MMP9
Description
The MMP9 (matrix metallopeptidase 9) is a protein-coding gene located on chromosome 20.
MMP9 is an enzyme belonging to the matrix metalloproteinase (MMP) family, which are involved in the breakdown of the extracellular matrix (ECM). MMP9 is encoded by the MMP9 gene in humans and is responsible for degrading type IV and V collagens, as well as other ECM proteins. It plays a role in various physiological processes such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning, and memory. It is also involved in pathological processes like arthritis, intracerebral hemorrhage, and metastasis. MMP9 is secreted as an inactive proprotein and activated by extracellular proteinases. Studies have shown that MMP9 is involved in the mobilization of hematopoietic progenitor cells from bone marrow and tissue remodeling associated with tumors. Thrombospondins, proteins found in intervertebral discs, regulate the interaction of MMP9 with MMP2, both of which are key factors in ECM remodeling. MMP9, along with elastase, appears to be a regulatory factor in neutrophil migration across the basement membrane. MMP9 has several important functions within neutrophil action, such as degrading ECM, activating IL-1β, and cleaving several chemokines. In a mouse model, MMP9 deficiency resulted in resistance to endotoxin shock, suggesting that MMP9 is important in sepsis.
MMP9 is a matrix metalloproteinase that plays a crucial role in the breakdown of extracellular matrix (ECM) and in the migration of leukocytes. It has been shown to cleave KiSS1 at a Gly-|-Leu bond, and NINJ1 to generate the Secreted ninjurin-1 form. MMP9 also cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. It degrades fibronectin but not laminin or Pz-peptide.
MMP9 is also known as CLG4B, GELB, MANDP2, MMP-9.
