ライフサイエンスコーパス: MMP-8

1 uppression of tissue damage and degradation (MMP-8 ).

2 ll (PMN)-derived matrix metalloproteinase-8 (MMP-8).

3 ere analyzed by immunofluorometric assay for MMP-8.

4 essing either control vector or E198A mutant MMP-8.

5 r MIP-1alpha-degrading activity than soluble MMP-8.

6 on of pro-MMP-13 but not of pro-MMP-2 or pro-MMP-8.

7 60 ng/10(6) cells) exclusively as latent pro-MMP-8.

8 which are the major cell type that expresses MMP-8.

9 MMP-8 +17 C/G, -799 C/T, -381 A/G and TIMP-1 372 T/C, *4

10 samples, MMP-1 (70+/-16%), MMP-3 (77+/-18%), MMP-8 (75+/-11%), MMP-9 (69+/-14%), and MMP-12 (85+/-15%

11 e present findings, it can be suggested that MMP-8 -799 C/T and TIMP-1 372 T/C, *429 T/G gene polymor

12 Distribution of the MMP-8 -799 C/T genotypes was significantly different bet

13 Compared to controls at 1 day p.i., MMP-8, -9, -10, -12, -13, -19, and TIMP-1 were significa

14 Transcriptional and translational levels of MMP-8, -9, -13, and TIMP-1 increase during the early sta

15 Using threshold values of MMP-8 (94 ng/muL), elastase (33 ng/muL), sialidase (23 n

16 te does not fit within the catalytic site of MMP-8, a representative fibrillar collagenase.

17 nhibition of matrix metalloproteinases (MMP)/MMP-8 abolished production of sIL-13Ralpha2 from human c

18 wild-type (WT) mice show that membrane-bound MMP-8 accounts for 92% of the MMP-mediated, PMN surface

19 studies support a causal connection between MMP-8 activity and the IL-6/IL-8 network, with an acute

20 he interleukins was no longer dependent upon MMP-8 activity.

21 transcripts in human chondrocytes or Mmp-3, Mmp-8, Adamts-4, Adamts-5, and Il-1 in mouse chondrocyte

22 e did not observe induction of MMP-1, MMP-3, MMP-8, ADAMTS-4, ADAMTS-5, and IL-1 transcripts in human

23 topical administration of active recombinant MMP-8 also accelerated diabetic wound healing as a conse

24 A neutrophil collagenase 2 (active MMP-8 [aMMP-8]) oral fluid immunoassay has recently been

25 a small molecule) and the active recombinant MMP-8 (an enzyme) enhanced healing even more, in a strat

26 Thus, salivary MMP-8 analysis could give adjunctive information regardi

27 GCF MMP-8 analysis with defined cutoff levels could be used

28 us keratitis models and suggesting roles for MMP-8 and -13.

29 egulated by IL-1 beta and TNF-alpha, whereas MMP-8 and -14 and tissue inhibitor of metalloproteinase

30 wever, expression of several MMPs, including MMP-8 and -15, was significantly elevated, suggesting in

31 binations of salivary biomarkers (especially MMP-8 and -9 and osteoprotegerin) combined with red-comp

32 MP-1 is the PMN receptor for pro- and active MMP-8 and -9 as shown by the following: 1) TIMP-1 is str

33 CONCLUSION(S): GCF concentrations of MMP-8 and -9 at early of pregnancy are increased in wome

34 ormed, and GCF samples were obtained for the MMP-8 and -9 determination by Multiplex Elisa Assays.

35 MMP-8 and -9 expression was mediated by native mesenchym

36 loped GDM showed increased concentrations of MMP-8 and -9 in GCF since the beginning of pregnancy (P

37 An increase in the concentration of MMP-8 and -9 in women with periodontitis stage III and I

38 In a comparison of ruptured AAA biopsies, MMP-8 and -9 levels were significantly elevated in the 1

39 ng: 1) TIMP-1 is strikingly colocalized with MMP-8 and -9 on activated human PMN surfaces and in PMN

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

41 ood outcome recipients, levels of TIMP-bound MMP-8 and -9 were higher in BOS.

42 8, TNF, MCP-1, MIP-1alpha, IFN-gamma, LTB-4, MMP-8 and -9, and IL-1Ra with more than 60% (p < 0.05 fo

43 A localized increase in MMP-8 and -9, mediated by native mesenchymal cells, pres

44 cluded an early and robust rise in MMP-9 and MMP-8 and a uniform fall in TIMP-4.

