ライフサイエンスコーパス: TIMP

1 TIMP-1 372 T/C and *429 T/G genotypes in males were also

2 TIMP-1 induced P110/P85 PI3K-signalling and AKT phosphor

3 TIMP-1 was significantly higher in PACG (p = 0.049) and

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

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

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

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

8 P-9/ tissue inhibitor of metalloproteases-1 (TIMP-1) complex presents as a major form detected in nor

9 ing tissue inhibitor of metalloproteinase 1 (TIMP-1) and TIMP-3/4 as assessed by zymography and rever

10 2), tissue inhibitor of metalloproteinase 1 (TIMP-1), interleukin-6 (IL-6), and inducible nitric oxid

11 and tissue inhibitor of metalloproteinase 1 (TIMP-1), with the latter being the result of defective s

12 Tissue inhibitor of metalloproteinase-1 (TIMP-1) is the major endogenous regulator of matrix meta

13 and tissue inhibitor of metalloproteinase-1 (TIMP-1) were increased.

14 9), tissue inhibitor of metalloproteinase-1 (TIMP-1), macrophage chemoattractant protein-1 (MCP-1), v

15 of tissue inhibitor of metalloproteinase-1 (TIMP-1).

16 ), tissue inhibitor of metalloproteinases 1 (TIMP-1), and TIMP-4.

17 of tissue inhibitor of metalloproteinases 1 (TIMP-1), downregulated expression of proinflammatory cyt

18 9, tissue inhibitor of metalloproteinases 1 (TIMP-1), TIMP-2, CD68, and caspase 3.

19 of tissue inhibitor of metalloproteinases-1 (TIMP-1) by UDCA was studied using zymography and qRT-PCR

20 Tissue inhibitor of metalloproteinases-1 (TIMP-1) recently emerged as a pro-metastatic factor high

21 of tissue inhibitor of metalloproteinases-1 (TIMP-1).

22 e (NE), and MMP-9/tissue inhibitor of MMP-1 (TIMP)-1 ratio in patients with polycystic ovary syndrome

23 inase (MMP)-8 and tissue inhibitor of MMP-1 (TIMP-1) gene polymorphisms in generalized aggressive per

24 MMP)-8, MMP-9, and tissue inhibitor of MP-1 (TIMP-1) in biofluids of women with gestational diabetes

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

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

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

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

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

30 romoting a synergistic decrease in the MMP-1/TIMP-1 ratio.

31 1beta and CsA showed a decrease in the MMP-1/TIMP-1 ratio.

32 Comparing our structure of MMP-10cd.TIMP-1 with the previously solved structure of MMP-3cd.T

33 ssue inhibitor of metalloproteinase 1 and 2 (TIMP-1 and -2) into the spent medium, which was collecte

34 sue inhibitors of metalloproteinase 1 and 2 (TIMP-1 and TIMP-2), insulinlike growth factor-binding pr

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

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

37 Similarly, the MMP-2/TIMP-1 ratio was highest in PACG (1.50 +/- 1.69), follow

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

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

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

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

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

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

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

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

46 n the levels of total protein, MMP-2, MMP-3, TIMP-1 and TIMP-2 between patients on prostaglandin anal

47 Levels of total protein, MMP-2, MMP-3, TIMP-1 and TIMP-2 were quantified by protein assay and e

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

49 h the previously solved structure of MMP-3cd.TIMP-1 (Protein Data Bank entry 1UEA), we see substantia

50 of tissue inhibitor of metalloproteinases 4 (TIMP-4).

51 th Hg group (P <0.05) whereas salivary MMP-8/TIMP-1 molar ratio was lower in Gh compared with Hg grou

52 There was no significant difference in MMP-8/TIMP-1 ratio among the study groups (P >0.05).

53 Serum MMP-8, MMP-9, TIMP-1, MPO, and NE levels in circulation were assessed

54 We investigated the role of MMP-9/TIMP-1 in regulating innate antitumor immunity in breast

55 parameters and serum MMP-9 levels and MMP-9/TIMP-1 ratio in systemically healthy patients (P <0.05).

