MMP24

This gene encodes a member of the peptidase M10 family of matrix metalloproteinases (MMPs). Proteins in this family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. The encoded preproprotein is proteolytically processed to generate the mature protease. Unlike most MMPs, which are secreted, this protease is a member of the membrane-type MMP (MT-MMP) subfamily, contains a transmembrane domain and is expressed at the cell surface. Substrates of this protease include the proteins cadherin 2 and matrix metallopeptidase 2 (also known as 72 kDa type IV collagenase).

MATRIX METALLOPEPTIDASE 24

Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity).

Cell-cell adhesion mediated by cadherin Source: UniProtKB
Cell-cell adhesion via plasma-membrane adhesion molecules Source: UniProtKB
Collagen catabolic process Source: GO_Central
Detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
Extracellular matrix organization Source: GO_Central
Glial cell differentiation Source: UniProtKB
Neuronal stem cell population maintenance Source: UniProtKB
Proteolysis Source: UniProtKB

Matrix metalloproteinase-24:
Plasma membrane
Cell membrane
Golgi apparatus
trans-Golgi network membrane
Note: Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3.
Processed matrix metalloproteinase-24:
Extracellular region or secreted
extracellular matrix
Note: Also shed from cell surface as soluble proteinase, by a proteolytic cleavage.

Extracellular: 53-602
Helical: 603-623
Cytoplasmic: 624-645

Cleaved by a furin endopeptidase in the trans-Golgi network.