ライフサイエンスコーパス: S100A4

1 to expression of a canonical EMT biomarker (S100A4).

2 homologue of the metastasis-promoting human S100A4.

3 even more extensive than, that reported for S100A4.

4 ers vimentin, alpha-smooth muscle actin, and S100A4.

5 sess myosin fragment filament disassembly by S100A4.

6 ression of the small calcium-binding protein S100A4.

7 is-inducing proteins osteopontin, S100P, and S100A4.

8 r residues in the hydrophobic pocket of Ca2+-S100A4.

9 he 1.7 A crystal structure of the human Ca2+-S100A4.

10 reports on the Ca2+-bound, activated form of S100A4.

11 the most robustly up-regulated (22-fold) was S100A4.

12 comparable effects on myosin-IIA assembly as S100A4.

13 its the same effects on cell polarization as S100A4.

14 xpressing Ki67 and the MPC markers SSEA4 and S100A4.

15 ) of RPE cells was assessed by expression of S100A4.

16 rker p21(WAF1/Cip) or the mesenchymal marker S100A4.

17 ic mediator S100 Calcium-binding protein A4 (S100A4) (1.78-fold, P<0.05).

18 eased expression of S100 calcium-binding A4 (S100A4), a protein linked to cancer cell proliferation a

19 ity, it significantly reduced SUMOylation of S100A4, a critical posttranslational modification that d

20 ssing cancer cells responded by upregulating S100A4, a marker of cancer-associated fibroblasts (CAFs)

21 Overexpression of S100A4, a member of the S100 family of Ca(2+)-binding pr

22 S100A4, a member of the S100 family of Ca(2+)-binding pr

23 S100A4, a member of the S100 family of Ca(2+)-binding pr

24 S100A4, a member of the S100 family of Ca(2+)-binding pr

25 S100A4, a member of the S100 family of Ca2+-binding prot

26 S100A4, a member of the S100 family of proteins, plays a

27 S100A4, a specific protein-binding partner for CD16A-CY

28 Biochemical assays revealed that S100A4 activates Src and focal adhesion kinase (FAK) sig

29 a activation of JAK/STAT signaling, and then S100A4 acts in an autocrine manner to stimulate MMP-13 p

30 To examine how the biochemical properties of S100A4 affect cell motility, we determined the effect of

31 h levels of the S100 calcium binding protein S100A4 also called fibroblast specific protein 1 (FSP1)

32 S100A4, also known as mts1, is a member of the S100 fami

33 BEC expression of S100A4 (an early fibroblast lineage marker established a

34 ased while expression of mesenchymal markers S100A4 and alpha-smooth muscle actin increased.

35 ost of these residues are not exposed in apo-S100A4 and explain the Ca2+ dependence of formation of t

36 Targeting S100A4 and GRM3 may help prevent bone metastasis.

37 art to the post-metastatic downregulation of S100A4 and GRM3.

38 han two other markers of cancer progression, S100A4 and MACC1, and clustering of all GEFs together im

39 d STAT-3, leading to increased production of S100A4 and MMP-13.

40 as examined by stimulating chondrocytes with S100A4 and monitoring for the activation of MAP kinases

41 for two other metastasis-inducing proteins, S100A4 and osteopontin.

42 BEC expression of S100A4 and pSmad 2/3 was seen as early as 24 days after

43 Interestingly, we found that S100A4 and Rhotekin can form a complex with active RhoA.

44 ence, we determined that suppression of both S100A4 and Rhotekin leads to loss of Rho-dependent membr

45 dingly, our data suggest that interaction of S100A4 and Rhotekin permits S100A4 to complex with RhoA

46 s and primary human glioma tissues show that S100A4 and S100A6 are expressed in a small subset of can

47 the expression of two genes from this list (S100a4 and S100a6) in primary mouse gliomas and human gl

