ライフサイエンスコーパス: JAM

1 JAM-A also is expressed on the surface of circulating he

2 JAM-A dimerization on a common cell surface (in cis) has

3 JAM-A is reported to contain N-glycans, but the extent o

4 JAM-A is required for establishment of viremia and viral

5 JAM-A is robustly expressed in normal human mammary epit

6 JAM-A localizes to tight junctions and contributes to pa

7 JAM-A or CD9 knockdown impairs endothelial cell migratio

8 JAM-A recruits Csk to the integrin-c-Src complex, where

9 JAM-A redistribution was associated with internalization

10 JAM-A serves many roles and contributes to barrier funct

11 JAM-A-deficient mice and cultured epithelial cells demon

12 JAM-A-deficient platelets showed increased aggregation a

13 JAM-C expressed on both murine B16 melanoma cells as wel

14 JAM-C expression was identified in human and murine mela

15 JAM-C has been implicated in leukocyte transendothelial

16 JAM-C inhibition significantly decreased the chemokine-i

17 JAM-C knockdown caused a delay in the hfRPE cell polariz

18 JAM-C localized at the tight junctions of cultured hfRPE

19 JAM-C localizes specifically in the tight junctions of h

20 JAM-C was also expressed on the surface of OA ST and RA

21 JAM-C was highly expressed by RA ST lining cells, and it

22 JAM-C(-/-) mice as well as endothelial-specific JAM-C-de

23 EC junctional adhesion molecule-1 (JAM-1), an alternative ligand for LFA-1, contributes exc

24 d in the HT-lo/diss variant, whereas NCAM-1, JAM-C, and TF levels were increased in the HT-hi/diss va

25 ndidates, four targets (i.e. TIMP-2, NCAM-1, JAM-C, and tissue factor (TF)) were selected for further

26 on the basal expression of TJ proteins ZO-1, JAM-2, Occludin, Claudin-3 and Claudin-5, using in vitro

27 ing in vivo differences in levels of TIMP-2, JAM-C, and TF were demonstrated in primary tumors grown

28 We have identified DHHC7 as a JAM-C palmitoylating enzyme by screening all known palmi

29 ohydrate and junctional adhesion molecule A (JAM-A) and internalization by beta1 integrin.

30 glycans and junctional adhesion molecule A (JAM-A) as attachment receptors.

31 Junctional adhesion molecule A (JAM-A) is a broadly expressed adhesion molecule that reg

32 Junctional adhesion molecule A (JAM-A) is a unique tight junction (TJ) transmembrane pro

33 , CLDN4, and junctional adhesion molecule A (JAM-A) subunits is induced at the GL.

34 PDZ3 ligand, junctional adhesion molecule A (JAM-A) to determine how the activity of different domain

35 irus engages junctional adhesion molecule A (JAM-A) to disseminate hematogenously.

36 recruited by junctional adhesion molecule A (JAM-A) to primordial junctions where aPKC is activated b

37 Junctional adhesion molecule A (JAM-A), a member of the cortical thymocyte marker of the

38 we show that junctional adhesion molecule A (JAM-A), a tight junction protein, is a key negative regu

39 proteins is junctional adhesion molecule A (JAM-A), an Ig fold transmembrane protein.

40 ace glycans, junctional adhesion molecule A (JAM-A), and the Nogo-1 receptor (depending on the cell t

41 1), CD99 and junctional adhesion molecule A (JAM-A), but apparently not vascular endothelial cell-spe

42 ttachment to junctional adhesion molecule A (JAM-A), virions undergo clathrin-mediated endocytosis fo

43 ohydrate and junctional adhesion molecule A (JAM-A).

44 ous receptor junctional adhesion molecule A (JAM-A).

45 Mice lacking junctional adhesion molecule A (JAM-A, encoded by F11r) exhibit enhanced intestinal epit

46 ins, such as junctional adhesion molecule-A (JAM)-A, occludin, and zonula occludens (ZO)-1.

47 ind to human Junctional Adhesion Molecule-A (JAM-A) and alpha4 integrin, respectively.

48 glycans and junctional adhesion molecule-A (JAM-A) and enters cells by receptor-mediated endocytosis

49 eceptors and junctional adhesion molecule-A (JAM-A) and is thought to undergo a conformational change

50 s: occludin, junctional adhesion molecule-A (JAM-A) and N-cadherin at the BTB.