56 MMP-9/TIMP-1 ratio was significantly higher in patients with h

57 ted EAE mice had a significantly lower MMP-9/TIMP-1 ratio, and significantly lower MCT-1 and CD98 lev

58 livary MMP-9 and NE levels, as well as MMP-9/TIMP-1 ratios, were higher in the systemically healthy w

59 ormal DNA methylation and restored the MMP-9/TIMP-1, -2 balance.

60 nt of the cell-surface levels of the active, TIMP-free MT1-MMP enzyme.

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

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

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

64 ever, only pre-LT plasma OPN (P = 0.009) and TIMP-1 (P = 0.019) levels were significantly higher in r

65 els but inhibited type I collagen, MMP 1 and TIMP 1 mRNA levels.

66 1, -3, and -9 also decreased while PAI-1 and TIMP-1 and -3 increased.

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

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

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

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

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

72 ibitor of metalloproteinases 1 (TIMP-1), and TIMP-4.

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

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

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

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

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

78 GAgP) and to assess the effects of MMP-8 and TIMP-1 genotypes on the outcomes of non-surgical periodo

79 ed morphine-induced alterations in MMP-9 and TIMP expression and identified organs, including the liv

80 thylation and an imbalance between MMP-9 and TIMP-1 and -2 lead to ECM remodeling and renal fibrosis.

81 tor forkhead box protein O1 to the MMP-9 and TIMP-1 promoters.

82 MMP-8, MMP-9, and TIMP-1 levels were determined in gingival crevicular flu

83 By enabling profiling of active and TIMP-bound MMPs, our novel method may open opportunities

84 Upon correction of VD levels, TGF-beta1 and TIMP-1 levels were decreased, and the MMP2 and MMP9 leve

85 ers between groups showed that TGF-beta1 and TIMP-1 levels were significantly decreased and the MMP2

86 ough paracrine mechanisms involving bFGF and TIMP-2.

87 MMP-8 +17 C/G, -799 C/T, -381 A/G and TIMP-1 372 T/C, *429 T/G polymorphisms were determined b

88 MMP activity was higher and TIMP-1 levels were lower in oGVHD than in control (P < .

89 association of adipose metalloproteinase and TIMP expression with whole-body lipid distribution and i

90 the context of disease pathogenesis, MMP and TIMP expression are interpreted with respect to the prot

91 studies strongly supports a role for MMP and TIMP genes as candidate genes for non-syndromic cleft li

92 MMP-3, MMP-7, MMP-8, MMP-9, MMP-12, MPO, and TIMP-1 using multianalyte bead-based enzyme-linked immun

93 both arginase activity (EC(50)=261.8 nM) and TIMP-1 production (EC(50)=80.67 nM), and both pharmacolo

94 A combined model including elevated OPN and TIMP-1 levels, age <57, and absence of diabetes had the

95 it can be suggested that MMP-8 -799 C/T and TIMP-1 372 T/C, *429 T/G gene polymorphisms in males may

96 results suggest that metalloproteinases and TIMPs regulate adipose tissue remodelling and distributi

97 an adipocytes express metalloproteinases and TIMPs, and that their expression varies with inflammator

98 We found altered levels of MMPs and TIMPs as well as imbalance of MMP:TIMP ratios in the aqu

99 In this study, levels of specific MMPs and TIMPs in the aqueous humour of primary angle-closure gla

100 aluate a possible imbalance between MMPs and TIMPs in these samples.

101 ts of sulphated glycosaminoglycans, MMPs and TIMPs were assessed using the Dimethylmethylene Blue ass

102 accompanied by induction of low-angiogenic, TIMP-1-encumbered proMMP-9.

103 sion, resulting in production of angiogenic, TIMP-deficient proMMP-9.

104 This correlation seemed paradox as TIMP-1 is best described as an inhibitor of pro-tumourig

105 matrix metalloproteinase inhibitors, such as TIMP-4, holds promise as a means to interrupt the progre

106 eptor-mediated actions of TIMPs, inasmuch as TIMPs are themselves inhibitors of MMP-mediated proteoly

107 and NECA were less efficacious in augmenting TIMP-1 release by A(2A) receptor-deficient than control

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

109 he serum levels of 25-hydroxy VD, TGF-beta1, TIMP-1, MMP2 and MMP9 were measured at baseline and at t

110 We observed a linear relationship between TIMP-1 expression, liver metastatic burden, and infiltra

111 ere increased within the MI region with both TIMP-4 interventions, suggestive of matrix stabilization

112 d bioavailability of glycosaminoglycan-bound TIMP-3.