48 Furthermore, coordinate expression of S100A4 and SAA in tumor samples from colorectal carcinom

49 eraction between the calcium-binding protein S100A4 and the C-terminal fragments of nonmuscle myosin

50 To establish a direct link between S100A4 and the regulation of myosin-IIA function, we pre

51 We have thus demonstrated that both S100A4 and UA act as DAMPs and, as such, may play a crit

52 Similar to necrotic tumor material, S100A4 and UA both dose-dependently induced chemotaxis o

53 With regard to MSC proliferation, both S100A4 and UA inhibited MSCs without altering survival o

54 re to determine whether chondrocytes produce S100A4 and whether S100A4 can stimulate the production o

55 es, such as S100 calcium-binding protein A4 (S100A4) and miR-181b, after SCF plus GM-CSF administrati

56 kn2d (cyclin-dependent kinase inhibitor 2D), s100a4, and IL10R alpha.

57 with growth or local invasion such as Ki67, S100A4, and MMP2, 9, and 13.

58 ariate regression analysis identifies S100P, S100A4, and osteopontin as the most significant independ

59 h mobility group box (HMGB)-1, B7 Homolog 1, S100A4, and resistin have been detected in tissues of de

60 rs for the metastasis-promoting functions of S100A4, and serve as a link between inflammation and tum

61 in, and the mesenchymal markers fibronectin, s100A4, and vimentin were evaluated.

62 Since both IL-7 and S100A4 are up-regulated in OA cartilage and can stimulat

63 he well-characterized myofibroblastic marker S100A4, are functionally relevant.

64 Overall, our findings highlight nuclear S100A4 as a candidate therapeutic target in cholangiocar

65 stemness and EMT in glioblastoma, suggesting S100A4 as a candidate therapeutic target.

66 Overall, our results establish S100A4 as a central node in a molecular network that con

67 owth in vitro and in vivo We also identified S100A4 as a critical regulator of GSC self-renewal in mo

68 Our studies point to S100A4 as a critical regulator of matrix degradation, wh

69 vide evidence that supports a novel role for S100A4 as a prosurvival factor in pancreatic cancer.

70 demonstrate a novel mechanism for sumoylated S100A4 as a regulator of expression of the MMP-13 gene.

71 These studies establish S100A4 as a regulator of physiological macrophage motili

72 In contrast with previous reports of S100A4 as a reporter of EMT, we discovered that S100A4 i

73 In cells, localized activation of S100A4 at the cell periphery is observed during random m

74 IIA function, we prepared an antibody to the S100A4 binding site on the myosin-IIA heavy chain that h

75 S100A4 binding to Rhotekin is calcium-dependent and uses

76 that the coiled-coil partially unwinds upon S100A4 binding.

77 Interestingly, we also find that S100A4 binds as strongly to a homologous heavy chain fra

78 This is the first study to demonstrate that S100A4 binds to RAGE and stimulates a RAGE-mediated sign

79 A pulldown assay showed that S100A4 binds to RAGE in chondrocytes.

80 The latter assay demonstrated that S100A4 binds to the filaments and actively promotes disa

81 Human S100A4 binds two Ca2+ ions with the typical EF-hand exhi

82 S100A4(-/-) BMMs form unstable protrusions, overassemble

83 the 2.3 A crystal structure of human Ca(2+)-S100A4 bound to TFP.

84 imide blocked the IL-7-mediated secretion of S100A4, but pretreatment with brefeldin A did not.

85 Downregulation of nuclear S100A4 by low-dose paclitaxel was associated with a stro

86 Suppression of S100A4 by small interference RNA resulted in a reduced c

87 required post-translational modification of S100A4 by the sumo-1 protein.

