ライフサイエンスコーパス: TIMP-2

1 hibitor of metalloproteinases 1 [TIMP-1] and TIMP-2).

2 r, tissue inhibitor of metalloproteinases-2 (TIMP-2).

3 0.08 for untreated cells; 0.71 +/- 0.09 with TIMP-2).

4 nd tissue inhibitor of metalloproteinases-2 (TIMP-2).

5 nd tissue inhibitor of metalloproteinases-2 (TIMP-2).

6 nd tissue inhibitor of metalloproteinases-2 (TIMP-2).

7 s regulated by their physiological inhibitor TIMP-2.

8 ecrease in the levels of secreted TIMP-1 and TIMP-2.

9 P-2 (2-fold), while not affecting TIMP-1 and TIMP-2.

10 xpressed higher levels of MMP-2, TIMP-1, and TIMP-2.

11 nverting enzyme (TACE), but not by TIMP-1 or TIMP-2.

12 nd -2 and MMP1, -2, -9, and -10 and inducing TIMP-2.

13 s caused by the downregulation of MMP-14 and TIMP-2.

14 reduced neurite length, which is rescued by TIMP-2.

15 n effector of the antiangiogenic function of TIMP-2.

16 IMP-3, but was insensitive to treatment with TIMP-2.

17 nhibitor of metalloproteinase-1 (TIMP-1) and TIMP-2.

18 ype 1-matrix metalloproteinase (MT1-MMP) and TIMP-2.

19 ientation of crystalline MT1-MMP(DeltaC) and TIMP-2.

20 t had no catalytic activity and did not bind TIMP-2.

21 formation of the complex of active MMP-2 and TIMP-2.

22 more acidic conditions than either TIMP-1 or TIMP-2.

23 le active MT1-MMP species capable of binding TIMP-2.

24 nhibitors of metalloproteinase (TIMP) -1 and TIMP-2.

25 ough paracrine mechanisms involving bFGF and TIMP-2.

26 meras were then inhibited by both TIMP-1 and TIMP-2.

27 these mechanisms to the antitumor effects of TIMP-2.

28 generated containing 2 x 10(10) variants of TIMP-2.

29 rotein and mRNA levels of MMP-2, MMP-14, and TIMP-2.

30 MT6-MMP partially exists in its complex with TIMP-2.

31 TIMP-2, -3, and -4 are also upregulated.

32 ve cultures), MMP-24 (in all five cultures), TIMP-2, -3, and -4 expression (in three of five cultures

33 In A549 cells expressing increased levels of TIMP-2, a significant decrease in SP was observed, and t

34 In vivo, both TIMP-2 and Ala+TIMP-2 A549 xenografts exhibited reduced growth rate, CD

35 We demonstrate here that TIMP-2 abrogates angiogenic factor-induced endothelial c

36 ds tissue inhibitor of metalloproteinases-2 (TIMP-2), activates matrix metalloproteinase-2 (MMP-2), a

37 ry resulted in a decrease of both MMP-14 and TIMP-2 activity and protein.

38 mogenates were collected to assess MMP-2 and TIMP-2 activity by zymography and reverse zymography, pr

39 collected for analysis of MMP-2, MMP-14, and TIMP-2 activity, mRNA and protein expression.

40 Neither TIMP-1 or TIMP-2 affected the onset of rejection pathology.

41 invasion assays showed that re-expression of TIMP-2 after a combined treatment with 5-aza and trichos

42 Overexpression of either MMP-14 or TIMP-2 alone before oxidant injury is not enough to prev

43 d identical behavior to those overexpressing TIMP-2 alone.

44 anifested by the selective downregulation of TIMP-2 along with upregulation of MMP-2 and CVF-I in the

45 TIMP-2 and Ala+TIMP-2 also suppress basal hMVEC migration via a time-de

46 G, EGFL6, EGFR, angiopn-1, angiopn-2, ICAM2, TIMP-2, among others.

47 ative expressions of TIMP mRNA were TIMP-1 > TIMP-2 and -3 > TIMP-4.

