ライフサイエンスコーパス: TIMP-3

1 or tissue inhibitor of metalloproteinases-3 (TIMP-3).

2 PAI-2A) and protease inhibitors (TIMP-2 and TIMP-3).

3 he N-terminal inhibitory domain of TIMP-3 (N-TIMP-3).

4 itutes the basis of the ECM binding motif in TIMP-3.

5 mmunostaining of Fas, Fas-L, cleaved Bid and TIMP-3.

6 by TIMP-1 and less efficiently by TIMP-2 and TIMP-3.

7 d expression of a metalloprotease inhibitor, TIMP-3.

8 uded hemisphere but no significant change in TIMP-3.

9 s VHL, p16/CDKN2a, p14ARF, APC, RASSF1A, and Timp-3.

10 tion of activity by the endogenous inhibitor TIMP-3.

11 could be reversed with recombinant wild type TIMP-3.

12 S156C (Ser(156) changed to cysteine) mutant TIMP-3.

13 form a double track on the outer surface of TIMP-3.

14 ffinity similar to that of full-length mouse TIMP-3.

15 located within the N-terminal three loops of TIMP-3.

16 hibitor of metalloproteinases (TIMP) family, TIMP-3.

17 all of these fragments were able to bind to TIMP-3.

18 d bioavailability of glycosaminoglycan-bound TIMP-3.

19 es from patients with CD increased levels of TIMP-3.

20 al tissues from patient with CD up-regulates TIMP-3.

21 otype of ocular vessels in mice deficient in TIMP-3.

22 cornea and laser-induced CNV in mice lacking TIMP-3.

23 intervertebral disc tissue, as was mRNA for TIMP-3.

24 diated Ad-MMP-2-Si-CM-stimulated increase of TIMP-3.

25 ethylated in 20%), p16 (18%), CACNA1G (16%), TIMP-3 (11%), E-cad (7%), THBS1 (7%), hMLH1 (4%), DAP ki

26 e-associated VEGFR-2 in endothelial cells of Timp-3(156/156) mutant mice as well as in human Sorsby f

27 les was detected in 40% for RARbeta, 26% for TIMP-3, 25% for p16INK4a, 21% for MGMT, 19% for DAPK, 18

28 nhibitor of metalloproteinase 1 (TIMP-1) and TIMP-3/4 as assessed by zymography and reverse zymograph

29 TIMP-3 (74+/-23%) was reduced compared with control valu

30 g MMP) because the cleavage was inhibited by TIMP-3 (a potent inhibitor of ADAMTS4), but not by TIMP-

31 cent cells, and is specifically inhibited by TIMP-3, a matrix-associated metalloproteinase inhibitor.

32 ere that the N-terminal inhibitory domain of TIMP-3, a member of the TIMP family that has functional

33 We showed that EGF and TIMP-3 act through TACE as endogenous regulators of meso

34 TIMP-3 also enhances the activation of pro-MMP-2 by MT3-

35 ed by TIMP-1 or by the N-terminal portion of TIMP-3, although FGF-2 did not affect production of the

36 of tissue inhibitor of metalloproteinases-3 (TIMP-3), an endogenous inhibitor of ADAMTS-4 and -5.

37 Tissue inhibitor of metalloproteinase-3 (TIMP-3), an extracellular matrix-associated MMP inhibito

38 totally abolished MMP-inhibitory activity of TIMP-3 and also failed to promote apoptosis.

39 accumulation and expression overlap of both TIMP-3 and EFEMP1 between the retinal pigment epithelia

40 , included lower levels of MMPs 3 and 10 and TIMP-3 and higher levels of ADAM-12 and MMP-23 in painfu

41 og of suramin, has an increased affinity for TIMP-3 and increased ability to inhibit TIMP-3 endocytos

42 RP1, thus increasing extracellular levels of TIMP-3 and inhibiting cartilage degradation by the TIMP-

43 atients with CD were cultured with exogenous TIMP-3 and levels of inflammatory cytokines were measure

44 support the further development of combined TIMP-3 and oncolytic virotherapy for cancer.