45 ide tests of MMP activity, in particular for MMP-8 and bone collagen fragments, show strong potential

46 Low MMP-8 and high TIMP-1 levels may indicate the role of th

47 negatively correlated with concentrations of MMP-8 and IL-1beta.

48 ay for the high-throughput quantification of MMP-8 and IL-8 and -1beta in GCF.

49 sequence yielded significant stimulation of MMP-8 and lower levels of modulation of MMP-1, -2, -13,

50 es MMP-2 and MMP-9, and for the collagenases MMP-8 and MMP-13, as well as TIMP-1 profiles were examin

51 nases with collagenolytic activity by MMP-1, MMP-8 and MMP-13, collectively known as the collagenases

52 f specific metallocollagenases, particularly MMP-8 and MMP-13, where MMP-13 was the key collagenase.

53 MMP-9 and low to middle micromolar range for MMP-8 and MMP-13.

54 The PMN receptor(s) to which MMP-8 and MMP-9 bind(s) is not known.

55 XLOC_006277 knockdown suppressed MMP-8 and MMP-9 expression, both associated with heart l

56 To determine the roles of MMP-8 and MMP-9 in a neutrophil-dependent inflammatory r

57 rophils contribute to the production of both MMP-8 and MMP-9 in LPS-injected corneas and that MMP-8 r

58 ulates colocalized expression of TIMP-1 with MMP-8 and MMP-9 on peripheral blood PMN surfaces.

59 Competitive binding experiments showed that Mmp-8 and Mmp-9 share binding sites on murine PMN surfac

60 By anchoring MMP-8 and MMP-9 to PMN surfaces, membrane-bound TIMP-1 p

61 Elevated concentrations of GCF MMP-8 and MMP-9 were found in Gg compared with Gh group

62 and P=.002, respectively), whereas levels of MMP-8 and MMP-9 were higher in antibiotic-resistant pati

63 e forms of matrix metalloproteinases (MMPs), MMP-8 and MMP-9, in the wounds of db/db mice.

64 Because MMP-8 and MPO are produced by inflammatory cells, partic

65 roups, MMP-9 levels correlated strongly with MMP-8 and MPO levels, and MMP-8 correlated with MPO, but

66 olyzes type II collagen efficiently, whereas MMP-8 and MT1-MMP are similar in their preference for ty

67 eneral, MMP-13 was found to be distinct from MMP-8 and MT1-MMP(Delta279-523), in that enhanced substr

68 collagen specificity of MMP-13 compared with MMP-8 and MT1-MMP, in that MMP-13 hydrolyzes type II col

69 residues enhanced k(cat)/K(m) and k(cat) for MMP-8 and MT1-MMP.

70 , the COOH-terminal hemopexin domains of pro-Mmp-8 and pro-Mmp-9 are required for their binding to me

71 oluble hemopexin inhibits the binding of pro-Mmp-8 and pro-Mmp-9 to Mmp-8(-/-)x Mmp-9(-/-) murine PMN

72 s reconstitutes the binding of exogenous pro-Mmp-8 and pro-Mmp-9 to the surface of Timp-1(-/-) PMNs.

73 Unlike full-length pro-Mmp-8 and pro-Mmp-9, mutant pro-Mmp proteins lacking the

74 100A12-S100A8 locus affects serum and plasma MMP-8 and shows a suggestive association with the risk o

75 Elevated salivary MMP-8 and T. denticola biofilm levels displayed robust c

76 dontitis (GAgP) and to assess the effects of MMP-8 and TIMP-1 genotypes on the outcomes of non-surgic

77 Whereas bleomycin-treated Mmp-8(-/-) and WT mice have similar lung levels of sever

78 in coding genes, matrix metalloproteinase-8 (MMP-8) and transcription factor T-Box 3 (TBX3) by qRT-PC

79 librium was seen in all of the MMP-1, MMP-3, MMP-8, and MMP-12 SNPs and in four of five MMP-9 polymor

80 ce the expression of the collagenases MMP-1, MMP-8, and MMP-13 as well as MMP-3, an activator of proM

81 , progranulin, interleukin (IL)-1beta, IL-8, MMP-8, and MMP-13 levels were measured using enzyme-link

82 ated substrate hydrolysis and spared ADAM10, MMP-8, and MMP-14.