48 all, these data reveal a novel role for both TIMP-2 and -3 in the pericyte-induced stabilization of n

49 and invasion) is primarily controlled by the TIMP-2 and -3 target membrane type (MT) 1 MMP.

50 reased MMPs-2, -3 & -9, ADAMTS-4 and -5, and TIMP-2 and -3 transcript levels but inhibited type I col

51 omain cleavage of ICAM-1 that was blocked by TIMP-2 and -3.

52 In vivo, both TIMP-2 and Ala+TIMP-2 A549 xenografts exhibited reduced

53 TIMP-2 and Ala+TIMP-2 also suppress basal hMVEC migratio

54 In vitro, growth assays suggested that TIMP-2 and Ala+TIMP-2 did not alter basal cell prolifera

55 (Ser473) showed decreased activation in both TIMP-2 and Ala+TIMP-2 tumor cells.

56 ibitor of matrix metalloproteinase (TIMP)-1, TIMP-2 and C-terminal propeptide of collagen type-I with

57 or-1 receptor as a binding partner of Loop 6/TIMP-2 and characterize this interaction on the endothel

58 Invasion was blocked by TIMP-2 and GM6001 but not by TIMP-1.

59 Urinary TIMP-2 and IGFBP7 were measured using a clinical immunoa

60 However, the association of urinary TIMP-2 and IGFBP7 with long-term outcomes is unknown.

61 ral delivery system, we stably overexpressed TIMP-2 and its mutant Ala+TIMP-2 (devoid of MMP inhibito

62 In contrast, TIMP-2 and mutant Ala+TIMP-2, which is devoid of MMP inh

63 plasmin activity and decreased expression of TIMP-2 and PAI-1 in tubular cells, and upregulation of r

64 eolytic activity, and elevated expression of TIMP-2 and PAI-1 in tubular cells.

65 fering RNA technology, the suppression of EC TIMP-2 and pericyte TIMP-3 expression leads to capillary

66 l system appears to occur through EC-derived TIMP-2 and pericyte-derived TIMP-3 to block both the cap

67 deoxycytidine and trichostatin A reactivated TIMP-2 and restored its expression in TIMP-2-silenced me

68 mino acid peptide corresponding to Loop 6 of TIMP-2 and show that Loop 6 is a potent inhibitor of bot

69 TIMP-2 and TIMP-4 also inhibited the activation of pro-M

70 eviously shown that the C-terminal domain of TIMP-2 and, in particular, Loop 6 inhibit capillary endo

71 Tissue inhibitor metalloproteinase-2 (TIMP-2) and IGF-binding protein-7 (IGFBP7) have been val

72 the PEX of MMP-2 (that forms a complex with TIMP-2) and of MMP-9 (that forms a complex with TIMP-1)

73 ved tissue inhibitor of metalloproteinase-2 (TIMP-2) and pericyte-derived TIMP-3 are shown to coregul

74 tic tissue inhibitor of metalloproteinase-2 (TIMP-2) and plasminogen activator inhibitor-1 (PAI-1).

75 inhibitor of metalloproteinases (TIMP-1 and TIMP-2), and activation of p38 mitogen-activated protein

76 itor of matrix metalloproteinase 1 (TIMP-1), TIMP-2, and hypoxanthine phosphoribosyl transferase-1 (H

77 nhibitor of metalloproteinase (TIMP) -1, and TIMP-2, and IL-13 level increased markedly in both CD73K

78 s of mRNA for MT1-MMP, MMP-2, MMP-3, TIMP-1, TIMP-2, and TIMP-3 in the scleras of tree shrews that ha

79 inhibitor of metalloproteinases 1 (TIMP-1), TIMP-2, and TIMP-3 messenger RNA (mRNA) expression in ar

80 The observed changes in MT1-MMP, MMP-2, TIMP-2, and TIMP-3 mRNA are consistent with visually mod

81 aled that MMP-26 was colocalized with MMP-9, TIMP-2, and TIMP-4 in DCIS cells.