51 e identify the junction adhesion molecule-A (JAM-A) as a key target for miR-34/449 in the developing

52 Junctional adhesion molecule-A (JAM-A) is a member of the immunoglobulin family with div

53 Junctional adhesion molecule-A (JAM-A) is a serotype-independent receptor for reovirus.

54 Junctional adhesion molecule-A (JAM-A) is a tight junction protein that serves as a rece

55 Junctional adhesion molecule-A (JAM-A) is a tight junction-associated signaling protein

56 Junctional adhesion molecule-A (JAM-A) is a TJ-associated protein that regulates barrier

57 Junctional adhesion molecule-A (JAM-A) is a transmembrane component of tight junctions t

58 Junctional adhesion molecule-A (JAM-A) is a transmembrane tight junction protein that ha

59 Junctional adhesion molecule-A (JAM-A) is an adherens and tight junction protein express

60 y shown that junctional adhesion molecule-A (JAM-A) renders protection from thrombosis by suppressing

61 Although we understand much about JAM-A, little is known regarding the protein's role in m

62 neage raised the possibility that additional JAM family paralogues may also function in muscle develo

63 permeability similar to that observed after JAM-A loss.

64 presence of neutralizing antibodies against JAM-C.

65 s, we generated strains of mice with altered JAM-A expression in these cell types and assessed bloods

66 tion proteins (occludin, claudin-5, ZO-1 and JAM-1) in the parenchymal blood vessels, as well as albu

67 tein down-regulation of ZO-1, claudin-5, and JAM-1 in HBMEC.

68 gnificant sub-functionalisation of JAM-B and JAM-C orthologues with respect to binding strength (but

69 the heterotypic adhesion molecules JAM-B and JAM-C.

70 engagement of cell-surface carbohydrate and JAM-A by the length and IDR mutant viruses.

71 junction proteins such as ZO-1, claudin, and JAM-A; however, exposure of SCs to inflammatory mediator

72 eased in the trJAM-A(-/-) apoe(-/-)mice, and JAM-A-deficient platelets showed increased binding to mo

73 also formed a stable complex with Pals1 and JAM-C (a component of the apical ES) in normal testes.

74 to the cell surface, reovirus particles and JAM-A codistribute into each of these compartments.

75 iously shown to be involved in angiogenesis (JAM-B and PTTG1IP), that, when overexpressed, are respon

76 Accordingly, anti-JAM-C antibodies blocked adhesion of JAM-C-expressing B

77 Neutralizing anti-JAM-C Abs inhibited RA synovial fluid-induced HMVEC chem

78 Long-term administration of anti-JAM-C antibodies prevented engraftment of JAM-Cpos lymph

79 Treatment with anti-JAM-C antibodies in short-term experiments reduced migra

80 To assess JAM-A function in the lung, we depleted JAM-A in primary

81 We also show that integrin-associated JAM-A is tyrosine phosphorylated and is rapidly dephosph

82 method, that junctional adhesion molecule B (JAM-B) marks a previously unrecognized class of OFF RGCs

83 rin, ICAM-2, junctional adhesion molecule-B (JAM-B), laminin, and cellular fibronectin, supported bin

84 A functional link between JAM-A and beta1 integrin was confirmed by restoration of

85 cell lines, an inverse relationship between JAM-A expression and the ability of these cells to migra

86 In addition, native MS analysis of bsAb/JAM-A immune complexes revealed that bsAb can bind up to

87 ued by inhibition of ROCK and phenocopied by JAM-A, JACOP, or p114RhoGEF down-regulation.

88 egrin, which responds to bFGF stimulation by JAM-A release to regulate mitogen-activated protein kina

89 xpression of junctional adhesion molecule C (JAM-C) at EC junctions, and they were enhanced by blocka

90 the role of junctional adhesion molecule C (JAM-C) in mediating leukocyte recruitment and retention

91 Junctional adhesion molecule C (JAM-C) is a transmembrane protein with significant roles

92 Junctional adhesion molecule C (JAM-C) is an immunoglobulin superfamily protein expresse

93 Junctional adhesion molecule C (JAM-C) is expressed by vascular endothelium and human bu

94 s, including junctional adhesion molecule-C (JAM-C) and myelin-associated glycoprotein (MAG).

95 e identified junctional adhesion molecule-C (JAM-C) as a novel player in melanoma metastasis to the l

96 Junctional adhesion molecule-C (JAM-C) is an adhesion molecule expressed at junctions be

97 Junctional adhesion molecule-C (JAM-C) is an adhesion molecule expressed by endothelial

98 ty of the EC junctional adhesion molecule-C (JAM-C).