83 arameters and whole salivary IL-1beta, IL-6, MMP-8, and MMP-9 levels among habitual gutka chewers and

84 re worse, and whole salivary IL-6, IL-1beta, MMP-8, and MMP-9 levels were higher among gutka chewers

85 Levels of IL-6, IL-1beta, MMP-8, and MMP-9 were measured in UWS using an enzyme-li

86 MMP-13, MMP-8, and MT1-MMP increased by >300% in the transition

87 parameters correlated positively with CSF-1, MMP-8, and with the CSF-1/IL-34 ratio, and negatively wi

88 though concentrations of IL-1beta, IL-6, and MMP-8 approached healthy levels, whereas MIP-1alpha and

89 nly approximately 15-20% of their content of MMP-8 ( approximately 60 ng/10(6) cells) exclusively as

90 Elevated serum and plasma concentrations of MMP-8 are associated with the risk for and outcome of ca

91 Serum levels of calprotectin and MMP-8 are elevated in patients with AgP.

92 Elevated salivary MMP-8 associated significantly with more severe oral/per

93 Moreover, we studied whether MMP-8-associated variants are linked to increased risk o

94 e activity is attributable to membrane-bound MMP-8 because: 1) MMP-8 is expressed in an inducible man

95 Studies of bleomycin-treated Mmp-8 bone marrow chimeric mice show that both leukocyte

96 nd -13, and SDD reduced the odds of elevated MMP-8 by 60% compared to placebo (P=0.006).

97 However, sustained expression of WT MMP-8 by breast cancer cells was non-permissive for long

98 om 118 predialysis patients were assayed for MMP-8 by immunofluorometric assay.

99 Plasma MMP-9 increased by over 400% and MMP-8 by over 100% from baseline values by 12 h post-MI

100 rored at the mRNA level and was dependent on MMP-8 catalytic activity.

101 -13Ralpha2 transcript in humans through MMPs/MMP-8 cleavage of memIL-13Ralpha2, supporting a limited

102 Soluble MMP-8 cleaved and inactivated MIP-1alpha in vitro, but m

103 MMP-8 concentration in GCF was associated with GDM (RR:

104 plement system strongly contributes to serum MMP-8 concentration.

105 al pocket, associated with elevated salivary MMP-8 concentrations (P < 0.05 in all associations).

106 GCF and serum MMP-8 concentrations, serum MMP-9 concentrations, and se

107 ermines a significant portion of circulating MMP-8 concentrations.

108 ted to be potentially regulated by ET-1, and MMP-8, considered as neutrophil collagenase, as well as

109 m the PMNs in relation to the total cellular MMP-8 content.

110 ated strongly with MMP-8 and MPO levels, and MMP-8 correlated with MPO, but it did not reach signific

111 Most optimal MMP-8 cutoff levels were searched with receiver operatin

112 Thus, during bleomycin-mediated lung injury, MMP-8 dampens the lung acute inflammatory response, but

113 When C57BL/6 wild-type (n=15) and MMP-8-deficient mice (n=17) were subjected to elastase p

114 parenchymal cells are sources of profibrotic MMP-8 during bleomycin-mediated lung fibrosis.

115 Increases in GCF IL-1beta and MMP-8 during the first year of periodontal maintenance w

116 odulate both local and circulating levels of MMP-8 especially when associated with gingivitis.

117 TIMP-resistant, active MMP-8 expressed on the surface of activated PMN is likel

118 irus around the injection site in MMP-1- and MMP-8-expressing tumors.

119 MMP-8 expression is increased in leukocytes in the lungs

120 e (WT) versus Mmp-8(-/-) mice and quantified MMP-8 expression, and inflammation and fibrosis in the l

121 Neutrophil collagenase (MMP-8) expression was detected only in the 14-day contro

122 e62 in factor H) led to decreased release of MMP-8 from neutrophils compared with the major allele (V

123 Thus, MMP-8 has an unexpected, anti-inflammatory role during a

124 Thus, MMP-8 has novel roles in restraining lung inflammation a

125 rface promotes its stability because soluble MMP-8 has t(1/2) = 7.5 h at 37 degrees C, but membrane-b

126 formation in vivo, suggesting that wild-type MMP-8 has the ability to inhibit melanoma progression.

127 Levels of MMP-8 have indicated high values in PER21 compared with

128 lytically inactive (E198A) mutant version of MMP-8 in human breast cancer cell lines.