82 The expression levels of MMP-26, MMP-9, TIMP-2, and TIMP-4 proteins in DCIS were significantly h

83 issue inhibitor of matrix metalloproteinase [TIMP-2] and epidermal growth factor [EGF]) and/or bacter

84 Here, we examine the hypothesis that the TIMP-2 antitumor activity may involve regulation of the

85 However, the mechanisms underlying TIMP-2 antitumor effects are not fully characterized.

86 Both TIMP-1 and TIMP-2 are capable of inhibiting the proteolytic activit

87 recently reported that forced expression of TIMP-2, as well as the modified form Ala+TIMP-2 (that la

88 the balanced regulation of the MT1-MMP/MMP-2/TIMP-2 axis and the invasive behavior in cancer cells.

89 An MT1-MMP/MMP-2/TIMP-2 axis plays a key role in the invasive behavior of

90 dependently of plasminogen, the gelatinase A/TIMP-2 axis, gelatinase B, collagenase-3, collagenase-2,

91 -9, MMP-2, tissue inhibitor of MMP (TIMP)-1, TIMP-2, Bax, and BCl-2 proteins in retinal extracts were

92 sue inhibitor of matrix metalloproteinase-2 (TIMP-2) belongs to a small family of endogenous proteins

93 s of total protein, MMP-2, MMP-3, TIMP-1 and TIMP-2 between patients on prostaglandin analogues and t

94 TIMP-2 binding to MT1-MMP induces activation of ERK1/2 b

95 by TIMP-3 and TIMP-4 and weakly inhibited by TIMP-2 but not by TIMP-1, a profile distinct from other

96 Overexpression of TIMP-2 but not TIMP-1 inhibits atherosclerotic plaque de

97 ed a similar affinity for MMP-1 as wild-type TIMP-2 but reduced affinity for MMP-3.

98 d only after co-overexpression of MMP-14 and TIMP-2, but activity further decreased after HQ for 18 h

99 In addition, up-regulation of TIMP-2 by alpha1(IV)NC1 led to saturation of MT1-MMP bin

100 Secondly, TIMP-2 can disrupt VEGF signaling required for initiatio

101 Third, TIMP-2 can enhance expression of RECK via Rap1 signaling

102 First, TIMP-2 can inhibit cell migration after VEGF stimulation

103 These results suggest that TIMP-2 can inhibit cell migration via several distinct m

104 inhibitor of metalloproteinases 1 (TIMP-1), TIMP-2, CD68, and caspase 3.

105 sue inhibitor of matrix metalloproteinase-2 (TIMP-2), characterized for its ability to inhibit matrix

106 entrations of IL-1beta, TNF-alpha, and MMP-2/TIMP-2 complex were assessed using enzyme-linked immunos

107 nt association among the production of MMP-2/TIMP-2 complex with the presence of CP (P = 0.008) and p

108 l artery and higher salivary levels of MMP-2/TIMP-2 complex.

109 Transfection with MMP-14 and/or TIMP-2 contributed to the return of type IV collagen lev

110 on to extracellular proteolysis, MT1-MMP and TIMP-2 control cell proliferation and migration through

111 TIMP-2 decreases cyclins B and D expression and increase

112 Blocking TIMP-2 degradation with bafilomycin A1 significantly inc

113 TIMP-2 deletion causes a delay in neuronal differentiati

114 ably overexpressed TIMP-2 and its mutant Ala+TIMP-2 (devoid of MMP inhibitory activity) in human aden

115 growth assays suggested that TIMP-2 and Ala+TIMP-2 did not alter basal cell proliferation rates, how

116 ely inhibits KL cleavage, whereas Timp-1 and Timp-2 do not, a profile that indicates the involvement

117 inhibition, as A549 cells overexpressing Ala+TIMP-2 exhibited identical behavior to those overexpress

118 sorbent assay (ELISA), we confirmed enhanced TIMP-2 expression and its MMP inhibitory activity by rev

119 involved concurrent reciprocal modulation of TIMP-2 expression by ERK1/2 and p38 MAPKs, such that inh

120 nduces a specific pattern of furin, MMP, and TIMP-2 expression in corneal myofibroblasts.

