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MMP2  -  matrix metallopeptidase 2 (gelatinase A,...

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Disease relevance of MMP-2


High impact information on MMP-2

  • Cruciate ligament metabolism was determined by measuring the following markers of collagen turnover: matrix metalloproteinase 2 (MMP-2), tissue inhibitor of metalloproteinases 2, C-terminal type I procollagen propeptide (PICP), and the immature collagen-derived crosslink dihydroxylysinonorleucine (DHLNL) [6].
  • We observed elevated levels of pro and active MMP-2, PICP, and DHLNL in the cruciate ligaments of DH animals at most ages, compared with BS2 guinea pigs [6].
  • Smooth muscle cell outgrowth from the media was regulated by endogenous TIMPs, since TIMP inhibition (recombinant MMP-2 or neutralizing anti-TIMP antibodies) facilitated cell outgrowth (P<0.001) [7].
  • These observations were paralleled by the predominant expression of TIMP-1 and -2 in the media (14-fold and 37-fold higher than in adventitia, respectively, P<0.001), whereas higher gelatinolytic activities (MMP-2 and -9) were released from adventitial explants [7].
  • MMP-2 activity peaks at day seven in the adventitia and days 19 to 26 in the intima [3].

Chemical compound and disease context of MMP-2

  • We developed a chronic porcine model of septic shock and ARDS and hypothesized that blocking the proteases neutrophil elastase (NE) and matrix metalloproteinases (MMP-2 and MMP-9) with the modified tetracycline, COL-3, would significantly improve morbidity in this model [8].

Biological context of MMP-2

  • Studies were conducted to define the signal transduction pathway responsible for the increases in MMP-2 and -14 that occur in response to mechanical stretching of TM cells [9].
  • Translational initiation involving eIF-4E and its inhibitory binding protein 4E-BP1 appear to be involved in both the MMP-2 and -14 increases with stretching and are normally regulated by mTOR [9].
  • Increased platelet aggregation and activity of MMP-2 would alter platelet-platelet and platelet-vessel wall interactions, contributing to an exaggerated response to injury with loss of ovarian hormones [10].
  • Pretreatment of the GP-TSMC with the bradykinin B2 receptor (BKB2-R) antagonist Hpp-HOE-140 (Hpp-D-Arg0-Hyp3-Thi5-D-Tic7-Oic8-BK; 10(-8)-10(-4) M) significantly inhibited the BK-stimulated upregulation of MMP-2 in GP-TSMC in a concentration-related manner [11].
  • Only at luteolysis (day 17), Ca++/Mg++-dependent endonuclease and MMP-2 spontaneous activity increased significantly [12].

Anatomical context of MMP-2

  • These results provide the first evidence for the involvement of BK in the release of MMP-2 from airway smooth muscle cells through activation of the BKB2-R [11].
  • Likewise, inhibitor activity against MMP-2 in the uterine cervix was enhanced in response to relaxin (P < 0.05) [13].
  • 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 [14].
  • Specific localization of MMP-2 and -9 transcripts above background was not observed by in situ hybridization in either embryos or uterus [15].
  • RESULTS: Pressure distention irreversibly overstretched the porcine jugular vein and increased MMP-2 and MMP-9 proteolytic activity by 40% and 77%, respectively [16].

Associations of MMP-2 with chemical compounds


Other interactions of MMP-2

  • Wortmannin blocked the MMP-2 but not the MMP-14 increase [9].
  • Molecular analysis using reverse transcription-polymerase chain reaction, Western immunoblotting, gelatin zymography, and reverse zymography were performed to study the expression and activation of MMP-2 and MMP-9, and tissue inhibitors of MMP (TIMP)-1 and TIMP-2 [16].
  • Inhibitor activity in uterine tissue extracts and uterine flushes from relaxin-treated animals was greater than that in controls; however, this activity was restricted to inhibition of MMP-2 [13].
  • After 1 month, the specimens were rapidly thawed (37 degrees C) and processed for biomechanical, ultrastructural, morphological and immunohistochemical (MMP-1, MMP-2, MMP-3 and MMP-9) analysis [17].
  • The matrix metalloproteinase-9 (MMP-9) activity increased by 30, 46, 12 and 23% after 3, 24, 48 and 72 h of HN2 exposure, respectively, whereas the MMP-2 was elevated by 8, 65, 8 and 30%, respectively [18].

Analytical, diagnostic and therapeutic context of MMP-2

  • METHODS: Porcine TM cells were subjected to mechanical stretching, and changes in MMP-2 and -14 levels were determined by gelatin zymography and Western immunoblot analysis [9].
  • The furin inhibitor decanoyl-Arg-Val-Lys-Arg-chloromethylketone did not prevent MMP-2 activation after balloon angioplasty [1].
  • METHODS: In a porcine model of isolated-reperfused lung, we studied the alveolar-capillary permeability and the zymographic expression of MMP-9 and MMP-2 in the bronchoalveolar lavage fluid of lungs submitted ex vivo to ischemia in three preservation solutions [modified Euro-Collins (EC), low-potassium-dextran, modified-blood] [19].
  • BACKGROUND: We hypothesized the source of early proliferating cells contributing to venous stenosis formation in a porcine hemodialysis grafts is the adventitia and media, and migration of these cells is greatest within the first two weeks following graft placement, resulting in increased matrix metalloproteinase-2 (MMP-2) activity [3].
  • MMP-2 mRNA expression was evaluated by quantitative real-time PCR [20].