45 After UUO operation, renal mRNA levels for Timp-3 and plasminogen activator inhibitor-1 were signif

46 for matrilysin, stromelysins 1-3, TIMP-1, or TIMP-3 and secretion of these proteins, indicating that

47 s with the full-length inhibitors TIMP-1 and TIMP-3 and the hybrid N.TIMP-2/C.TIMP-1 by a factor of u

48 Activity was inhibited moderately by TIMP-3 and TIMP-4 and weakly inhibited by TIMP-2 but not

49 s, tissue inhibitor of metalloproteinases 3 (TIMP-3), and cycloheximide pretreatment were used to ide

50 of the TACE (also known as ADAM17) inhibitor TIMP-3, and lead to the inhibition of tumor necrosis fac

51 MPs), showed strong inhibition using TIMP-2, TIMP-3, and TIMP-4, while TIMP-1 was less efficient.

52 by other protease inhibitors such as TIMP-2, TIMP-3, and/or plasminogen activator inhibitor-1 or to t

53 Tissue inhibitor of metalloproteinase-3 (TIMP-3) antagonizes matrix metalloproteinase activity an

54 owth, and that the antiangiogenic effects of TIMP-3 appear to be mediated through the inhibition of f

55 e associated with functional specialization, Timp-3 appears to have conserved most of the functions o

56 mera, in which the N-terminal three loops of TIMP-3 are replaced by those of TIMP-2, failed to induce

57 loproteinase-2 (TIMP-2) and pericyte-derived TIMP-3 are shown to coregulate human capillary tube stab

58 Models of the structures of dN-TIMP and N-TIMP-3 are strikingly similar in surface charge distribu

59 ore than 100-fold, improving the efficacy of TIMP-3 as an aggrecanase inhibitor.

60 erin by endothelial cells in the presence of TIMP-3 as seen both in an in vitro assay and in TIMP-3-o

61 Here, we overexpressed TIMP-3 at the luminal surface of human saphenous veins b

62 Immunoreactivity of TIMP-3 bands in each western blot was densitometrically

63 TIMP-3 binding may be important for the cellular regulat

64 Among the proteins analyzed, TIMP-3 bound to LRP-1 with highest affinity (K(D) = 1.68

65 TIMP-3 bound to sLRP-1, which was resistant to endocytos

66 h factor-beta augmented levels of TIMP-1 and TIMP-3 but not TIMP-2.

67 TIMP-3 (but not TIMP-1 or -2) effectively blocked cleava

68 and tissue inhibitor of metalloproteinase-3 (TIMP-3) but not TIMP-1 or -2 inhibited such shedding.

69 nase III or chondroitinase ABC also releases TIMP-3, but neither one alone gives complete release.

70 e presence of TACE small interfering RNA and TIMP-3, but not TIMP-1.

71 inhibitors of metalloproteinases TIMP-2 and TIMP-3, but only partially by TIMP-1.

72 All PGAs increased TIMP-3, but only unoprostone increased TIMPs1 and -4 by

73 ding was differentially blocked by TIMP-1 or TIMP-3, but was insensitive to treatment with TIMP-2.

74 In this study, the loss of TIMP-3 by loss of heterozygosity and/or promoter hyperme

75 y number of ADAMTS 1, 4, 5, 8, 9, and 15 and TIMP-3 by real-time reverse transcription-polymerase cha

76 Additionally, we found that TIMP-3 can facilitate the clearance of its target metall

77 derstanding the mechanism(s) by which mutant TIMP-3 can induce abnormal neovascularization provides i

78 e results demonstrate that overexpression of TIMP-3 can inhibit angiogenesis and associated tumor gro

79 Mutations in TIMP-3 cause Sorsby Fundus Dystrophy, a dominant inherit

80 a K(D) of 34.6 nM for LRP-1, while the MMP-1/TIMP-3 complex had a sevenfold higher affinity (K(D) = 4

81 face and formation of soluble LRP-1 (sLRP-1)-TIMP-3 complexes.