121 ted by peroxynitrite, as the latter reversed TIMP-2 expression in iNOS(-/-) lung smooth muscle cells

122 re, we investigated the mechanism underlying TIMP-2 expression in prostate cancer cell lines and prim

123 putative physiological inhibitors TIMP-1 and TIMP-2 for the active catalytic domain of human MMP-10 (

124 ed amounts of IL-8, hBD-1, VEGF, TIMP-1, and TIMP-2 from corresponding EVPOMEs.

125 our data provide strong evidence that these TIMP-2 functions occur independent of MMP inhibition, as

126 sults suggest that the downregulation of the TIMP-2 gene is associated with promoter methylation and

127 igenetic analysis of the MT1-MMP, MMP-2, and TIMP-2 gene promoters in highly migratory glioblastoma c

128 oter hypermethylation and lost expression of TIMP-2 gene, which was supported by other results demons

129 n (ANT), PDGF-BB, VEGF, FGF-2, IL-8, TIMP-1, TIMP-2, GM-CSF, and IP-10.

130 The relative expression of TIMP mRNA was TIMP-2 > TIMP-1 > TIMP-3 > TIMP-4.

131 pable of activating pro-MMP-2, and exogenous TIMP-2 had a biphasic effect on this membrane-mediated M

132 TIMP-1 and TIMP-2 had differential effects on delayed type hypersen

133 MP-1 and TIMP-2 (N-TIMPs) and MMP-3cd with N-TIMP-2 have been characterized by isothermal titration c

134 ed for the protein detection of EGF, TIMP-1, TIMP-2, HGF, angiopn-1, angiopn-2, VEGF-A, IP-10, PDGF,

135 en HCV cirrhosis and HCV-HCC groups (TIMP-1, TIMP-2, HGF, angiopn-1, angiopn-2, VEGF-A, IP-10, PDGF,

136 to tissue inhibitor of metalloproteinase-2 (TIMP-2), ie, CNHRYMQMC, CNQRHQMSC, and CNNRSDGMC.

137 We now validate a clinical test for urinary [TIMP-2].[IGFBP7] at a high-sensitivity cutoff greater th

138 Urinary [TIMP-2].[IGFBP7] greater than 0.3 (ng/ml)(2)/1,000 ident

139 Critically ill patients with urinary [TIMP-2].[IGFBP7] greater than 0.3 had seven times the ri

140 del including clinical information, urinary [TIMP-2].[IGFBP7] remained statistically significant and

141 For a single urinary [TIMP-2].[IGFBP7] test, sensitivity at the prespecified h

142 primary analysis was the ability of urinary [TIMP-2].[IGFBP7] to predict moderate to severe AKI withi

143 % CI, 0.80-0.90 for clinical variables plus [TIMP-2].[IGFBP7]).

144 Two predefined [TIMP-2][IGFBP7] cutoffs (0.3 for high sensitivity and 2.

145 e analysis adjusted for the clinical model, [TIMP-2][IGFBP7] levels>0.3 were associated with death or

146 In conclusion, [TIMP-2][IGFBP7] measured early in the setting of critica

147 Baseline [TIMP-2][IGFBP7] values were available for 692 subjects,

148 Univariate analysis showed that [TIMP-2][IGFBP7]>2.0 was associated with increased risk o

149 ent samples revealed aberrant methylation of TIMP-2 in 33/90 (36.7%) cases of non-Hodgkin's lymphoma

150 expression by pericytes, whereas ECs produce TIMP-2 in EC-pericyte cocultures.

151 est expression in the epithelial tissues and TIMP-2 in the fibers.

