MMP24 is an extracellular matrix (ECM) degradative peptidase enzyme that is a member of the large family of matrix metalloproteinases (MMP). Each MMP has a different substrate specificity, and the aberrant or derailed expression of these is strongly correlated with unregulated events such as tumor invasion, metastasis, angiogenesis, and arthritis. This is in contrast to the tightly controlled normal physiological processes such as tissue remodeling, reproduction, rebuilding, and embryonic development. Deregulation often occurs through the loss of negative checks. Most MMP's are secreted as inactive proteins which are activated upon cleavage by extracellular proteinases. However, this protein is unusual is that it belongs to the membrane-type MMP (MT-MMP) subfamily – it contains a potential transmembrane domain suggesting that proteins of this subfamily are expressed at the cell surface rather than secreted. MMP24 activates MMP2 by cleavage. MMP24 is ubiquitously expressed in the developing brain but in the adult, is restricted to areas of neuroplasticity. Ross et al performed mapping studies with the MMP24 antibody in their multipotent NT2 cell model for neurogenesis and differentiation1. They detected multiple transcripts in both the multipotent and differentiated neuronal cells, as well as the hippocampus. A recent profiling study from de la Pena’s group at the University of Veracruz evaluated a matrix of MMP and tissue inhibitor of metalloproteinase (TIMP) as biomarkers for advanced human gastric cancer (GC) 2. Using quantitative PCR and immunoblotting on a panel of samples, they identified MMP2, MMP14, MMP24, MMP25, and TIMP3 all as potential candidates for unfavorable GC prognostic markers. A recent Nature Cell Biology publication from Porlan’s lab at the Spanish National Cancer Research Centre highlights how MMP24 may modulate the proliferative status of mammalian adult stem cells by dynamically regulating the cleavage of cell adhesion molecules (CAMs) such as N-cadherin3.
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