82 d B beta-strands of the N-terminal domain of TIMP-3 contain two potential heparin-binding sequences r

83 Inhibitory activity correlated well with TIMP-3 content (r = 0.82) and was also significantly hig

84 TIMP-3 content in AMD eyes was elevated relative to that

85 During normal aging, TIMP-3 content in Bruch's membrane of the macula shows a

86 TIMP-3 content ranged from 92 to 1061 ng/cm2 and increas

87 ylation and that discrete regions within the TIMP-3 CpG island may be important for the silencing of

88 TIMP-3 decreased surface levels of ADAM-10, APP, and Apo

89 in tissue inhibitor of metalloproteinase 3 (TIMP-3)-deficient mice, supporting physiological regulat

90 he activation state of MMPs in the retina of TIMP-3-deficient mice was examined by in situ zymography

91 CaPPS inhibition of aggrecan degradation is TIMP-3 dependent.

92 7/30/76E + R163/K165Q) resulted in a soluble TIMP-3 devoid of ECM-adhering ability.

93 a cell type not heretofore known to express TIMP-3, did so in atheroma in vivo.

94 However, N-TIMP-3 displayed profound inhibitory activity against th

95 In AMD eyes, TIMP-3 distribution in Bruch's membrane was abundant in

96 the core of the MMP interaction surface of N-TIMP-3 dramatically reduce the binding affinity for MMPs

97 The molecular basis for the TIMP-3:ECM association has never been fully investigated

98 for TIMP-3 and increased ability to inhibit TIMP-3 endocytosis and protect cartilage.

99 lencing experiments showing that the loss of TIMP-3 expression abrogated the effect of N6L.

100 igned to investigate ADAMTS-1, -4 and -5 and TIMP-3 expression after experimental cerebral ischaemia

101 EC-pericyte interactions strongly induce TIMP-3 expression by pericytes, whereas ECs produce TIMP

102 TIMP-3 expression has been observed to be repressed in m

103 y, the suppression of EC TIMP-2 and pericyte TIMP-3 expression leads to capillary tube regression in

104 elationship between metastatic potential and TIMP-3 expression level.

105 induced phenotypic changes, and that loss of TIMP-3 expression may enhance the invasion potential of

106 These data suggest that early, transient TIMP-3 expression mediates specific HGF-induced phenotyp

107 A marked decrease in TIMP-3 expression was caused by promoter hypermethylatio

108 Similarly, TIMP-3 expression was detected only when treated with CT

109 TIMP-3 expression was restored after 5-aza-2'deoxycytidi

110 TIMP-3 expression was significantly higher in AAA (mean,

111 hat ERK1/2 functions as the major pathway in TIMP-3 expression, whereas Akt plays a minor role.

112 in tubular cells, and upregulation of renal TIMP-3 expression.

113 wk with CTGF, in contrast to control with no TIMP-3 expression.

114 CaPPS also increased the affinity of TIMP-3 for ADAMTS-4 and -5 by more than 100-fold, improv

115 , demonstrating opposite roles of TIMP-1 and TIMP-3 for the regulation of extrinsic apoptosis.

116 as suramin and pentosan efficiently extract TIMP-3 from the postpartum rat uterus.

117 Mutations in the Timp-3 gene cause Sorsby fundus dystrophy (SFD), a hered

118 ssue inhibitor of metalloproteinases type 3 (TIMP-3) gene by greater than tenfold.

119 the tissue inhibitor of metalloproteinase-3 (TIMP-3) gene.

120 the tissue inhibitor of metalloproteinase-3 (TIMP-3) gene.

121 xpression of TIMP mRNA was TIMP-2 > TIMP-1 > TIMP-3 > TIMP-4.

122 revealed that although tumors overexpressing TIMP-3 had an increased number of CD31(+) endothelial ce

123 S156C TIMP-3 had reduced matrix metalloproteinase (MMP) inhibi

124 Loss of TIMP-3 has been related to the acquisition of tumorigene

125 TIMP-3 has the potential to inhibit angiogenesis.

126 mly highly expressed in native tissues, with TIMP-3 having the highest expression in the epithelial t

127 ression models showed that patients with low-TIMP-3/high-IL-6 tumors had shorter overall survival and

128 TIMP-3, however, was shown to enhance extrinsic cell dea

129 s, the retention of their ability to repress TIMP-3 illustrate one mechanism by which mutant forms of

130 In both models, high TIMP-3 immunoreactivity occurred in the luminal and uppe

131 ic mice, suggesting that increased levels of TIMP-3 in AD may contribute to higher levels of Abeta.