113 n activity and osteogenic differentiation by TIMP-1.

114 ession and produced proMMP-9 unencumbered by TIMP-1.

115 The broad-spectrum inhibition of MMPs by TIMPs and their N-domains (NTIMPs) is consistent with th

116 Pro-fibrogenic gene expressions (COL1, TIMP-1, TGF-beta1, alpha-SMA) and protein expression of

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

118 CP, ICTP, MMP-2, TGF-beta1, desmosine, CTGF, TIMP-1).

119 function of TIMP-1 may explain why elevated TIMP-1 levels in lung cancer patients are highly correla

120 an increase of both exogenous and endogenous TIMP-1 led to the upregulation of miR-210 in a CD63/PI3K

121 rence of TIMP-1 has revealed that endogenous TIMP-1 suppresses the proliferation, metabolic activity,

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

123 on serum neutrophilic enzyme levels, except TIMP-1.

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

125 rate that selective myocardial targeting for TIMP-4 induction through either a viral or transgenic ap

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

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

128 ion fraction was improved with either Ad-GFP-TIMP-4 or hTIMP-4exp.

129 Low MMP-8 and high TIMP-1 levels may indicate the role of the lozenges in r

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

131 cent protein (GFP) and the full-length human TIMP-4 (Ad-GFP-TIMP4) or GFP.

132 Adenoviruses carrying the human TIMP-1 gene had no effect on tumor growth or the immune

133 njections of adenoviruses carrying the human TIMP-1 or MMP-9 gene (AdMMP-9).

134 Our results identify TIMP-1 as an essential promoter of hepatic premetastatic

135 1 as a critical transcriptional activator in TIMP-3 regulation, and Sp1 activity is modulated by ERK1

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

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

138 ion into S phase and mitosis was impaired in TIMP-1-deficient livers after IRI.

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

140 ntly attenuated albumin-induced increases in TIMP-1 and collagen-I levels.

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

142 A uniform reduction in TIMP-4 post-MI has been observed.

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

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

145 Decreased GCF MMP-8 levels and increased TIMP-1 levels were found to be significant up to day 180

146 plus UVA also decreased MMP-1 and increased TIMP-1 protein levels.

147 Indeed, TIMP-1(-/-) livers were characterized by massive leukocy

148 o the adenosine augmentation of IL-4-induced TIMP-1 release, as both adenosine and NECA were less eff

149 a two-step mechanism, whereby LfcinB induces TIMP-1 through an IL-11-dependent pathway involving tran

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

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

152 racellular MMP-9 activity with its inhibitor TIMP-1 provides evidence that local MMP-9 activity in th

153 alloproteinases and their tissue inhibitors (TIMPs) have been implicated in human adipose tissue remo

154 The inhibitor of MMP-9 is TIMP-1, and high levels of this enzyme have been associa

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

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

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

158 Tissue inhibitor of metalloprotease (TIMP)-3 was expressed in CD146(+) TSCs at 1 wk with CTGF

159 not by tissue inhibitor of metalloproteases (TIMP)-1, TIMP-2, or the N-terminal inhibitory domain of

160 issue inhibitor of matrix metalloproteinase (TIMP)-1 were analyzed using multianalyte bead-based ELIS

161 issue inhibitor of matrix metalloproteinase (TIMP)-1, TIMP-2 and C-terminal propeptide of collagen ty

162 ssue inhibitors of matrix metalloproteinase (TIMP)-2, showed both increased expression and enhanced i

163 n of tissue inhibitors of metalloproteinase (TIMP) -1 and TIMP-2.

164 9 and tissue inhibitor of metalloproteinase (TIMP)-1 and -2 and also increased collagen and galectin-

165 lpha, tissue inhibitor of metalloproteinase (TIMP)-1 and collagen-I, which were blocked by HIF-1alpha

166 8 and tissue inhibitor of metalloproteinase (TIMP)-1 by enzyme-linked immunosorbent assay.

167 MP-1, tissue inhibitor of metalloproteinase (TIMP)-1, and TIMP-2 levels increased across all particip

168 , and tissue inhibitor of metalloproteinase (TIMP)-2 increased, and the expression of TIMP3 declined.

