Multifaceted Roles of Matrix Metalloproteinase-2 (MMP2) in Normal and Disease State

Mon, 03/21/2016 - 13:25

MMP2 is a 72 kDa enzymatic protein and it belongs to matrix metalloproteinases (MMPs), a heterogenous family of zinc/calcium-dependent TIMPs (tissue inhibitors of matrix metalloproteinases) regulated matrix-degrading endopeptidases which are classified into collagenases (MMP-1, -8, -13, -18), gelatinases (MMP-2, -9), stromelysins (MMP-3, -7, -10, -11), elastase (MMP-12), and membrane-type matrix metalloproteinases (MT-MMP-1 through -5) (1). MMP2 involves in extracellular matrix metabolism and cleaves type IV collagen along with degrading the already denatured collagens. TIMP2 and MT-MMP1 (membrane type MMP, MMP14) regulate the activity of MMP2, and the cleavage of pro-MMP2 to active-MMP2 is dependent upon MMP14. MMP2 is expressed ubiquitously and it implicates in a diverse array of functions such as vasculature remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. Mutations in MMP2 gene has been linked to multicentric osteolysis, nodulosis, and arthropathy (MONA), a chronic skeleton disorder caused by matrix metalloproteinase 2 (MMP2) deficiency and characterized by facial dysmorphism, subcutaneous fibrocollagenous nodules, carpal and tarsal osteolysis and interphalangeal joint erosions. MMP2 is emerging as a critical target in various sub-disciplines of experimental biology as well as in clinical diagnostics.

MMP2 antibody



MMP2 antibodies

MMP2 Antibody (clone 8B4) [NB200-114] [10 Publications] Western blot analysis of MMP2 protein in samples containing pro-MMP2 (Lane 1), active MMP2 (Lane 2) and a lysate of human pressure ulcer biopsy (Lane 3). The antibody detected the 72 kDa pro-MMP2 as well as the 66kDa active-MMP2 bands.


MMP-2 Antibody [NB200-193] [21 Publications] IHC analysis of a formalin fixed and paraffin embedded tissue section of human hepatic carcinoma using MMP2 antibody with HRP-DAB detection followed by hematoxylin counterstaining. The cancer cells depicted a specific cytoplasmic positivity for MMP2 protein.

Novus Biologicals offers several different MMP2 Antibodies in their unconjugated as well as in multiple pre-conjugated formats. Novus’ MMP2 Antibodies are cited in many publications from highly reputed biomedical journals.

Recently, Kendziorski and Belcher (2015) from University of Cincinnati employed Novus’ MMP2 antibody (NB200-193) for Western blot application on uterine lysates from control CD-1 mice, C57Bl/6N mice and 30 ppm BPA-exposed CD-1 mice. The antibody detected pro and active MMP2 forms, and the activity of MMP2 was found to be decreased with BPA exposure. MMP2 antibody was also used for IHC on formalin fixed paraffin embedded sections of uterus and lungs (positive control) for analysis of differential expression of MMP2 protein in CD-1 and C57Bl/6N mice (2). In another investigation, the authors employed Novus’s MMP2 antibody (NB200-193) for Zymography on T84 cells (treated in-vitro with IFN-gamma, IL1-beta or TNF-alpha), and on supernatants of ex vivo mouse colonic mucosa cultures derived from controls mice or animals with dextran sulfate sodium/DSS-induced colitis. Zymographic analysis revealed an increased MMP2 levels in IL1-beta treated T84 cells and in the colonic mucosal cultures derived from colitic mice (3). MMP2 antibody (clone 8B4) was employed for Immunohistochemistry of Whole-Mount (IHC-WhMt) on retinal pigment epithelium/RPE from rats that were exposed to laser photocoagulation for induction of focal RPE lesions. The MMP2 expression was found to be consistent with the process of extracellular degradation and tissue remodeling in and around the lesion areas (4). Scheede-Bergdahl’s team from University of Copenhagen used MMP2 antibody (clone 2C1; NB200-113) for WB assays on lysates from skeletal muscle of type 2 diabetes/T2DM subjects and demonstrated that exercise-induced stimulation of MMP2 is preserved in skeletal muscle of patients with T2DM. In a recent research publication from the journal Oncogene, Novus’ MMP-2 antibody [NB200-193] was used for IHC on Paraffin Sections of murine prostate tissues and with their findings, the authors established that the loss of ATF3 increases MMP-2 expression in prostate lesions from PTEN-knockout mice (6).

Compiled by: Subhash Gangar  

MMP2 Products from Novus Biologicals:


  1. Nelson et al. (2000). Matrix metalloproteinases: biologic activity and clinical implications. J Clin Oncol 18, 1135–1149
  2. Kendziorski JA, Belcher SM. Strain-specific induction of endometrial periglandular fibrosis in mice exposed during adulthood to the endocrine disrupting chemical bisphenol A. Reprod Toxicol. 2015 Dec;58:119-30.
  3. Kamekura R, Nava P, Feng M et al. Inflammation-induced desmoglein-2 ectodomain shedding compromises the mucosal barrier. Mol Biol Cell. 2015 Sep 15;26(18):3165-77
  4. von Leithner PL, Ciurtin C, Jeffery G. Microscopic mammalian retinal pigment epithelium lesions induce widespread 
    proliferation with  differences inmagnitude between center and periphery.
    Mol Vis. 2010 Mar 31;16:570-81.
  5. Scheede-Bergdahl C, Bergdahl A, Schjerling P et al. Exercise-induced regulation of matrix metalloproteinases in the skeletal muscle of subjects with type 2 diabetes. Diab Vasc Dis Res. 2014 Sep;11(5):324-34
  6. Wang Z, Xu D, Ding HF et al. Loss of ATF3 promotes Akt activation and prostate cancer development in a Pten knockout mouse model. Oncogene. 2015 Sep 17;34(38):4975-84


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