129 ng a specific ribozyme and overexpression of MMP-8 in M-4A4 cells by retroviral transduction both str

130 similar post-treatment decreases in salivary MMP-8 in periodontitis.

131 We show that overexpression of MMP-1 and MMP-8 in the human soft tissue sarcoma HSTS26T leads to

132 ted the apparently paradoxical expression of MMP-8 in these cell lines.

133 cells, and mononuclear phagocytes, expressed MMP-8 in vitro upon stimulation with proinflammatory cyt

134 Activated murine lung fibroblasts express Mmp-8 in vitro.

135 mine the role of matrix metalloproteinase-8 (MMP-8) in acute lung injury (ALI), we delivered LPS or b

136 ase 2 (PAD2) and matrix metalloproteinase-8 (MMP-8) in gingival crevicular fluid (GCF) in patients wi

137 -cleaving enzyme matrix metalloproteinase-8 (MMP-8) in saliva from healthy and periodontally diseased

138 In vivo, administration of an MMP-8 inhibitor attenuated early systolic dysfunction in

139 IL-6/IL-8 network, with an acute response to MMP-8 involving induction of the proinflammatory mediato

140 ibutable to membrane-bound MMP-8 because: 1) MMP-8 is expressed in an inducible manner in both pro- a

141 The origin of circulating MMP-8 is not completely clear.

142 Because MMP-8 is one of the most important biomarkers for period

143 Matrix metalloproteinase-8 (MMP-8) is a potent interstitial collagenase thought to b

144 Matrix metalloproteinase 8 (MMP-8) is a proinflammatory enzyme expressed mainly by n

145 Matrix metalloproteinase 8 (MMP-8) is a tumor-suppressive protease that cleaves nume

146 no study has yet evaluated the expression of MMP-8, known as "neutrophil collagenase," the enzyme tha

147 Decreased GCF MMP-8 levels and increased TIMP-1 levels were found to b

148 Serum MMP-8 levels and salivary TIMP-1 levels were higher in G

149 MMP-8 levels are also increased in saliva from patients

150 Salivary IL-6 and MMP-8 levels are elevated in patients with CP with and w

151 roups exhibited significant reduction in GCF MMP-8 levels at the post-treatment visit and at 2 weeks

152 seline GCF MMP-8 levels strongly predict how MMP-8 levels behave during the maintenance period.

153 mbers of missing teeth, or salivary IL-6 and MMP-8 levels between patients in groups 1 and 2.

154 After treatment CSF-1 and MMP-8 levels decreased together with observed clinical i

155 GCF MMP-8 levels decreased until 3 months after non-surgical

156 MMP-8 levels exceeding the optimal cutoff levels separat

157 med a genome-wide association study of serum MMP-8 levels in 2 populations comprising altogether 6049

158 is (CP) and test the utility of baseline GCF MMP-8 levels in predicting categorically assessed treatm

159 ith periodontitis displayed higher CSF-1 and MMP-8 levels in saliva compared with healthy patients, a

160 In smoker sites, high baseline MMP-8 levels indicate weak treatment response.

161 iodontitis (GAgP) to test the utility of GCF MMP-8 levels predicting the site-level treatment outcome

162 In smoker sites, baseline MMP-8 levels significantly predicted the categorical tre

163 Baseline GCF MMP-8 levels strongly predict how MMP-8 levels behave du

164 The ability of baseline MMP-8 levels to predict categorical treatment outcomes w

165 reupon changes in salivary CSF-1, IL-34, and MMP-8 levels were determined and related to periodontal

166 SEMA4D, PAD2, and MMP-8 levels were determined by enzyme-linked immunosorb

167 GCF MMP-8 levels were determined by immunofluorescence assay

168 GCF MMP-8 levels were measured with an immunofluorometric as

169 t 3 months, visfatin, progranulin, IL-8, and MMP-8 levels were significantly decreased compared with

170 d TIMP-1 and BMP-2 expressions and decreased MMP-8 levels.