88 ther chondrocytes produce S100A4 and whether S100A4 can stimulate the production of matrix metallopro

89 Although the metastatic capabilities of S100A4(+) cancer cells have been examined, the functiona

90 Increased numbers of S100A4(+) cells are associated with poor prognosis in pa

91 S100A4(+) cells in gliomas are enriched with cancer cell

92 ttributable to local non-bone marrow-derived S100A4(+) cells, which are likely fibroblasts in this se

93 Knockdown of S100A4 clearly induced apoptosis with increased fragment

94 delling of these in vitro data suggests that S100A4 concentrations in the micromolar region could dis

95 F MPCs are intrinsically fibrogenic and that S100A4 confers MPCs with fibrogenicity.

96 We suggest that S100A4 could be used as a biomarker for CaP progression

97 g cancer cells showed a dramatic increase in S100A4, COX-2 and the alteration of 30 tumor-related gen

98 ls (Sharpin(cpdm)), and mice with a stromal (S100a4-Cre) deletion of Sharpin, have reduced mammary du

99 S100a4-Cre; EP4 (flox/flox) (EP4cKO(S100a4)) repairs hea

100 S100A4 to normal physiology, we established S100A4-deficient mice by gene targeting.

101 emarkably decreased in animals injected with S100A4-deficient pancreatic tumor cells.

102 , while cyclin E expression is decreased, in S100A4-deficient pancreatic tumors in vivo.

103 S100A4-deficient tumors have lower expression of vascula

104 Here we establish an S100A4-dependent link between inflammation and metastati

105 osis to a model of persistent fibrosis in an S100A4-dependent manner.

106 S100P, like S100A4, differentially interacts with the isoforms of no

107 ues of the coiled-coil are wrapped around an S100A4 dimer disrupting the ACD and resulting in filamen

108 sin chain is wrapped around the Ca(2+)-bound S100A4 dimer occupying both hydrophobic binding pockets.

109 n each pentamer most of the contacts between S100A4 dimers occurs through the TFP moieties.

110 S100A4 downregulation remarkably reduces cell migration

111 S100A4 downregulation results in significant cell growth

112 etic studies in a Drosophila model to define S100A4 effector functions that mediate metastatic dissem

113 sed metastatic dissemination associated with S100A4 elevation, defining required signaling pathway(s)

114 otility by affecting cell polarization, with S100A4 expressing cells displaying few side protrusions

115 Selective ablation of S100A4-expressing cells was sufficient to block tumor gr

116 S100A4 expression by BEC appears to occur before the dev

117 In the tumor mass, nuclear S100A4 expression by cholangiocarcinoma cells was signif

118 S100A4 expression correlated well with integrin alpha6be

119 s in the motility cycle that are affected by S100A4 expression have not been investigated.

120 S100A4 expression is associated with poor clinical outco

121 t cell motility, we determined the effect of S100A4 expression on protrusive behavior during chemoatt

122 Silencing of S100A4 expression using a stable siRNA vector (pSM2; Ope

123 regulated in vivo as in mouse kidney tissues S100A4 expression was many -fold greater in the papilla

124 e, mannitol, and choline chloride stimulated S100A4 expression, whereas urea did not.

125 ibodies, there was a significant decrease in S100A4 expression.

126 ctional importance of stromal Tenascin-C and S100A4(+) fibroblast-derived VEGF-A in metastasis was es

127 In particular, S100A4(+) fibroblast-derived VEGF-A plays an important r

128 Reduction in metastasis due to the loss of S100A4(+) fibroblasts correlated with a concomitant decr

129 study demonstrates a crucial role for local S100A4(+) fibroblasts in providing the permissive "soil"

130 CD24 were negative, whereas SNAI2, vimentin, S100A4, FN1, HRAS, transforming growth factor beta1, and

131 y integrin alpha6beta4 expression, including S100A4, FST, PDLIM4, CAPG, and Nkx2.2.

132 s demonstrate that significant inhibition of S100A4 function occurs only at TFP concentrations that p

133 ation of just Cys81 is sufficient to inhibit S100A4 function with respect to myosin-IIA binding and d

134 development of reagents that interfere with S100A4 function.

