◀ Back to MMP7

MMP7 — TIMP2

Text-mined interactions from Literome

Jo et al., Biochem J 2000 : In contrast, activation of pro-MMP-2 by sMT1-MMP was dose-dependently inhibited by TIMP-2
Miyamori et al., J Biol Chem 2001 : In contrast to the stimulatory effect of TIMP-2 on pro-MMP-2 activation by MT1-MMP, activation of pro-MMP-2 by DeltaMT1-MMP in the presence of claudin-5 and proDeltaMMP-2 processing by MT1-MMP were both inversely repressed by expression of exogenous TIMP-2
Munshi et al., J Biol Chem 2002 (Carcinoma, Squamous Cell...) : The decrease in TIMP-2 levels in the conditioned media was prevented by a broad spectrum MMP inhibitor, suggesting that calcium promotes recruitment of TIMP-2 to MT1-MMP on the cell surface
Bernardo et al., Biochem J 2003 : TIMP-2 ( tissue inhibitor of metalloproteinase-2 ) regulates MMP-2 ( matrix metalloproteinase-2 ) activity in the extracellular environment after pro-MMP-2 activation by MT1 ( membrane type 1 ) -MMP
Fernández et al., J Biol Chem 2003 : To address these differences, a series of structure-function studies were conducted to identify and to characterize the anti-angiogenic domains of TIMP-2 , the endogenous MMP inhibitor that uniquely inhibits capillary endothelial cell ( EC ) proliferation as well as angiogenesis in vivo
Karagiannis et al., J Biol Chem 2004 : A theoretical model of type I collagen proteolysis by matrix metalloproteinase (MMP) 2 and membrane type 1 MMP in the presence of tissue inhibitor of metalloproteinase 2
Cantemir et al., Dev Dyn 2004 : Because TIMP-2 is required for activation of proMMP-2 by MT1-MMP , this finding suggests TIMP-2 expression by cardiac NC cells initiates proMMP-2 activation important for their migration
Lee et al., J Gene Med 2005 (Breast Neoplasms...) : As expected, overexpression of TIMP-2 inhibited matrix metalloprotenase ( MMP ) activity and invasion of the tumor cells
Orlandi et al., Am J Pathol 2005 (Heart Neoplasms...) : Reverse transcriptase-polymerase chain reaction demonstrated that increased MMP activity was due, at least in part, to increased transcription and that TIMP-2 transcripts increased in embolic myxomas
Zhu et al., Zhonghua Gan Zang Bing Za Zhi 2005 (Liver Cirrhosis, Experimental) : In liver fibrosis, MMP-2 expression increases , while TIMP-2 expression relatively decreases
Moche et al., Pneumologie 2005 (Lung Neoplasms...) : MMP and TIMP plasma concentrations were not different in CA vs. CHF, but MMP-9, TIMP-1, and TIMP-2 were increased vs. CON ( p < 0.005, each )
Jiang et al., J Zhejiang Univ Sci B 2005 : Reverse zymography confirmed the bioactivity of MMP ( matrix metalloproteinase ) inhibition of TIMP-2
Zhang et al., Zhonghua Kou Qiang Yi Xue Za Zhi 2006 (Carcinoma, Squamous Cell...) : Furthermore, the expression of TIMP-2 consequently increased with the increasing of the MMP , but the increase of TIMP-2 was less than that of MMP
Sanka et al., Invest Ophthalmol Vis Sci 2007 : Primary human TM ( HTM ) cells treated with different actin cytoskeleton interfering agents, including cytochalasin D, latrunculin A, ethacrynic acid ( ECA ), a Rho kinase inhibitor ( Y-27632 ), and H-7 ( serine/threonine kinase inhibitor ), were examined for changes in actin cytoskeletal organization by phalloidin staining, MMP-2 activation by gelatin zymography, expression of MT1-MMP by quantitative real-time PCR analysis, levels of tissue inhibitor of metalloproteinases ( TIMP-1 and TIMP-2 ), and activation of p38 mitogen activated protein kinase ( p38 MAPK ) and extracellular signal regulated protein kinase ( ERK ) by immunoblotting
Hubbard et al., J Nutr 2007 (Mammary Neoplasms, Animal...) : The steady-state mRNA and protein levels of tissue inhibitors of metalloproteinase-1 ( TIMP-1 ) and TIMP-2 , natural inhibitors of MMP , were increased at higher dietary CLA levels relative to low or no CLA
Rogliani et al., Respir Med 2008 (Pulmonary Emphysema...) : In contrast, fibroblasts in areas of parenchymal destruction of emphysema/UIP expressed MMP-2, MMP-9 , MMP-7 and MT1-MMP at variable but significantly higher levels when compared to emphysema subjects, in the presence of similar levels of TIMP-1, TIMP-2 and TNF-alpha ... In contrast, fibroblasts in areas of parenchymal destruction of emphysema/UIP expressed MMP-2, MMP-9, MMP-7 and MT1-MMP at variable but significantly higher levels when compared to emphysema subjects, in the presence of similar levels of TIMP-1, TIMP-2 and TNF-alpha
Visser et al., Equine Vet J 2012 (Foot Diseases...) : Gene expression of TIMP-2 , a MMP regulator , decreases during laminitis development
Walsh et al., Journal of cell communication and signaling 2012 : TIMP-2 , the most studied member of the family, can both inhibit and activate MMPs directly, as well as inhibit MMP activity indirectly by upregulating expression of RECK, a membrane anchored MMP regulator ... Using an ALA + TIMP-2 mutant which is devoid of MMP inhibition, but still capable of initiating specific cell signaling cascades, we show that TIMP-2 can differentially affect MMP activity and cellular invasiveness in both an MMP dependent and independent manner
Furmanova-Hollenstein et al., Radiation oncology (London, England) 2013 : Furthermore, siRNA depletion of TIMP-1 or TIMP-2 prevented IR-mediated induction of MMP activity and cell invasion
Kolkenbrock et al., Biol Chem 1997 : the activation of the progelatinase A/TIMP-2 complex proceeds in two steps : At first MT2-MMP is inhibited by the progelatinase A/TIMP-2/MT2-MMP , complex, whereby a ternary complex, progelatinase A/TIMP-2/ MT-2MMP is generated
Wada et al., Gene 1998 : Enzyme activity of MMP-C31 and -H19 was inhibited by human tissue inhibitor of MMPs (TIMP)-1, TIMP-2 and synthetic MMP inhibitors, BB94 and CT543, indicating that the catalytic sites of these C. elegans MMPs are structurally closely related with those of mammalian MMPs