132 ed that CTGF-induced expression of IL-10 and TIMP-3 in CD146(+) TSCs are regulated by JNK/signal tran

133 Ectopic overexpression of TIMP-3 in cultured leiomyosarcoma cells conferred an epi

134 cell surface and that cell surface levels of TIMP-3 in endotoxin-activated human macrophages are dyna

135 We investigated the role of TIMP-3 in intestinal inflammation in human beings and mi

136 tion and flow cytometry to measure levels of TIMP-3 in intestine samples from patients with Crohn's d

137 Loss or reduction of TIMP-3 in mice promotes development of colitis.

138 to effect sustained autocrine expression of TIMP-3 in murine neuroblastoma and melanoma tumor cells

139 The implication of TIMP-3 in N6L-induced inhibition of cell invasion was ev

140 dN-TIMP resembles mammalian N-TIMP-3 in strongly inhibiting human tumor necrosis facto

141 This was associated with an increase in TIMP-3 in the cell culture medium without a change in TI

142 shows colocalization of heparan sulfate and TIMP-3 in the endometrium subjacent to the lumen of the

143 of sLRP-1 can thus increase the half-life of TIMP-3 in the extracellular space, controlling the bioav

144 The purpose of this study was to localize TIMP-3 in the retina/choroid of normal human and animal

145 r MT1-MMP, MMP-2, MMP-3, TIMP-1, TIMP-2, and TIMP-3 in the scleras of tree shrews that had received e

146 res), MMP-17 (in four of five cultures), and TIMP-3 (in all five cultures); MMP-1, -2, -12, -14, -15,

147 r, tissue inhibitor of metalloproteinases 3 (TIMP-3), in human intervertebral disc tissue.

148 indings suggest that regulated expression of TIMP-3, in addition to the presence of TIMP-1 and TIMP-2

149 concentrations and for longer than wild-type TIMP-3, indicating that their increased half-lives impro

150 Here we demonstrate that overexpression of TIMP-3 induced activation of initiator caspase-8 and -9

151 Furthermore, TIMP-3 induced mitochondrial activation as demonstrated

152 inhibitor of caspase-8, completely inhibited TIMP-3-induced apoptosis.

153 tle is known about the mechanisms underlying TIMP-3-induced apoptosis.

154 Fas-associated death domain mutant inhibited TIMP-3-induced death substrate cleavage and apoptotic de

155 TIMP-3 induction was mediated by ERK activation.

156 es, tissue inhibitor of metalloproteinase 3 (TIMP-3) induction.

157 tudies suggesting that genetic variants near TIMP-3 influence susceptibility to age-related macular d

158 Endogenous matrix metalloprotease inhibitor TIMP-3 inhibited activity.

159 We found that TIMP-3 inhibited alpha-secretase cleavage of APP and an

160 report that the endogenous ADAM17 inhibitor TIMP-3 inhibits ADAM17 activity only when it is bound to

161 TIMP-3 inhibits chemotaxis of vascular endothelial cells

162 e previously reported that overexpression of TIMP-3 inhibits MMPs and induces apoptotic cell death in

163 ary to the accepted view, we have found that TIMP-3 interacts with the ECM via both its N- and C-term

164 ated protein-1 (LRP-1) plays a major role in TIMP-3 internalization.

165 Inhibition kinetic studies showed that TIMP-3 is a high affinity inhibitor of MT3-MMP when comp

166 These results demonstrate that TIMP-3 is a major regulator of MT3-MMP activity and furt

167 TIMP-3 is a member of a family of metalloproteinase inhi

168 ue inhibitors of metalloproteinases (TIMPs), TIMP-3 is distinguished by its tighter binding to the ex

169 TIMP-3 is down-regulated in inflamed intestine of patien

170 that methylation-associated inactivation of TIMP-3 is frequent in many human tumors.

171 ptosis assays, that the prodeath function of TIMP-3 is located within the N-terminal three loops and

172 s we demonstrate that the prodeath domain of TIMP-3 is located within the N-terminal three loops of T

173 Immunostaining of TIMP-3 is lost upon digestion of tissue sections with he

174 four mammalian TIMPs (TIMP-1 to -4) but only TIMP-3 is sequestered to the extracellular matrix (ECM).