135 azines as inhibitors of myosin-II associated S100A4 function.

136 S100A4 gain of function was sufficient to confer fibroti

137 We evaluated the mechanism through which the S100A4 gene controls invasiveness of cells by using a ma

138 Our data demonstrate that the S100A4 gene controls the invasive potential of human CaP

139 We tested a hypothesis that the S100A4 gene plays a role in the invasiveness of human Ca

140 erved that siRNA-mediated suppression of the S100A4 gene significantly reduced the proliferative and

141 S100A4 has a direct role in metastatic progression, like

142 S100A4 has been shown to be increased in osteoarthritic

143 s that stained positively for both S100P and S100A4 have a significantly reduced survival of 1.1% ove

144 e) also enhanced the chemotactic activity of S100A4 in a synergistic manner.

145 binding studies and the crystal structure of S100A4 in complex with a 45-residue-long myosin heavy ch

146 To address the role of S100A4 in normal mammary gland, its spatial and temporal

147 GF-beta1, supporting a non-canonical role of S100A4 in pancreatic cancer.

148 alpha-smooth muscle actin and expression of S100A4 in proximal tubular epithelial cells.

149 tor-1, platelet-derived growth factor-b, and S100A4 in R-cells were downregulated by valproic acid an

150 hat TFP binds to the target binding cleft of S100A4 in solution.

151 ere we report the crystal structure of human S100A4 in the active calcium-bound state at 2.03 A resol

152 , defining required signaling pathway(s) for S100A4 in this setting.

153 The role of S100A4 in tumor progression was studied by using an orth

154 of a significant number of genes, including S100A4, in the myofibroblastic signature; however, DNA c

155 Stimulation of chondrocytes with S100A4 increased the phosphorylation of Pyk-2, MAP kinas

156 In 3D culture models, topical addition of S100A4 induced a significant increase in the TGFalpha me

157 king of sumoylation and nuclear transport of S100A4 inhibited the IL-1beta-induced production of MMP-

158 iscovered that metastasis-associated protein S100A4 interacts with the Rho-binding domain (RBD) of Rh

159 ar expression of the calcium-binding protein S100A4 is a biomarker of increased invasiveness in chola

160 hibitor blocked this effect, suggesting that S100A4 is a downstream effector of EGFR activation.

161 S100A4 is a member of the S100 family of calcium-binding

162 Here, we show that S100A4 is a novel biomarker of GSCs.

163 These observations suggest that S100A4 is an excellent target for therapeutic interventi

164 0A4 as a reporter of EMT, we discovered that S100A4 is an upstream regulator of the master EMT regula

165 Additionally, increased S100A4 is associated with only one of the tumors.

166 These findings provide evidence that S100A4 is developmentally regulated and that it plays a

167 The calcium-binding protein S100A4 is expressed at elevated levels in human cancers,

168 n addition to its expression in tumor cells, S100A4 is expressed in normal cells and tissues, includi

169 S100A4 is implicated in metastasis and chronic inflammat

170 s under sublethal osmotic stress, suggesting S100A4 is involved in the osmoadaptive response.

171 Numerous studies indicate that S100A4 is not simply a marker for metastatic disease, bu

172 Thus, S100A4 is one effector of the paracrine action of E2 in

173 We have previously shown that S100A4 is overexpressed in diseased cartilage and that e

174 tin immunoprecipitation, we demonstrate that S100A4 is regulated by NFAT5, thus identifying the first

175 As a DAMP, S100A4 is sensitive to oxidation whereas uric acid (UA)

176 oblast-specific protein 1 (FSP1, also called S100A4) is considered a marker of fibroblasts in differe

177 S100A4 knockdown also resulted in an increased sensitivi

178 uently showed that RNA interference-mediated S100A4 knockdown resulted in an elevated expression of B

179 The mechanism by which S100A4 leads to increased cancer aggressiveness has yet

180 of TMD cells, while Paclitaxel decreased the S100A4 level and reduced TMD's cellular motility.