99 In endothelial cells, JAM-A has been implicated in basic fibroblast growth fac

100 In contrast, JAM-A deficiency in bone marrow cells impeded monocyte d

101 Compared to wild-type (WT) controls, JAM-C SC KO mice showed electrophysiological defects, mu

102 Overexpression of dimerization-defective JAM-A mutants in 293T cells inhibited cell spreading and

103 rt the effects of cis-dimerization-defective JAM-A mutants on epithelial cell migration and adhesion.

104 Protein phosphatase 2A dephosphorylates JAM-A at S285, suggesting that it antagonizes the activi

105 sess JAM-A function in the lung, we depleted JAM-A in primary alveolar epithelial cells using shRNA.

106 JAM-C-positive) and germinal center-derived (JAM-C-negative) B-cell lymphomas.

107 the classification of marginal zone-derived (JAM-C-positive) and germinal center-derived (JAM-C-negat

108 he Hz6F4 family preferentially binds dimeric JAM-A.

109 cycling to the membrane surface occur during JAM-A redistribution.

110 d vascular leakage, suggesting a role for EC JAM-C in the development of functional tumor vessels.

111 findings provide evidence for a role for EC JAM-C in tumor growth and aggressiveness as well as recr

112 However, tumor microvessels from EC JAM-C-deficient mice exhibited reduced pericyte coverage

113 , survival in this model was increased in EC JAM-C knockouts (KOs; 88 vs. 96 d, P=0.04) and reduced i

114 tumor growth was significantly reduced in EC JAM-C KOs (87% inhibition at 10 wk, P<0.0005), this was

115 (KOs; 88 vs. 96 d, P=0.04) and reduced in EC JAM-C transgenics (88 vs. 78.5 d, P=0.03), mice deficien

116 Local proteolytic cleavage of EC JAM-C by neutrophil elastase (NE) drove this cascade of

117 nt in promoting tumor growth, the role of EC JAM-C in tumor development was investigated using the ID

118 .03), mice deficient in or overexpressing EC JAM-C, respectively.

119 Our data identify endothelial JAM-A as an important effector molecule integrating athe

120 nt and luminal redistribution of endothelial JAM-A and were preferentially protected by its deficienc

121 expression and redistribution of endothelial JAM-A was increased by oxidized low-density lipoprotein,

122 We found that endothelial JAM-A but not hematopoietic JAM-A facilitates reovirus T

123 M-A reveals that both sigma1 proteins engage JAM-A with similar affinities and via conserved binding

124 , but not a DHHC7 catalytic mutant, enhances JAM-C S-palmitoylation.

125 Finally, JAM-C promotes the basal-to-apical transmigration of gra

126 ngs identify N-glycosylation as critical for JAM-A's many functions.

127 ies identified JAM-B as the major ligand for JAM-C, whereas homotypic JAM-C interactions remained at

128 tetraspanin CD9 as novel binding partner for JAM-A in endothelial cells.

129 w that glycosylation of N185 is required for JAM-A-mediated reduction of cell migration.

130 iles and gene expression data generated from JAM-C-expressing leukemic cells, we defined a single cel

131 derlying cause of these defects, nerves from JAM-C SC KO mice were found to have morphological defect

132 Cell adhesion genes, JAM-A and FSCN1, were downregulated with overexpression

133 ntributions of endothelial and hematopoietic JAM-A to reovirus dissemination and pathogenesis, we gen

134 that endothelial JAM-A but not hematopoietic JAM-A facilitates reovirus T1L bloodstream entry and egr

135 he major ligand for JAM-C, whereas homotypic JAM-C interactions remained at background levels.

136 However, JAM-A is dispensable for reovirus replication in the CNS

137 We show that human JAM-A contains a single N-glycan at N185 and that this r

138 Plasmon resonance studies identified JAM-B as the major ligand for JAM-C, whereas homotypic J

139 Our results identify JAM-C as a key regulator of polarized neutrophil TEM in

140 We show that impaired JAM-A expression in endothelial cells reduced mononuclea

141 omatic or endothelium-specific deficiency in JAM-A and bone marrow chimeras with JAM-A-deficient leuk

142 ls after overexpression of beta1 integrin in JAM-A dimerization-defective cells.

143 icated involvement of RhoA and Rho kinase in JAM-A relocalization.