152 tic MMP inhibitors work synergistically with TIMP-2 in the promotion of pro-MMP-2 activation by MT1-M

153 macrophage-derived foam cells with exogenous TIMP-2 in vitro.

154 rge tissue inhibitor of metalloproteinase-2 (TIMP-2) increase detected in wild-type mice was absent i

155 nhibitor of metalloproteinase 1 (TIMP-1) and TIMP-2 increased after CCl(4) only in the gp91(phox(-/-)

156 ng RNA-mediated down-regulation of MMP-2 and TIMP-2 increased intravasation of HT-lo/diss cells.

157 ontrol at day 1 after MI (P < 0.05), whereas TIMP-2 increased only at later time points.

158 TIMP-2 induced collagen contraction, but the effect was

159 TIMP-2-induced RECK decreases cell-associated MMP activi

160 Further, TIMP-2 induces a decrease in total protein tyrosine phos

161 Here, we report that TIMP-2 induces pheochromocytoma PC12 cell-cycle arrest v

162 of a dominant negative Shp-1 mutant ablates TIMP-2 induction of p27Kip1.

163 embrane interactions beside the active site, TIMP-2-inhibited MMP-12 binds vesicles and cells, sugges

164 an unexpected, MMP-independent mechanism for TIMP-2 inhibition of endothelial cell proliferation in v

165 iable" Shp-1-deficient mice are resistant to TIMP-2 inhibition, demonstrating that Shp-1 is an import

166 TIMP-2 inhibits endothelial cell proliferation and migra

167 TIMP-2 inhibits the MMP-10cd with a K(i) of 5.8 x 10(-9)

168 ors of metalloproteinase 1 and 2 (TIMP-1 and TIMP-2), insulinlike growth factor-binding protein 2 (IG

169 findings illustrate a novel role for MT1-MMP-TIMP-2 interaction, which controls cell functions by a m

170 In contrast, TIMP-2 is a better inhibitor of MT1-MMP.

171 e conclude that promoter hypermethylation of TIMP-2 is a novel epigenetic event in the pathogenesis o

172 Tissue inhibitor of metalloproteinases-2 (TIMP-2) is a broad spectrum inhibitor of the matrix meta

173 Tissue inhibitor of metalloproteinase 2 (TIMP-2) is an angiogenesis inhibitor initially character

174 he tissue inhibitor of metalloproteinases-2 (TIMP-2) is known to antagonize matrix metalloproteinase

175 rresponding in vivo differences in levels of TIMP-2, JAM-C, and TF were demonstrated in primary tumor

176 referentially by TIMP-1 (K(i) = 0.2 nm) over TIMP-2 (K(i) = 2.0 nm), because of a slower association

177 with the PC12 cell data, primary cultures of TIMP-2 knock-out cerebral cortical neurons exhibit signi

178 mice and mice expressing a mutant truncated TIMP-2 (knock-down) show deficits in fear-potentiated st

179 at neither male nor female mice deficient in TIMP-2 (knockout) exhibit prepulse inhibition of the sta

180 inase phosphatase 1 in tumors overexpressing TIMP-2 leads to dephosphorylation of p38 mitogen-activat

181 MT1-MMP autolysis product and decline in the TIMP-2 levels in conditioned media were observed.

182 The decrease in TIMP-2 levels in the conditioned media was prevented by

183 n A1 significantly increased cell-associated TIMP-2 levels in the presence of high calcium.

184 inhibitor of metalloproteinase (TIMP)-1, and TIMP-2 levels increased across all participant groups.

185 ls and fibroblasts, suggesting that the iNOS-TIMP-2 link may explain the protective effect of iNOS-kn

186 SP phenotype and function, and suggests that TIMP-2 may act as an endogenous suppressor of the SP in

187 The regulatory effect of iNOS on TIMP-2 may be mediated by peroxynitrite, as the latter r

188 e for the TIMP-2(-/-) mice and suggests that TIMP-2 may play a role in the synaptic plasticity underl

189 ta suggest that the antiangiogenic action of TIMP-2 may rely on matrix metalloproteinase-independent

190 urine embryo fibroblasts fail to demonstrate TIMP-2-mediated decrease in cell migration despite activ

191 TIMP-2-mediated inhibition of Cdk4 and Cdk2 activity is

192 We conclude that TIMP-2-mediated inhibition of tumor growth occurs, at le

193 Expression of dominant-negative Rap1 blocks TIMP-2-mediated neurite outgrowth.

194 body increases MMP activity and reverses the TIMP-2-mediated reduction in cell migration.