181 f CD16A-CY by PKC in vitro, and reduction of S100A4 levels in vivo enhances receptor phosphorylation

182 is that deletion of the PGE2 receptor EP4 in S100a4-lineage cells would decrease adhesion formation.

183 the source of elevated elastase (NE) in the S100A4 lung, and NE mRNA and protein levels are greater

184 did not express alpha-smooth muscle actin or S100A4, markers of myofibroblasts and fibroblasts.

185 ractions provides a mechanism for inhibiting S100A4-mediated cellular activities and their associated

186 e S100A4/myosin-IIA interaction and inhibits S100A4-mediated depolymerization of myosin-IIA filaments

187 Assays examining the ability of TFP to block S100A4-mediated disassembly of myosin-IIA filaments demo

188 We suggest that S100A4-mediated effects during branching morphogenesis p

189 cal macrophage motility and demonstrate that S100A4 mediates macrophage recruitment and chemotaxis in

190 Here, we have examined whether S100A4 mediates MPC fibrogenicity.

191 and quantitative PCR also revealed increased S100A4 message in IMCD3 cells adapted to hypertonicity.

192 S100A4 (metastasin) is a member of the S100 family of ca

193 d in cell motility and metastasis, including S100A4/metastasin.

194 bing the cellular dynamics controlled by the S100A4 metastasis factor.

195 intimal lesions and elastin fragmentation in S100A4 mice 6 months after viral infection.

196 greater in PA smooth muscle cells (SMC) from S100A4 mice than from C57 mice.

197 increase in lung elastase activity occurs in S100A4 mice, 7 days after M1-MHV-68, unrelated to inflam

198 Homozygous S100A4(-/-) mice are fertile, grow normally and exhibit

199 bone marrow macrophages (BMMs) derived from S100A4(-/-) mice display defects in chemotactic motility

200 ed that bone marrow-derived macrophages from S100A4(-/-) mice exhibit defects in directional motility

201 Our studies show that S100A4 modulates cellular motility by affecting cell pol

202 Two sumoylation sites were identified on the S100A4 molecule, Lys(22) and Lys(96).

203 Exogenous EGF increased S100A4 mRNA levels in 231BR-EGFP cells (1.40+/-0.02-fold

204 METHODS AND Both S100A4/Mts1 (500 ng/mL) and BMP-2 (10 ng/mL) induce migr

205 ced CLIC4 expression does not interfere with S100A4/Mts1 internalization or its interaction with myos

206 lecule necessary for motility in response to S100A4/Mts1 or BMP-2.

207 es demonstrate how a single ligand (BMP-2 or S100A4/Mts1) can recruit multiple cell surface receptors

208 We hypothesized that S100A4/Mts1-mediated hPASMC motility might be enhanced b

209 identified as an inhibitor that disrupts the S100A4/myosin-IIA interaction and inhibits S100A4-mediat

210 hibition in which phenothiazines disrupt the S100A4/myosin-IIA interaction by sequestering S100A4 via

211 identified as an inhibitor that disrupts the S100A4/myosin-IIA interaction.

212 The structure of the S100A4-NMIIA complex reveals a unique mode of interactio

213 Here, we investigate the mechanism of S100A4-NMIIA interaction based on binding studies and th

214 gn of specific drugs that interfere with the S100A4-NMIIA interaction.

215 he Ca(2+)-dependent binding of myosin-IIA to S100A4, NSC 95397 was identified as an inhibitor that di

216 is study, we provide evidence that targeting S100A4 nuclear import by low-dose paclitaxel, a microtub

217 curs only at TFP concentrations that promote S100A4 oligomerization.

218 ed the effect of silencing the expression of S100A4 on the induction of apoptosis, cell cycle arrest,

219 In the presence of S100A4 or UA, MSCs gained an immunosuppressive capabilit

220 s in which the staining profile for the MIPs S100A4, osteopontin, anterior gradient-2, and S100P has

221 pulmonary artery (PA) neointimal lesions in S100A4-overexpressing, but not in wild-type (C57), mice.