175 Herein, we show that TIMP-3 is silenced in association with aberrant promoter

176 TIMP-3 is upregulated and may compensate for the increas

177 Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a central inhibitor of matrix-degrading and s

178 Tissue inhibitor of metalloproteinase-3 (TIMP-3) is a dual inhibitor of the matrix metalloprotein

179 Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a matrix-bound inhibitor of matrix metallopro

180 Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a matrix-bound inhibitor of matrix metallopro

181 Tissue Inhibitor of metalloproteinases-3 (TIMP-3) is a potent matrix-bound angiogenesis inhibitor.

182 The tissue inhibitor of metalloproteinase 3 (TIMP-3) is essential for limiting inflammation; therefor

183 The two mutants (TIMP-3 K26A/K45A and K42A/K110A) with lowest rates of up

184 TIMP-3 K26A/K45A retained higher affinity for sulfated g

185 of control LPMCs with TGF-beta1 up-regulated TIMP-3; knockdown of Smad7, an inhibitor of TGF-beta1, i

186 e evaluated the susceptibility of wild-type, TIMP-3-knockout (TIMP-3-KO), and transgenic (TIMP-3-Tg)

187 TIMP-3-KO mice developed severe colitis after administra

188 ctivating gene-1-null mice with T cells from TIMP-3-KO mice increased the severity of colitis, compar

189 e-1-null mice after transfer of wild-type or TIMP-3-KO T cells.

190 usceptibility of wild-type, TIMP-3-knockout (TIMP-3-KO), and transgenic (TIMP-3-Tg) mice to induction

191 ade of LRP1 inhibited endocytic clearance of TIMP-3, leading to an increase in cell surface levels of

192 TIMP-4 protein expression level, whereas the TIMP-3 level increased in CBS-/+, GABA(A)-/-, and CBS-/+

193 evelopment of novel therapeutics to increase TIMP-3 levels and inhibit cartilage degradation in osteo

194 TIMP-3 levels in AMD eyes were significantly higher than

195 We also analyzed TIMP-3 levels in lamina propria mononuclear cells (LPMCs

196 Following LPS stimulation, TIMP-3 levels on the surface of macrophages increased 4-

197 This dynamic regulation of cell surface TIMP-3 levels was independent of changes in TIMP-3 mRNA

198 2 mRNA levels were significantly higher, and TIMP-3 levels were lower by 1 to 4 days of minus lens tr

199 e, showing that MMP-2 inhibition upregulates TIMP-3 levels, which in turn, promotes apoptosis in lung

200 In vivo, TO-901317 decreased brain TIMP-3 levels.

201 e tissue that normally expresses the highest TIMP-3 levels.

202 ng inflammation; therefore, we expected that TIMP-3 loss might induce chronic inflammation, thereby p

203 Mechanistic studies indicated that TIMP-3 loss promoted interleukin-6 (IL-6) production, wh

204 eriods when compared with patients with high-TIMP-3/low-IL-6 tumors.

205 at the mechanism of inhibition of ADAM-17 by TIMP-3 may be distinct from that for MMPs.

206 Higher levels of TIMP-3 may contribute to the thickening of Bruch's membr

207 In summary, loss of TIMP-3 may increase IL-6 production via the tumor necros

208 Thus, abnormal local function of TIMP-3 may lead to the characteristic Bruch's membrane d

209 cular degeneration, these results imply that TIMP-3 may regulate the development of the choroidal vas

210 erimental stroke, together with no change in TIMP-3, may promote ECM breakdown after stroke, enabling

211 the ability of CaPPS to block endocytosis of TIMP-3 mediated by low-density lipoprotein receptor-rela

212 ttle is know about the mechanisms underlying TIMP-3-mediated apoptosis.

213 RK1/2 are crucial events in the induction of TIMP-3-mediated endothelial apoptosis in MMP-2 inhibited

214 There were no significant changes in TIMP-3 message levels in retinal tissues, and TIMP-1 mes

215 f metalloproteinases 1 (TIMP-1), TIMP-2, and TIMP-3 messenger RNA (mRNA) expression in articular cart

216 The most frequent TIMP-3 methylation was found in renal cancers, which ori

217 ed for the expression of TIMP-1, TIMP-2, and TIMP-3 mRNA and protein using RT-PCR and Western blot an

218 ed the human macrophage as a novel source of TIMP-3 mRNA and protein.