195 Here, we show that TIMP-2 mediates G1 growth arrest in human endothelial ce

196 The frequency of TIMP-2 methylation was slightly higher in aggressive NHL

197 s is the first report of a phenotype for the TIMP-2(-/-) mice and suggests that TIMP-2 may play a rol

198 gen degradation, and increased the levels of TIMP-2, MMP-14, and the active MMP-2 in the membrane ext

199 r findings provide the first indication that TIMP-2 modulates SP phenotype and function, and suggests

200 rs of exposure to LA increased expression of TIMP-2 mRNA by up to 11.3% +/- 0.2% (n = 3).

201 icantly increased MT1-MMP, MMP-2, MMP-9, and TIMP-2 mRNA expression, followed by increased active MT1

202 ptase-PCR analysis, we found that endogenous TIMP-2 mRNA levels showed a significant inverse correlat

203 However, no significant induction of TIMP-2 mRNA was observed at either 18 or 24 hours (n = 3

204 However, no significant induction of TIMP-2 mRNA was observed.

205 Variants of the N-terminal domain of TIMP-2 (N-TIMP-2) with the sequences of the most selecti

206 -1 with the inhibitory domains of TIMP-1 and TIMP-2 (N-TIMPs) and MMP-3cd with N-TIMP-2 have been cha

207 From these candidates, four targets (i.e. TIMP-2, NCAM-1, JAM-C, and tissue factor (TF)) were sele

208 Neither TIMP-2 nor a synthetic MMP inhibitor protects breast epi

209 olecular pathways involved in the effects of TIMP-2 on processes dependent on tumor-host interactions

210 The effects of TIMP-2 on RECK expression and cell migration were confir

211 d is a consequence of both direct effects of TIMP-2 on tumor cells and modulation of the tumor microe

212 pro-MMP-9) even in the presence of exogenous TIMP-2 or TIMP-1.

213 lexes with a catalytic domain of MT3-MMP and TIMP-2 or TIMP-3 suggesting that pro-MMP-2 activation by

214 ferent modes of interaction between proMMP-2-TIMP-2 (or TIMP-4) and active MMP-2-TIMP-2 (or TIMP-4) c

215 proMMP-2-TIMP-2 (or TIMP-4) and active MMP-2-TIMP-2 (or TIMP-4) complexes.

216 inhibitor of metalloproteinases 1 (TIMP-1), TIMP-2, or GM6001.

217 ssue inhibitor of metalloproteases (TIMP)-1, TIMP-2, or the N-terminal inhibitory domain of TIMP-3 (N

218 degrees rotation toward the MT1-MMP(DeltaC)/TIMP-2 orientation.

219 r more in the arc toward the MT1-MMP(DeltaC)/TIMP-2 orientation.

220 The SP isolated from TIMP-2-overexpressing A549 cells also demonstrated impai

221 MMP-14 or TIMP-2 overexpression alone contributed as much as the c

222 unctional analysis of A549 cells showed that TIMP-2 overexpression increased chemosensitivity to cyto

223 th first-generation adenoviruses, but murine TIMP-2 overexpression mediated by helper-dependent adeno

224 rine tumor model, we compared the effects of TIMP-2 overexpression on gene expression profiles in vit

225 Levels of MMP-2 (p<0.0005) and TIMP-2 (p<0.01), were elevated in ischemic samples.

226 These findings demonstrate that TIMP-2 possesses two distinct types of anti-angiogenic a

227 P-14 together with the addition of exogenous TIMP-2 prevented the reduction of MMP-2 activation.

228 hibition of ERK1/2 phosphorylation decreased TIMP-2 production, and down-regulation of p38 MAPK activ

229 ulting in defective formation of the MT1-MMP/TIMP-2/proMMP-2 trimeric activation complex.