222 sting that, in addition to hypermethylation, S100A4 overexpression may represent an alternative mecha

223 These findings support that S100A4 plays an important role in pancreatic cancer prog

224 The Ca(2+)-S100A4/prochlorperazine (PCP) complex exhibits a similar

225 We now show that the loss of S100A4 produces two mechanistically distinct phenotypes

226 ressing Cre recombinase under control of the S100A4 promoter crossed with mice carrying VEGF-A allele

227 viral thymidine kinase under control of the S100A4 promoter to specifically ablate S100A4(+) stromal

228 Our studies show for the first time that S100A4 promotes directional motility via a direct intera

229 in pancreatic cancer progression in vivo and S100A4 promotes tumorigenic phenotypes of pancreatic can

230 S100A4 protein expression was further confirmed by immun

231 Intravenously injected S100A4 protein induced expression of SAA proteins and cy

232 e three-dimensional structure of the dimeric S100A4 protein upon calcium binding.

233 The structure of the active form of S100A4 provides insight into its interactions with its b

234 s, which, along with annexin-binding protein S100A4, regulated fusogenic activity of syncytin 1.

235 ved in EP4cKO(S100a4) suggesting that EP4cKO(S100a4) repairs heal with increased infiltration of EP4

236 S100a4-Cre; EP4 (flox/flox) (EP4cKO(S100a4)) repairs healed with improved gliding function a

237 Interestingly, EP4cKO(S100a4) resulted in only transient deletion of EP4, sugg

238 of a novel solvatochromatic reporter dye to S100A4 results in a sensor that, upon activation, underg

239 no overt abnormalities; however, the loss of S100A4 results in impaired recruitment of macrophages to

240 We found that S100A1, S100A2, S100A4, S100A6 and S100B proteins bound different p63 an

241 biophysically the binding of S100A1, S100A2, S100A4, S100A6 and S100B to homologous domains of p63 an

242 Here, we found that S100A1, S100A2, S100A4, S100A6, and S100B bound to two subdomains of the

243 Real-time PCR confirmed that STMN3, S100A4, S100A6, c-Myb, estrogen receptor alpha, growth h

244 ls of genes associated with metastasis NPTN, S100A4, S100A9, and with epithelial mesenchymal transiti

245 taining for the metastasis-inducing proteins S100A4, S100P, osteopontin, and AGR2 (P < or = 0.002).

246 f this study was to examine the mechanism of S100A4 secretion by chondrocytes.

247 00 family proteins, of which two, S100A2 and S100A4, showed in vitro the ability to repress exogenous

248 Short hairpin RNA-mediated S100A4 silencing in 231BR-EGFP cells decreased their mig

249 S100A4-siRNA-transfected cells exhibited a reduced rate

250 nscriptional activation of the MMP-9 gene in S100A4-siRNA-transfected cells.

251 immunoprecipitation assays demonstrated that S100A4 specifically and directly binds to Rhotekin RBD,

252 in diseased cartilage and that extracellular S100A4 stimulates MMP-13 production, a major type II col

253 n studies demonstrated that these effects of S100A4(+) stromal cells are attributable to local non-bo

254 s have been examined, the functional role of S100A4(+) stromal cells in metastasis is largely unknown

255 To study the contribution of S100A4(+) stromal cells in metastasis, we used transgeni

256 Depletion of S100A4(+) stromal cells significantly reduced metastatic

257 f the S100A4 promoter to specifically ablate S100A4(+) stromal cells.