171 lar fluid (GCF) matrix metalloproteinases-8 (MMP-8) levels over 6 months in patients with severe gene

172 [GSH/GSSG]), and matrix metalloproteinase-8 (MMP-8) levels; and histopathological evaluation of perio

173 luding fibrosis and platelet markers such as MMP-8 (matrix metalloproteinase-8) and TIMP-1 (tissue in

174 These data suggest that the active form of MMP-8 may be partly responsible for degradation of the c

175 rapeutic strategies to reduce lung levels of MMP-8 may limit fibroproliferative responses to injury i

176 cally deleting either Ip-10 or Mip-1alpha in Mmp-8(-/-) mice abrogates their lung inflammatory respon

177 intratracheal route to wild-type (WT) versus Mmp-8(-/-) mice and quantified MMP-8 expression, and inf

178 lveolar lavage fluid (BALF) from LPS-treated MMP-8(-/-) mice had more MIP-1alpha than BALF from LPS-t

179 monstrate that 24 h after intratracheal LPS, MMP-8(-/-) mice have 2-fold greater accumulation of PMN

180 bleomycin-treated WT mice, bleomycin-treated Mmp-8(-/-) mice have greater lung inflammation, but redu

181 iators (TGF-beta, IL-13, JE, and IFN-gamma), Mmp-8(-/-) mice have higher lung levels of IFN-gamma-ind

182 Genetically deleting MIP-1alpha in MMP-8(-/-) mice reduced the increased lung inflammation

183 S or bleomycin by the intratracheal route to MMP-8(-/-) mice versus wild-type (WT) mice or subjected

184 MMP-8(-/-) mice with ALI had greater increases in lung p

185 ung inflammation and injury and mortality in MMP-8(-/-) mice with ALI.

186 The THPI targeting MMP-8 minimized lung damage, increased production of the

187 an be cleaved by matrix metalloproteinase 8 (MMP-8), minocycline hydrochloride, bovine serum albumin,

188 vated PMN from mice genetically deficient in MMP-8 (MMP-8(-/-)) vs wild-type (WT) mice show that memb

189 rotein levels of matrix metalloproteinase 8 (MMP-8), MMP-9, and MMP-13 were elevated in the cartilage

190 Novel targets, including MMP-8, MMP-10, MMP-14, MMP-19, MMP-25 and MMP-28, are al

191 S4 and the collagen-degrading enzymes MMP-1, MMP-8, MMP-13, and MMP-14, although differences in the m

192 te substrate selectivity among MMP-1, MMP-2, MMP-8, MMP-13, and MMP-14/membrane-type 1 (MT1)-MMP.

193 ters represented the collagen preferences of MMP-8, MMP-13, and MT1-MMP well.

194 ype I collagenolytic MMPs, including MMP-13, MMP-8, MMP-2, MMP-9, or MT1-MMP, we identify the membran

195 oring single deficiencies for either MMP-13, MMP-8, MMP-2, or MMP-9 to continue to degrade collagen c

196 idative stress (MDA and OSI), and proteases (MMP-8, MMP-9, and CtD) that was significantly higher in

197 lymorphism in MMP genes MMP-1, MMP-2, MMP-3, MMP-8, MMP-9, and MMP-12 with bladder cancer risk in 560

198 xcellent MMP inhibition potencies for MMP-2, MMP-8, MMP-9, and MMP-13 (IC(50) = 0.006-107 nM).

199 NE, MMP-8, MMP-9, and MPO levels were elevated in oGVHD tear

200 MMP-8, MMP-9, and MPO levels were elevated significantly

201 tears that correlated strongly with elevated MMP-8, MMP-9, and MPO suggests a common neutrophilic sou

202 rrelation studies were performed between NE, MMP-8, MMP-9, and MPO within study groups.

203 sive CP group had significantly higher serum MMP-8, MMP-9, and NE levels than the healthy control gro

204 IL)-1beta, matrix metalloproteinase (MMP)-3, MMP-8, MMP-9, and neutrophil gelatinase-associated lipoc

205 elevated baseline levels of IL-1beta, MMP-3, MMP-8, MMP-9, and NGAL compared with the other study gro

206 MMP-8, MMP-9, and TIMP-1 levels were determined in gingi

207 a, matrix metalloproteinases (MMP)-1, MMP-3, MMP-8, MMP-9, from baseline to week 2; regulated on acti

208 orrelations were noted between MMP-2, MMP-3, MMP-8, MMP-9, MMP-12, and MMP-13 levels and percentage o

209 MMP-1, MMP-8, MMP-9, MMP-12, and MMP-13 levels were reduced sig

210 id meter, and levels of MMP-1, MMP-2, MMP-3, MMP-8, MMP-9, MMP-12, and MMP-13 were assessed using flu

211 analyzed for levels of MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-12, MPO, and TIMP-1 using multianalyte

212 69-783, which is hydrolyzed by MMP-1, MMP-2, MMP-8, MMP-9, MMP-13, and MT1-MMP.