169 or 3, tissue inhibitor of metalloproteinase [TIMP]-1, and beta-2-microglobulin) were higher in rAKI v

170 e of tissue inhibitor of metalloproteinases (TIMP) 2 in the context of hepatocellular carcinoma (HCC)

171 ses, tissue inhibitor of metalloproteinases (TIMP)-1 has been thought to suppress tumor metastasis.

172 and tissue inhibitor of metalloproteinases (TIMP)-2 complex.

173 Tissue inhibitor of metalloproteinases (TIMP)-3 is an inhibitor of matrix metalloproteinases, wh

174 tor, tissue inhibitor of metalloproteinases (TIMP)-3, through blocking its interaction with the endoc

175 sue inhibitors of matrix metalloproteinases (TIMPs) and is associated with adverse left ventricular (

176 Tissue inhibitors of metalloproteinases (TIMPs) are pleiotropic extracellular proteins.

177 our tissue inhibitors of metalloproteinases (TIMPs) are potent inhibitors of the many matrixins (MMPs

178 and tissue inhibitors of metalloproteinases (TIMPs) in the aqueous humour of primary open-angle glauc

179 Tissue inhibitor of metalloproteinases (TIMPs) protect the extracellular matrix against excess d

180 the tissue inhibitor of metalloproteinases (TIMPs), are potentially interesting.

181 rs, tissue inhibitors of metalloproteinases (TIMPs), is abnormal in BOS.

182 and tissue inhibitors of metalloproteinases (TIMPs), leading to the accumulation of collagen in the a

183 MPs, tissue inhibitor of metalloproteinases (TIMPs).

184 of tissue inhibitors of metalloproteinases (TIMPs).

185 he kinetic inhibitors of metalloproteinases, TIMP-1 and PAI-1 protein levels, increased at MOI 25.

186 Compared to wildtype mice, TIMP-1(-/-) mice showed further impaired liver function

187 ase (MMP)-8, MMP-9, tissue inhibitor of MMP (TIMP)-1, myeloperoxidase (MPO), and neutrophil elastase

188 A role for MMP/TIMP balance in dolichoectasia appears more prominent in

189 he proteolytic consequences of increased MMP/TIMP ratios.

190 f MMPs and TIMPs as well as imbalance of MMP:TIMP ratios in the aqueous humour of PACG eyes that were

191 9, 10, and 13 and tissue inhibitors of MMPs (TIMPs) 1, 2, and 4 into the culture medium was assessed

192 via inhibition by tissue inhibitors of MMPs (TIMPs) and self-proteolysis.

193 (ADAMTS) and the tissue inhibitors of MMPs (TIMPs) was investigated using quantitative PCR.

194 ta1, and enzymes, tissue inhibitors of MMPs (TIMPs).

195 one hallmark of cancer progression, and MMPs/TIMPs may be involved in the local immune regulation.

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

197 Moreover, TIMP-1 knockdown cells exhibited enhanced beta-catenin t

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

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

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

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

202 involved in the growth factor activities of TIMP-1, however, remain controversial.

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

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

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

206 ar mechanism for high angiogenic capacity of TIMP-free proMMP-9 that would be uniquely produced in a

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

208 type, caused a substantial downregulation of TIMP-1 expression, resulting in production of angiogenic

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

210 not inhibit MMP indicated that the effect of TIMP-1 on beta-catenin signaling is MMP independent.

211 Moreover, UDCA regulates the expression of TIMP-1 and gelatinases activity in PMA stimulated cells.

212 noma development modulates the expression of TIMP-1 and sTNFR1, which in turn affect tumor cell proli

213 on of MMP-9 and stimulated the expression of TIMP-1 by preventing the binding of transcription factor

214 Expression of TIMP-1 is dramatically increased in response to a variet

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

216 An analysis of a mutant form of TIMP-1 that cannot inhibit MMP indicated that the effect

217 new pro-tumourigenic signalling function of TIMP-1 may explain why elevated TIMP-1 levels in lung ca

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

219 RNA interference of TIMP-1 has revealed that endogenous TIMP-1 suppresses th

220 The BAL levels of TIMP-1 and -2 and MMP-2, -3, -7, -8, and -9 were signifi

221 f BOS is associated with increased levels of TIMP-1 and -2 and total MMP-2, -3, -7, -8, and -9.