219 erved changes in MT1-MMP, MMP-2, TIMP-2, and TIMP-3 mRNA are consistent with visually modulated MT1-M

220 the cell culture medium without a change in TIMP-3 mRNA expression suggesting its release from cell

221 HGF transiently induced TIMP-3 mRNA in keratinocytes as well as kidney and mamma

222 differential changes in MT1-MMP, MMP-2, and TIMP-3 mRNA levels were all restricted to the treated ey

223 TIMP-3 levels was independent of changes in TIMP-3 mRNA levels, but correlated with shedding of LRP1

224 TIMP-3 mRNA was detected in uninfected (wounded and unwo

225 e tongue expressed stromelysin-3, TIMP-2 and TIMP-3 mRNA while stromelysin-3, TIMP-2 and gelatinase A

226 Here we report that expression of S156C TIMP-3 mutation in endothelial cells results in an abnor

227 However, the mechanism by which TIMP-3 mutations induce the disease phenotype in SFD rem

228 s that contribute to CNV as a consequence of TIMP-3 mutations will provide insight into the pathophys

229 g enzyme (TACE)) by the inhibitory domain of TIMP-3 (N-TIMP-3) shows positive cooperativity.

230 MP-2, or the N-terminal inhibitory domain of TIMP-3 (N-TIMP-3).

231 al neovascularization (CNV) were examined in TIMP-3-null mice.

232 Studies with TIMP-3-null mouse cartilage indicated that CaPPS inhibit

233 Aberrant methylation of TIMP-3 occurred in primary cancers of the kidney, brain,

234 indicates that significant downregulation of TIMP-3 occurs in OA chondrocytes, suggesting a beneficia

235 The effects of the absence of TIMP-3 on the phosphorylation status of the VEGF-recepto

236 lso suggest the potential therapeutic use of TIMP-3 or synthetic MMP inhibitors in this disease.

237 P-3 as seen both in an in vitro assay and in TIMP-3-overexpressing tumors.

238 TIMP-3 overexpression induced DNA synthesis, and promote

239 Taken together, these results indicate that TIMP-3 overexpression induces a type II apoptotic pathwa

240 hlight the potential therapeutic benefit for TIMP-3 overexpression to reduce neointima formation asso

241 In particular, we demonstrated that TIMP-3 overexpression using gene transfer induces apopto

242 medial layer were significantly elevated by TIMP-3 overexpression.

243 a), tissue inhibitor of metalloproteinase 3 (TIMP-3), p16INK4a, O6-methylguanine-DNA-methyltransferas

244 Tissue inhibitor of metalloproteinases-3 (TIMP-3) plays a key role in regulating extracellular mat

245 These data suggest that TIMP-3 preferentially routes APP and ApoER2 away from th

246 finding using real-time PCR and by measuring TIMP-3 protein in glia, SY5Y cells, and COS7 cells.

247 an in vivo quest for binding partners of the TIMP-3 protein in the subretina, we identified epidermal

248 ylation correlated with a lack of detectable TIMP-3 protein in these tumors.

249 TIMP-3 protein levels were increased in human Alzheimer'

250 dystrophy, the authors have examined whether TIMP-3 protein plays a role in the regulation of angioge

251 Increased TIMP-3 protein secretion returned to basal levels within

252 Although both wild type and N-terminal TIMP-3 proteins promoted apoptosis, a T-2/T-3 chimera, i

253 'deoxycytidine-mediated demethylation of the TIMP-3 proximal promoter region.

254 ata show that increased deposition of active TIMP-3, rather than dysregulation of metalloproteinase i

255 Exogenous TIMP-3 reduced levels of inflammatory cytokines in CD LP

256 1 as a critical transcriptional activator in TIMP-3 regulation, and Sp1 activity is modulated by ERK1

257 Mutagenesis experiments reveal that TIMP-3 requires its proteinase inhibitory function to in

258 Here, we used molecular modeling to predict TIMP-3 residues potentially involved in binding to LRP1

259 cts of intracoronary delivery of recombinant TIMP-3 (rTIMP-3) on I/R injury.