213 ngiogenesis-related factors (CD26, FGF, HGF, MMP-8, MMP-9, OPN, PF4, SDF-1) and cytokines (IL-1ra, IL

214 Saliva MMP-8, MMP-9, TIMP-1, and MPO concentrations distinguish

215 Serum MMP-8, MMP-9, TIMP-1, MPO, and NE levels in circulation

216 tions, serum MMP-9 concentrations, and serum MMP-8/MMP-1 and MMP-9/MMP-1 molar ratios were significan

217 3, and 13 was induced early, whereas that of MMP-8 mRNA occurred late.

218 Neither MMP-8 nor -13 expression was affected by mechanical trau

219 In addition, membrane-bound MMP-8 on activated lung PMNs is likely to be the key bio

220 ated MIP-1alpha in vitro, but membrane-bound MMP-8 on activated PMNs had greater MIP-1alpha-degrading

221 to compensate for the deleterious effects of MMP-8 on breast cancer cell growth.

222 We found no effects of MMP-8 on LPS-induced CXC chemokine (LIX, or CXCL5)-induc

223 genase activity; and 3) human membrane-bound MMP-8 on PMN cleaves types I and II collagens, and alpha

224 traps; 2) minimal immunoreactive and active Mmp-8 or Mmp-9 are detected on the surface of activated

225 phil infiltration and did not express either MMP-8 or MMP-9; ii) neutrophil migration through the cen

226 tal amount of SEMA4D and GCF total amount of MMP-8 (P < 0.05).

227 salivary IL-6 (P <0.01), IL-1beta (P <0.01), MMP-8 (P <0.01), and MMP-9 (P <0.01) concentrations.

228 creased the genic expression of IL-1beta and MMP-8 (P <0.05), increased the mRNA expression of IL-6 (

229 s other MMPs and TIMPs showed no difference (MMP-8, P<0.001; MMP-9, P=0.01).

230 ular fluid (GCF) matrix metalloproteinase-8 (MMP-8) patterns in smokers and non-smokers with chronic

231 in levels by Western blotting (P=0.017), and MMP-8-positive neutrophils were seen almost exclusively

232 MMP-2 over time, but no significant MMP-3 or MMP-8 production was observed.

233 calization studies confirmed the presence of MMP-8 protein and mRNA within the plaque, which colocali

234 y in the 14-day control mice, with increased MMP-8 protein levels by Western blotting (P=0.017), and

235 tly blocked ultraviolet-induced increases in MMP-8 protein levels, and neutrophil infiltration.

236 Increased full-length MMP-8 protein was associated with infiltration into the

237 trate that ultraviolet irradiation increases MMP-8 protein, which exists predominantly in a latent fo

238 In particular, MMP-8 proteolytically activates IL-8 and, thereby, regul

239 mong visfatin and IL-8 (r = 0.909, P <0.01), MMP-8 (r = 0.702, P = 0.02), and MMP-13 (r = 0.781, P =

240 01); chemerin and IL-8 (r = 0.913, P <0.01), MMP-8 (r = 0.770, P <0.01), and MMP-13 (r = 0.788, P <0.

241 d progranulin and IL-8 (r = 0.762, P <0.01), MMP-8 (r = 0.845, P <0.01), and MMP-13 (r = 0.813, P <0.

242 To determine whether MMP-8 regulates lung inflammatory or fibrotic responses

243 8 and MMP-9 in LPS-injected corneas and that MMP-8 regulates neutrophil migration through the dense c

244 ted PMN is likely to be an important form of MMP-8, regulating lung inflammation and collagen turnove

245 thod was used to determine the percentage of MMP-8 released from the PMNs in relation to the total ce

246 GCF MMP-8 response patterns could be clustered into two diff

247 MMP-8 response patterns were explored by cluster analysi

248 Different site-level MMP-8 response patterns were explored by the cluster ana

249 Distinct types of MMP-8 response patterns were found in both smokers and n

250 Degradation behavior and MMP-8-responsive drug release were performed by high-per

251 important biomarkers for periodontitis, the MMP-8-responsive hydrogel has potential to be used for i

252 orporated into the scaffolds to evaluate the MMP-8-responsive release behavior of the on-demand drug

253 = 7.5 h at 37 degrees C, but membrane-bound MMP-8 retains >80% of its activity after incubation at 3