230 TIMP-2 promoter hypermethylation in the lymphoma cell li

231 methylation status of the CpG island in the TIMP-2 promoter region by methylation-specific polymeras

232 Furthermore, CpG methylation of TIMP-2 promoter was also shown in primary prostate tumor

233 Furthermore, TIMP-2 promotes cell differentiation via activation of t

234 ntegrin in the cerebral cortex suggests that TIMP-2 promotes neuronal differentiation and maintains m

235 In contrast, TIMP-2 protein expression was insignificantly different

236 -MMP protein expression at 12 hours, whereas TIMP-2 protein increased at 24 hours.

237 ary prostate tumors that expressed decreased TIMP-2 protein levels.

238 ic array data, demonstrating that, in vitro, TIMP-2 protein was increased in the HT-lo/diss variant,

239 iological effects were the result of a known TIMP-2 protein-protein interaction or of a receptor-medi

240 dose-dependent manner and were inhibited by TIMP-2 protein.

241 ing the gene for human TIMP-1 (RAdTIMP-1) or TIMP-2 (RAdTIMP-2) or a control adenovirus (RAd66) and w

242 The MMP-2 + MMP-3/TIMP-1 + TIMP-2 ratio was higher in PACG (0.83 +/- 0.80) and POAG

243 tistically significant (p > 0.05), the MMP-2/TIMP-2 ratio was highest in PACG (2.83 +/- 7.40), follow

244 ains of MMP-3 and MT1-MMP bound to TIMP-1 or TIMP-2, respectively, differ in the orientation of the T

245 n baseline and 8 weeks of therapy were TSP4, TIMP-2, SEPR, MRC-2, Antithrombin III, SAA, CRP, NPS-PLA

246 TIMP-2 significantly inhibited migration and apoptosis o

247 T-hi/diss tumors with recombinant TIMP-1 and TIMP-2 significantly reduced HT-hi/diss cell intravasati

248 ivated TIMP-2 and restored its expression in TIMP-2-silenced metastatic prostate cell lines.

249 binding of MeCP2 to methylated CpG island in TIMP-2-silenced metastatic prostate cell lines.

250 ning alone (P = .001) or coexistent with low TIMP-2 staining was associated with dolichoectasia only

251 r) have essentially identical affinities for TIMP-2 suggests that there are two TIMP binding sites on

252 own-regulation of p38 MAPK activity enhanced TIMP-2 synthesis.

253 demonstrate that the COOH-terminal domain of TIMP-2 (T2C) inhibits the proliferation of capillary EC

254 splay was used to identify variants of human TIMP-2 that are selective inhibitors of human MMP-1, a c

255 of TIMP-2, as well as the modified form Ala+TIMP-2 (that lacks MMP inhibitory activity) significantl

256 characterize the anti-angiogenic domains of TIMP-2, the endogenous MMP inhibitor that uniquely inhib

257 in complex with TIMP-1 or in a mixture with TIMP-2, the protease failed to rescue the inhibitory eff

258 r association constant and, in contrast with TIMP-2, TIMP-1 is inefficient against MT1-MMP.

259 her of the general MMP inhibitors, GM6001 or TIMP-2 (tissue inhibitor of MMP), or with the specific g

260 MT3-MMP requires TIMP-2 to accomplish full pro-MMP-2 activation and this

261 alpha 3 beta 1 integrin-mediated binding of TIMP-2 to endothelial cells.

262 While binding of TIMP-2 to MMP-12 hinders membrane interactions beside th

263 gnificantly correlated with LA dimension and TIMP-2 to MMP-2 ratio.

264 gesting that calcium promotes recruitment of TIMP-2 to MT1-MMP on the cell surface.