260 te by tissue inhibitor of metalloprotease-3 (TIMP-3)-sensitive metalloproteinases in response to a va

261 TACE)) by the inhibitory domain of TIMP-3 (N-TIMP-3) shows positive cooperativity.

262 However, the cellular uptake of TIMP-3 significantly slowed down after 10 h due to shedd

263 Genomic bisulfite sequencing revealed that TIMP-3 silencing was related to the overall density of m

264 TIMP-3 similarly bridged binding of MMP-13 and MMP-14 to

265 a catalytic domain of MT3-MMP and TIMP-2 or TIMP-3 suggesting that pro-MMP-2 activation by MT3-MMP i

266 injury after inhibition of TACE activity by TIMP-3 suggests that TACE inhibition may play an importa

267 using a monoclonal antibody against a human TIMP-3 synthetic peptide.

268 and inhibiting cartilage degradation by the TIMP-3 target enzyme, adamalysin-like metalloproteinase

269 olitis after administration of TNBS, whereas TIMP-3-Tg mice were resistant to TNBS-induced colitis.

270 TIMP-3-knockout (TIMP-3-KO), and transgenic (TIMP-3-Tg) mice to induction of colitis with 2, 4, 6-tri

271 atheroma (n= 14) had 5-fold higher levels of TIMP-3 than nonatherosclerotic tissue (n= 10).

272 y a tissue inhibitor of metalloproteinase-3, TIMP-3, that can inhibit tumor necrosis factor alpha con

273 issue Inhibitor of Matrix Metalloproteinase (TIMP-3, TIMP-4), collagen-III and elastin levels were me

274 To date TIMP-3 (tissue inhibitor of matrix metalloproteinases-3)

275 rough EC-derived TIMP-2 and pericyte-derived TIMP-3 to block both the capillary tube formation and re

276 Addition of TIMP-3 to HTB94 human chondrosarcoma cells increased the

277 ar space, controlling the bioavailability of TIMP-3 to inhibit metalloproteinases.

278 ve previously determined a novel function of TIMP-3 to inhibit vascular endothelial growth factor (VE

279 apoptosis, a phenotype reproduced by adding TIMP-3 to uninfected cells, but not by a synthetic MMP i

280 urthermore, a point mutation at residue 1 of TIMP-3 totally abolished MMP-inhibitory activity of TIMP

281 Antisense suppression of TIMP-3 was associated with a scattered, fibroblastic cel

282 of vascular endothelial growth factor 2 and TIMP-3 was determined by coimmunoprecipitation experimen

283 TIMP-3 was endocytosed and degraded by a number of cell

284 The inhibitory function of TIMP-3 was evaluated with reverse zymography.

285 The N-terminal domain of human TIMP-3 was expressed and found to bind to heparin with a

286 In addition, TIMP-3 was found in the medium of treated but not contro

287 The COOH-terminal end of TIMP-3 was involved in the interaction.

288 evels, whereas high expression of TIMP-2 and TIMP-3 was observed predominantly in neurons and in the

289 TIMP-3 was present uniformly across Bruch's membrane in

290 onset of egg laying in infected mice, while TIMP-3 was unchanged.

291 t the IGD-aggrecanase site, was inhibited by TIMP-3, was blocked after preincubation with an antibody

292 Using the ECM binding motif derived from TIMP-3, we have also created a TIMP-1 mutant (K26/27/30

293 ains of the TIMPs and exhaustive mutation of TIMP-3, we have identified the surface residues directly

294 All these aggrecanases and TIMP-3 were also detected immunohistochemically in disc

295 Levels of TIMP-3 were reduced in intestine samples from patients w

296 Stromelysin-1 (MMP-3) and TIMP-3 were, however, over expressed in the AAA samples

297 fect production of the inhibitors TIMP-1 and TIMP-3 when IL-1alpha was present.

298 ptosis is mediated through the N terminus of TIMP-3, which harbors the MMP inhibitory domain.

299 overed that suramin (C51H40N6O23S6) bound to TIMP-3 with a KD value of 1.9 +/- 0.2 nM and inhibited i

300 gous, it was assumed that the interaction of TIMP-3 with adamalysins is closely similar.