254 CF-7, SK-BR-3, and MDA-MB-231) expressing WT MMP-8 revealed elevated levels of IL-6 and IL-8.

255 MMP-8 rose to > 120% at day 3 after MI (P < 0.05) and fe

256 MMP-8 secretion by PMNs in response to fMLP or serum-ops

257 Conversely, EMD did not induce MMP-8 secretion from PMNs.

258 MMP-8 secretion was analyzed by Western blotting.

259 chemotaxis, and matrix metalloproteinase-8 (MMP-8) secretion by PMN in vitro to better understand th

260 ken together, these results suggest that the MMP-8-sensitive hydrogel is a promising candidate for on

261 us 154+/-9.9%; P=0.603), which suggests that MMP-8 serves only as a marker for the presence of neutro

262 13 preferred the interrupted sequence, while MMP-8 showed little discrimination between non-interrupt

263 Mmp-8 steady state mRNA and protein levels increase in w

264 MMP-8 stimulation induces a proinflammatory phenotype in

265 ressing MMP (matrix metalloproteinase)-3 and MMP-8 synthesis and inducing TIMP (tissue inhibitor of m

266 s was serendipitously more effective against MMP-8 than MT1-MMP and was utilized successfully in a mo

267 red with Hg group (P <0.05) whereas salivary MMP-8/TIMP-1 molar ratio was lower in Gh compared with H

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

269 may be relevant to the recognized ability of MMP-8 to orchestrate the innate immune system in inflamm

270 Binding of MMP-8 to the PMN surface promotes its stability because

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

272 The GCF SEMA4D, PAD2, and MMP-8 total amounts were significantly reduced at first

273 GCF MMP-8 total amounts were similar in BP and NBP groups (P

274 The GCF SEMA4D, PAD2, and MMP-8 total amounts were similar in CP and G groups (P >

275 overed the presence of the metalloproteinase MMP-8, traditionally associated only with neutrophils, i

276 hydrolysis of a synthetic octapeptide), and MMP-8 (using a Western blot) and the bone-resorption mar

277 measure salivary matrix metalloproteinase-8 (MMP-8) using specific antibodies and surface acoustic wa

278 l) exerted slightly elevated median salivary MMP-8 values compared with the other CKD group or regard

279 Studies of MMP-8(-/-) vs WT mice given intratracheal LPS demonstrat

280 MN from mice genetically deficient in MMP-8 (MMP-8(-/-)) vs wild-type (WT) mice show that membrane-bo

281 In contrast with other MMPs, MMP-8 was epigenetically silenced in both cell types, th

282 The strongest association with serum MMP-8 was found in locus 1q31.3, containing the gene for

283 cells, expression of WT but not E198A mutant MMP-8 was lost, with IL-6 and IL-8 levels returning to b

284 In logistic regression model saliva, MMP-8 was mainly affected by pack years of smoking, wher

285 rom LPS-treated WT mice, but soluble, active MMP-8 was not detected in BALF samples.

286 MMP-8 was significantly elevated in the diseased sites o

287 In saliva, levels of MMP-8 were 5.66-fold higher in patients with AgP than in

288 High levels of membrane-bound MMP-8 were detected on lung PMNs from LPS-treated WT mic

289 l isolates of MDA-MB-231 cells expressing WT MMP-8 were generated, and these showed constitutively hi

290 IL-6 and MMP-8 were measured in UWS using enzyme-linked immunosor

291 Levels of calprotectin, CSF-1, MIF, MIG, and MMP-8 were measured using enzyme-linked immunosorbent as

292 ignificantly higher concentrations of active MMP-8 were observed in the plaques of symptomatic patien

293 Serum levels of MMP-8 were significantly elevated in patients with AgP c

294 sease, conventional measurements of salivary MMP-8 were used to validate the microfluidic assays desc

295 was a positive correlation between CSF-1 and MMP-8, which both correlated negatively to IL-34, in pat

296 roteinase (MMP) family of enzymes, MMP-1 and MMP-8, which can modulate the tumor matrix and enhance H

297 rite-dependent activation of the collagenase MMP-8, which is produced by neutrophils present at high

298 The predominant collagenase was MMP-8, which was likely neutrophil derived and M. tuberc

299 OH-terminal hemopexin domain fail to bind to Mmp-8(-/-)x Mmp-9(-/-) murine PMNs.

300 ts the binding of pro-Mmp-8 and pro-Mmp-9 to Mmp-8(-/-)x Mmp-9(-/-) murine PMNs.