265 in vitro, and addition of the MMP inhibitor TIMP-2 to TSP-2-null cells restored tTG activity (0.3 +/

266 of tissue inhibitor of metalloproteinases-2 (TIMP-2) to the cell surface, resulting in defective form

267 TIMP-2 treatment also results in a concomitant increase

268 TIMP-2 treatment of hMVECs increases the association of

269 decreased activation in both TIMP-2 and Ala+TIMP-2 tumor cells.

270 ing agent 5-aza-2'-deoxycytidine resulted in TIMP-2 upregulation in both cell lines.

271 ery and tested for MMP-2, MMP-9, TIMP-1, and TIMP-2 using substrate gel electrophoresis (zymography)

272 p16, p21ras, p21WAF1, p27kip1, p53, TIMP-1, TIMP-2, vascular endothelial growth factor (VEGF), and b

273 d by NR4A2 and TNFalpha, while expression of TIMP-2 was antagonized.

274 llagen lattice containing active MT1-MMP and TIMP-2 was capable of activating pro-MMP-2, and exogenou

275 The pattern of epigenetic regulation of TIMP-2 was clearly distinct from that of MMPs and includ

276 of MMP-2 was not affected and expression of TIMP-2 was decreased.

277 ed compared with control values (P<0.05) and TIMP-2 was elevated (128+/-31%) compared with non-MFS (7

278 TIMP-2 was expressed in the cell lines HL60, U266 and XG

279 ycle arrest and neurite outgrowth induced by TIMP-2 was independent of MMP inhibitory activity.

280 In contrast, TIMP-2 was not hypermethylated in any of the 40 cases of

281 ng for TGF-beta, PDGF, TPA, PAI-1, MMP-2 and TIMP-2 was observed in all allografts at the time of rej

282 tudies, overexpression with either MMP-14 or TIMP-2 was performed to revert the cells to a preinjury

283 TIMP-2 was significantly higher in POAG (p = 0.004) comp

284 TIMP-2 was unchanged by bimatoprost and latanoprost, but

285 inogen activator, MMP-2, MMP-9, MT1-MMP, and TIMP-2 were determined by real-time PCR.

286 MMP-1, -3, and -9 and TIMP-2 were either not detected or their secretion was n

287 The mRNA levels of MMP-2, MMP-14, and TIMP-2 were measured by reverse transcription-polymerase

288 s of total protein, MMP-2, MMP-3, TIMP-1 and TIMP-2 were quantified by protein assay and enzyme immun

289 nificantly higher levels of IL-8, hBD-1, and TIMP-2 were secreted from controls than from thermally s

290 , and tissue inhibitor of metalloproteinase (TIMP-2) were consistently and progressively up-regulated

291 inhibitors of metalloproteinases (TIMP-1 and TIMP-2) were overexpressed by gene therapy in F344 rat l

292 The MMP inhibitors, TIMP-1 and TIMP-2, were significantly reduced in the urine of mice

293 higher levels of HIF-1alpha, TGF-beta3, and TIMP-2 when compared with those from normal pregnant wom

294 up-regulation of HIF-1alpha, TGF-beta3, and TIMP-2 when compared with wild-type mice; normal levels

295 In contrast, TIMP-2 and mutant Ala+TIMP-2, which is devoid of MMP inhibitory activity, bloc

296 dent pro-MMP-2 activation in the presence of TIMP-2, while maintaining their ability to inhibit activ

297 le with those previously reported for intact TIMP-2, while the NH2-terminal domain (T2N), which inhib

298 The interaction of TIMP-2 with alpha3beta1 integrin in the cerebral cortex

299 riants of the N-terminal domain of TIMP-2 (N-TIMP-2) with the sequences of the most selective clones

300 e inhibitor of metalloproteinase (TIMP)-1 or TIMP-2 would attenuate atherosclerotic plaque developmen

301 gate whether overexpression of MMP-14 and/or TIMP-2 would overcome the effect of nonlethal oxidant in