  1. Activation of MMP-2 in response to vascular injury is mediated by phosphatidylinositol 3-kinase-dependent expression of MT1-MMP. Zahradka, P., Harding, G., Litchie, B., Thomas, S., Werner, J.P., Wilson, D.P., Yurkova, N. Am. J. Physiol. Heart Circ. Physiol. (2004) [Pubmed]
  2. Acetaminophen attenuates peroxynitrite-activated matrix metalloproteinase-2-mediated troponin I cleavage in the isolated guinea pig myocardium. Rork, T.H., Hadzimichalis, N.M., Kappil, M.A., Merrill, G.F. J. Mol. Cell. Cardiol. (2006) [Pubmed]
  3. Adventitial remodeling with increased matrix metalloproteinase-2 activity in a porcine arteriovenous polytetrafluoroethylene grafts. Misra, S., Doherty, M.G., Woodrum, D., Homburger, J., Mandrekar, J.N., Elkouri, S., Sabater, E.A., Bjarnason, H., Fu, A.A., Glockner, J.F., Greene, E.L., Mukhopadhyay, D. Kidney Int. (2005) [Pubmed]
  4. Regulation of matrix metalloproteinase expression in endothelial cells by heat-inactivated Streptococcus pneumoniae. Michel, U., Zobotke, R., Mäder, M., Nau, R. Infect. Immun. (2001) [Pubmed]
  5. Selective inhibition of matrix metalloproteinase isozymes and in vivo protection against emphysema by substituted gamma-keto carboxylic acids. Ma, D., Jiang, Y., Chen, F., Gong, L.K., Ding, K., Xu, Y., Wang, R., Ge, A., Ren, J., Li, J., Li, J., Ye, Q. J. Med. Chem. (2006) [Pubmed]
  6. Cruciate ligament laxity and femoral intercondylar notch narrowing in early-stage knee osteoarthritis. Quasnichka, H.L., Anderson-MacKenzie, J.M., Tarlton, J.F., Sims, T.J., Billingham, M.E., Bailey, A.J. Arthritis Rheum. (2005) [Pubmed]
  7. Role of matrix metalloproteinases and their tissue inhibitors in the regulation of coronary cell migration. Shi, Y., Patel, S., Niculescu, R., Chung, W., Desrochers, P., Zalewski, A. Arterioscler. Thromb. Vasc. Biol. (1999) [Pubmed]
  8. Chemically modified tetracycline prevents the development of septic shock and acute respiratory distress syndrome in a clinically applicable porcine model. Steinberg, J., Halter, J., Schiller, H., Gatto, L., Carney, D., Lee, H.M., Golub, L., Nieman, G. Shock (2005) [Pubmed]
  9. Signaling pathways used in trabecular matrix metalloproteinase response to mechanical stretch. Bradley, J.M., Kelley, M.J., Rose, A., Acott, T.S. Invest. Ophthalmol. Vis. Sci. (2003) [Pubmed]
  10. Effects of ovariectomy on aggregation, secretion, and metalloproteinases in porcine platelets. Jayachandran, M., Owen, W.G., Miller, V.M. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  11. Bradykinin stimulates MMP-2 production in guinea pig tracheal smooth muscle cells. Zaczynska, E., Gabra, B.H., Sirois, P. Inflammation (2003) [Pubmed]
  12. Gelatinases, endonuclease and Vascular Endothelial Growth Factor during development and regression of swine luteal tissue. Ribeiro, L.A., Turba, M.E., Zannoni, A., Bacci, M.L., Forni, M. BMC Dev. Biol. (2006) [Pubmed]
  13. Relaxin increases secretion of tissue inhibitor of matrix metalloproteinase-1 and -2 during uterine and cervical growth and remodeling in the pig. Lenhart, J.A., Ryan, P.L., Ohleth, K.M., Palmer, S.S., Bagnell, C.A. Endocrinology (2002) [Pubmed]
  14. 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]
  15. 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]
  16. Pressure distention compared with pharmacologic relaxation in vein grafting upregulates matrix metalloproteinase-2 and -9. Chung, A.W., Rauniyar, P., Luo, H., Hsiang, Y.N., van Breemen, C., Okon, E.B. J. Vasc. Surg. (2005) [Pubmed]
  17. Rapid thawing increases the fragility of the cryopreserved arterial wall. Buján, J., Pascual, G., García-Honduvilla, N., Gimeno, M.J., Jurado, F., Carrera-San Martín, A., Bellón, J.M. European journal of vascular and endovascular surgery : the official journal of the European Society for Vascular Surgery. (2000) [Pubmed]
  18. Topical treatment with povidone iodine reduces nitrogen mustard-induced skin collagenolytic activity. Wormser, U., Brodsky, B., Reich, R. Arch. Toxicol. (2002) [Pubmed]
  19. Matrix metalloproteinases correlate with alveolar-capillary permeability alteration in lung ischemia-reperfusion injury. Soccal, P.M., Gasche, Y., Pache, J.C., Schneuwly, O., Slosman, D.O., Morel, D.R., Spiliopoulos, A., Suter, P.M., Nicod, L.P. Transplantation (2000) [Pubmed]
  20. Resuscitation of hypoxic piglets with 100% O2 increases pulmonary metalloproteinases and IL-8. Munkeby, B.H., Børke, W.B., Bjørnland, K., Sikkeland, L.I., Borge, G.I., Lømo, J., Rivera, S., Khrestchatisky, M., Halvorsen, B., Saugstad, O.D. Pediatr. Res. (2005) [Pubmed]
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