222 However, elevated systemic levels of TIMP-1 correlate with poor prognosis in cancer patients,

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

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

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

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

227 However, BAL levels of TIMP-bound MMP-8 and -9 were higher in BOS than in good

228 served in good outcome recipients, levels of TIMP-bound MMP-8 and -9 were higher in BOS.

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

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

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

232 Upon the overexpression of TIMP-1 in tumour cells, miR-210 was accumulated in exoso

233 and SDHD, were decreased in the presence of TIMP-1.

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

235 suggesting a metastasis-stimulating role of TIMP-1.

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

237 investigated the functional significance of TIMP-1 expression in a well-established mouse model of p

238 being the result of defective stimulation of TIMP-1 promoter activity by TLRs.

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

240 ay regulate the receptor-mediated actions of TIMPs, inasmuch as TIMPs are themselves inhibitors of MM

241 ibition represent two important functions of TIMPs that have the potential to affect tissue pathology

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

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

244 truct with cardiac-restricted overexpression TIMP-4 (hTIMP-4exp) was used in a parallel set of studie

245 tal cancer patients, tumor as well as plasma TIMP-1 levels were correlated with synchronous liver met

246 % CI, 0.80-0.90 for clinical variables plus [TIMP-2].[IGFBP7]).

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

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

249 Only recently, TIMP-1 has been revealed as a signalling molecule that c

250 nd systemic depletion of neutrophils reduced TIMP-1-induced increased liver susceptibility towards me

251 signaling pathway to critically up-regulate TIMP-1 expression, as a consecutive secondary cellular r

252 Serum MMP-8 levels and salivary TIMP-1 levels were higher in Gh compared with Hg group (

253 ately assist in the design of more selective TIMP-based inhibitors tailored for specificity toward in

254 All study groups had similar serum TIMP-1 levels (P >0.05).

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

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

257 ICAM-1) and pro-fibrogenic (Col1, alpha-SMA, TIMP-1) genes.

258 High systemic TIMP-1 led to increased hepatic SDF-1 levels, which in t

259 In mice, high systemic TIMP-1 levels increased the liver susceptibility towards

260 Our results demonstrate that TIMP-1 is a direct regulator of hMSC functions and revea

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

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

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

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

265 iew reflects our emerging understanding that TIMP signaling and MMP inhibition represent two importan

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

267 The TIMP-1 levels were decreased in SJS and OCP patients whe

268 ignificantly down-regulated member among the TIMP family in human HCCs.

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

270 rucial functional role of neutrophils in the TIMP-1-induced premetastatic niche.

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

272 crophages were nonangiogenic, although their TIMP-1 was severely downregulated.

273 -derived M2 macrophages also shut down their TIMP-1 expression and produced proMMP-9 unencumbered by

274 y of murine M2 macrophages depended on their TIMP-free proMMP-9, Mmp9-null M2 macrophages were nonang

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

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

277 tivity-based extraction and their binding to TIMP-1, -2, -3, and -4 in bronchoalveolar lavage (BAL) o

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

279 ial binding of stromelysin family members to TIMP-1.

280 The MMP-8-to-TIMP-1 and MMP-9-to-TIMP-1 ratios were markedly elevated

281 The MMP-8-to-TIMP-1 and MMP-9-to-TIMP-1 ratios were markedly elevated in SJS and OCP tear

282 Elevated MMP-to-TIMP ratios and MMP activity suggest an imbalance in tea

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

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

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

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

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

288 In parallel, UDCA upregulates TIMP-1 that in turn inhibits matrix metalloproteinases,

289 ing MMP-2, MMP-9 expression and upregulating TIMP-1.

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

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

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

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

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

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

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

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

298 ng to secreted amounts of IL-8, hBD-1, VEGF, TIMP-1, and TIMP-2 from corresponding EVPOMEs.

299 st after its complexing with TIMP-1, whereas TIMP-1 silencing in M0/M1 macrophages rendered them both

300 proMMP-9 was lost after its complexing with TIMP-1, whereas TIMP-1 silencing in M0/M1 macrophages re