258 The Ca(2+)-bound S100A4 structure reveals a large conformational change i

259 ouble-positive cells were observed in EP4cKO(S100a4) suggesting that EP4cKO(S100a4) repairs heal with

260 Partial silencing of S100A4 suppressed migratory capabilities of TMD cells, w

261 ies provide the foundation for understanding S100A4 target recognition and may support the developmen

262 entification of small molecules that disrupt S100A4/target interactions provides a mechanism for inhi

263 EP4 and impaired gliding function in EP4cKO(S100a4) tendon repairs.

264 nding results in the assembly of five Ca(2+)-S100A4/TFP dimers into a tightly packed pentameric ring.

265 e cooperative formation of a similarly sized S100A4/TFP oligomer in solution.

266 We developed a fluorescent biosensor (Mero-S100A4) that reports on the Ca2+-bound, activated form o

267 n flies overexpressing mutant Ras(Val12) and S100A4, there was a significant increase in activation o

268 S100A4, thus, provides a connection between the actomyos

269 ese lysine residues abolished the ability of S100A4 to be sumoylated and to translocate into the nucl

270 endent conformational change is required for S100A4 to bind peptide sequences derived from the C-term

271 Calcium-activated binding of S100A4 to CD16A, promoted by the initial calcium flux, a

272 t interaction of S100A4 and Rhotekin permits S100A4 to complex with RhoA and switch Rho function from

273 atory mechanism for mediating the binding of S100A4 to myosin-IIA.

274 To examine the contribution of S100A4 to normal physiology, we established S100A4-defic

275 of evolutionarily conserved pathways used by S100A4 to promote metastatic dissemination, with potenti

276 lanine significantly impaired the ability of S100A4 to promote myosin-IIA filament disassembly.

277 ng domain (RBD) of Rhotekin, thus connecting S100A4 to the Rho pathway.

278 lar chondrocytes, we show that intracellular S100A4 translocated into the nucleus upon interleukin-1b

279 angiocarcinoma cell lines expressing nuclear S100A4 triggered a marked reduction in nuclear expressio

280 The expression of S100a6 and S100a4, two highly upregulated genes, is closely correla

281 Downregulation of S100A4 using shRNA significantly reduced TGFalpha induce

282 documented the heightened susceptibility of S100A4 versus C57 PA elastin to degradation by elastase.

283 IL-7 stimulates chondrocyte secretion of S100A4 via activation of JAK/STAT signaling, and then S1

284 100A4/myosin-IIA interaction by sequestering S100A4 via small molecule-induced oligomerization.

285 A) 1 and SAA3 are transcriptional targets of S100A4 via Toll-like receptor 4 (TLR4)/nuclear factor-ka

286 lization of YFP with the mesenchymal markers S100A4, vimentin, alpha-SMA, or procollagen 1alpha2, alt

287 S100A4, vimentin, and pSmad 2/3 expression in early recu

288 Marked positive immunostaining for S100A4 was also noted in sections of human cartilage wit

289 Increased expression of S100A4 was also observed in the medulla and papilla, but

290 Nuclear S100A4 was bound to the promoter region of MMP-13 in IL-

291 Secretion of S100A4 was measured in conditioned media by immunoblotti

292 Chondrocyte secretion of S100A4 was observed after treatment with IL-6 or IL-8 bu

293 t analysis, S100 calcium-binding protein A4 (S100A4) was aligned to a principal axis associated with

294 The effects of loss or gain of S100A4 were examined in pancreatic cancer cell lines.

295 MMP13 correlated more closely with levels of S100A4, whereas MMP9 levels correlated more closely with

296 hat IPF MPCs had increased levels of nuclear S100A4, which interacts with L-isoaspartyl methyltransfe

297 clude that Ca(2+) binds to the EF2 domain of S100A4 with micromolar affinity and that the K(d) value

298 hydrophobic target binding pocket of Ca(2+)-S100A4 with no significant conformational changes observ

299 To examine the interaction of S100A4 with TFP, we determined the 2.3 A crystal structu

300 a marked reduction in nuclear expression of S100A4 without modifying its cytoplasmic levels, an effe