECM molecules, altering the ECM microenvironment, and modulating the activity of biologically active molecules. They are also involved in tissue morphogenesis, ECM remodeling, and the regulation of cell proliferation and apoptosis. MMPs can modulate the activity of growth factors, cytokines, and other molecules by cleaving them or releasing them from bound stores. They also regulate the balance of protease activity by cleaving enzymes or their inhibitors. MMPs are involved in various developmental processes, including implantation, wound healing, and mammary development. In implantation, MMP-9 is crucial for trophoblast migration and ECM degradation. In wound healing, MMPs are required for keratinocyte migration and ECM remodeling. In mammary development, MMPs are involved in ductal branching and alveolar formation. In bone development, MMP-9 and MT1-MMP are essential for endochondral ossification and bone remodeling. MMPs also play a role in the regulation of angiogenesis by modulating the availability of angiogenic factors such as VEGF. They can generate angiogenic inhibitors such as angiostatin and endostatin through proteolytic cleavage. MMPs can also modulate the activity of other proteinases by activating or inactivating them. However, the exact roles of MMPs in development are still being elucidated, and further studies are needed to fully understand their functions.Matrix metalloproteinases (MMPs) are a family of extracellular enzymes that regulate development and physiological processes by degrading extracellular matrix (ECM) components. They play critical roles in cell migration, invasion, proliferation, and apoptosis, and are involved in various developmental processes such as branching morphogenesis, angiogenesis, wound healing, and ECM degradation. MMPs are synthesized as proenzymes and activated by the removal of an amino-terminal propeptide, which is regulated by interactions with a cysteine residue and zinc in the active site. They are inhibited by tissue inhibitors of metalloproteinases (TIMPs). There are over 20 MMPs, divided into subgroups based on their substrates and structural domains. MMPs are essential for cell migration, as they help cells overcome ECM barriers by degrading ECM molecules, altering the ECM microenvironment, and modulating the activity of biologically active molecules. They are also involved in tissue morphogenesis, ECM remodeling, and the regulation of cell proliferation and apoptosis. MMPs can modulate the activity of growth factors, cytokines, and other molecules by cleaving them or releasing them from bound stores. They also regulate the balance of protease activity by cleaving enzymes or their inhibitors. MMPs are involved in various developmental processes, including implantation, wound healing, and mammary development. In implantation, MMP-9 is crucial for trophoblast migration and ECM degradation. In wound healing, MMPs are required for keratinocyte migration and ECM remodeling. In mammary development, MMPs are involved in ductal branching and alveolar formation. In bone development, MMP-9 and MT1-MMP are essential for endochondral ossification and bone remodeling. MMPs also play a role in the regulation of angiogenesis by modulating the availability of angiogenic factors such as VEGF. They can generate angiogenic inhibitors such as angiostatin and endostatin through proteolytic cleavage. MMPs can also modulate the activity of other proteinases by activating or inactivating them. However, the exact roles of MMPs in development are still being elucidated, and further studies are needed to fully understand their functions.