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Gene Review

MMP1  -  matrix metallopeptidase 1 (interstitial...

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Disease relevance of MMP1


High impact information on MMP1

  • This opposite regulation of 72-kDa collagenase type IV to that of MMP-1 seems to indicate that it has a specific role in remodeling the extracellular matrix during wound healing, fibrogenesis, and angiogenesis [3].
  • Results revealed that in fibrotic fibroblasts, the amount of MMP-1 mRNA was greatly reduced to undetectable levels whereas the amount of TIMP mRNA was increased fourfold compared to controls [3].
  • The matrix metalloproteinases (MMP-1 and MMP-8), fibronectin, OPN, TGF-beta1 proteins and the mRNAs for fibronectin, TGF-beta1, and OPN were significantly elevated in the infarct area as compared to the remote area and the non-infarcted hearts [4].
  • Cholesterol-rich diet augmented plasma lipid peroxidation (P<0.05), reduced the collagen content and increased vascular MMP-1 expression after injury (P<0.05) [1].
  • RNA was extracted from Day 15.75 pig embryos and uteri and reverse transcribed, and cDNA was amplified by polymerase chain reactions using primers specific for urokinase-type plasminogen activator (uPA), matrix metalloproteinases-2 and -9 (MMP-2 and -9), and tissue inhibitors of MMP-1, -2, and -3 (TIMP-1, -2, and -3) [5].

Biological context of MMP1

  • Four weeks later, after sacrifice, the vascular collagen content and MMP-1 protein expression, along with the plasma caseinolytic activity and lipid peroxidation, were measured [1].
  • Several leads were identified with IC50 values around 100 nM in a porcine TACE assay and selective over MMP-1, -2, -9, -13, and aggrecanase [6].

Other interactions of MMP1


Analytical, diagnostic and therapeutic context of MMP1

  • We have explored the effects of vitamins C and E on the collagen content and metalloproteinase-1 (MMP-1) expression after angioplasty in hypercholesterolemic pigs [1].


  1. Antioxidant vitamins increase the collagen content and reduce MMP-1 in a porcine model of atherosclerosis: implications for plaque stabilization. Orbe, J., Rodríguez, J.A., Arias, R., Belzunce, M., Nespereira, B., Pérez-Ilzarbe, M., Roncal, C., Páramo, J.A. Atherosclerosis (2003) [Pubmed]
  2. Selective matrix metalloproteinase inhibition with developing heart failure: effects on left ventricular function and structure. King, M.K., Coker, M.L., Goldberg, A., McElmurray, J.H., Gunasinghe, H.R., Mukherjee, R., Zile, M.R., O'Neill, T.P., Spinale, F.G. Circ. Res. (2003) [Pubmed]
  3. Expression of 72-kDa gelatinase (MMP-2), collagenase (MMP-1), and tissue metalloproteinase inhibitor (TIMP) in primary pig skin fibroblast cultures derived from radiation-induced skin fibrosis. Lafuma, C., El Nabout, R.A., Crechet, F., Hovnanian, A., Martin, M. J. Invest. Dermatol. (1994) [Pubmed]
  4. Increase of fibronectin and osteopontin in porcine hearts following ischemia and reperfusion. Kossmehl, P., Schönberger, J., Shakibaei, M., Faramarzi, S., Kurth, E., Habighorst, B., von Bauer, R., Wehland, M., Kreutz, R., Infanger, M., Schulze-Tanzil, G., Paul, M., Grimm, D. J. Mol. Med. (2005) [Pubmed]
  5. Expression of proteinases and proteinase inhibitors during embryo-uterine contact in the pig. Menino, A.R., Hogan, A., Schultz, G.A., Novak, S., Dixon, W., Foxcroft, G.H. Dev. Genet. (1997) [Pubmed]
  6. Non-hydroxamate 5-phenylpyrimidine-2,4,6-trione derivatives as selective inhibitors of tumor necrosis factor-alpha converting enzyme. Duan, J.J., Lu, Z., Wasserman, Z.R., Liu, R.Q., Covington, M.B., Decicco, C.P. Bioorg. Med. Chem. Lett. (2005) [Pubmed]
  7. Topical treatment with povidone iodine reduces nitrogen mustard-induced skin collagenolytic activity. Wormser, U., Brodsky, B., Reich, R. Arch. Toxicol. (2002) [Pubmed]
  8. Rapid communication: a BstXI polymorphism in the porcine matrix metalloproteinase 1 (MMP-1) gene locus. Jiang, Z.H., Rottmann, O.J., Pirchner, F. J. Anim. Sci. (1999) [Pubmed]
  9. ONO-4817, an orally active matrix metalloproteinase inhibitor, prevents lipopolysaccharide-induced proteoglycan release from the joint cartilage in guinea pigs. Yamada, A., Uegaki, A., Nakamura, T., Ogawa, K. Inflamm. Res. (2000) [Pubmed]
  10. Gene expression is altered in perfused arterial segments exposed to cyclic flexure ex vivo. Vorp, D.A., Peters, D.G., Webster, M.W. Annals of biomedical engineering. (1999) [Pubmed]
  11. Matrix remodeling expression in anulus cells subjected to increased compressive load. Wenger, K.H., Woods, J.A., Holecek, A., Eckstein, E.C., Robertson, J.T., Hasty, K.A. Spine. (2005) [Pubmed]
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