MMP2 is a peptidase enzyme that belongs to the large family of matrix metalloproteinases (MMPs) which degrade the extracellular matrix (ECM) with different substrate specificities. Aberrant and unregulated expression of MMPs via deregulation of key negative check controls is strongly associated with increased tumor invasiveness, metastasis potential, and angiogenesis. This uncontrolled behavior is in direct contrast to the tightly controlled physiological systems of embryonic development, tissue remodeling, and rebuilding. MMP2 antibody immunostaining was paired with sophisticated computed tomography as viable prognostic indication assessment method for small lung adenocarcinomas1. The Japanese group that did these studies also identified CD34, MMP9, VEGF, and TIMP-2 as other markers. Ribeiro-Silva’s studies in breast cancer used a MMP2 antibody as one component of a panel of thirteen antibodies to create detailed sub-phenotypes of a large pool of basal breast cancer samples2. It was determined that in this particular cancer compartment, only a subset of MMPs (of which MMP2 did not fall under) correlated with uncontrolled tumor properties and phenotypes.
Qian et al investigated lung cancer cell invasiveness with a xenograft nude mice system, and used a MMP2 antibody to prove that the reduction of type 1 insulin-like growth factor receptor (IGF-1R) through siRNA inhibited metastases in an MMP2- and MMP9-dependent fashion3. In some interesting time-resolved analyses of the MMP10 degradome, Schlage’s group employed a MMP2 antibody as part of a workflow based on multiplexed terminal amine isotopic substrate labeling4. Additionally, neuronal axonal growth experiments suggest that substances such as chondroitin sulfate proteoglycans (CSPGs) act as inhibitors, and a MMP2 antibody allowed investigators to identify MMP2 as the key regulator for CSPG degradation and subsequent inhibitory block, thus enabling nerve regeneration5.
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