144 hemokine (C-C motif) ligand 2 (CCL2) induced JAM-A redistribution from the interendothelial cell area

145 By ~20 min, most internalized JAM-A moved to the brain endothelial cell apical membran

146 of JAM-C-expressing B cells to their ligand JAM-B, and immunofluorescence analysis showed the expres

147 On alphaIIbbeta3 ligation, JAM-A was shown to be dephosphorylated, which could be p

148 binds to Junctional Adhesion Molecule-like (JAM-L) expressed on leukocytes.

149 gulates barrier; however, mechanisms linking JAM-A to epithelial permeability are poorly understood.

150 rowth factor (VEGF), respectively, CD9 links JAM-A specifically to alphavbeta3 integrin.

151 ts reduced migration of normal and malignant JAM-C-expressing B cells to bone marrow, lymph nodes, an

152 The mammalian JAM family is composed of three cell surface receptors.

153 RPE (hfRPE) with or without si-RNA mediated JAM-C knockdown and in adult native RPE wholemounts.

154 r signature of J-RGCs, the adhesion molecule JAM-B, regulates morphogenesis, and showed that it promo

155 mined the role of the cell adhesion molecule JAM-C, a protein known to mediate cellular polarity duri

156 Junctional adhesion molecule (JAM)-A expressed in endothelial, epithelial, and blood c

157 In platelets, junctional adhesion molecule (JAM)-A was previously identified as an inhibitor of inte

158 , and for the heterotypic adhesion molecules JAM-B and JAM-C.

159 mite and that junctional adhesion molecules (JAMs) mediate this required Notch signal transduction.

160 ngs indicate that CD9 incorporates monomeric JAM-A into a complex with alphavbeta3 integrin, which re

161 CD9 interacts predominantly with monomeric JAM-A, which suggests that bFGF induces signaling by tri

162 anine substitutions to residues 43NNP45 (NNP-JAM-A) within the predicted trans-dimerization site did

163 revealed decreased association forces in NNP-JAM-A compared with WT and cis-null JAM-A.

164 Expression of nonphosphorylatable JAM-A/S285A interferes with single lumen specification d

165 n, antibodies against PECAM or CD99, but not JAM-A, block transcellular migration.

166 In contrast, beads coated with cis-null JAM-A demonstrated enhanced clustering similar to that o

167 d that expression of trans- but not cis-null JAM-A mutants decreased Rap2 activity.

168 s in NNP-JAM-A compared with WT and cis-null JAM-A.

169 ciated integral membrane proteins: occludin, JAM-A, and N-cadherin.

170 The ability of JAM-A to attenuate cell invasion correlated with the for

171 Absence of JAM-A results in impaired c-SrcY(529) phosphorylation an

172 fection experiments revealed accumulation of JAM-A at sites between transfected cells, which was lost

173 y, anti-JAM-C antibodies blocked adhesion of JAM-C-expressing B cells to their ligand JAM-B, and immu

174 ighly migratory, express the least amount of JAM-A.

175 vely, the generation and characterization of JAM-C SC KO mice has provided unequivocal evidence for t

176 Deletion of JAM-A causes a gain-of-function in platelets, with lower

177 enhanced by blockade or genetic deletion of JAM-C in ECs.

178 ns further, mice with a specific deletion of JAM-C in SCs (JAM-C SC KO) were generated.

179 Trans-dimerization of JAM-A may thus act as a barrier-inducing molecular switc

180 e results suggest that trans-dimerization of JAM-A occurs at a unique site and with different affinit

181 These results suggest that dimerization of JAM-A regulates cell migration and adhesion through indi

182 alization and expression after disruption of JAM-A dimerization suggested that internalization of bet

183 Last, we show that the functional effects of JAM dimerization require its carboxy-terminal postsynapt

184 Assessment of effects of JAM-A dimerization on cell signaling revealed that expre

185 Notably, these proinflammatory effects of JAM-A-deficient platelets could be abolished by the inhi

186 ti-JAM-C antibodies prevented engraftment of JAM-Cpos lymphoma cells in bone marrow, spleen, and lymp

187 he HIV-induced decrease in the expression of JAM-A and occludin was restored by inhibition of MMP act

188 -NT did not alter cell surface expression of JAM-A or attachment of reovirus to cells.

189 ion of sigma1 and requires the expression of JAM-A.

190 th Afadin was dependent on the expression of JAM-A.

191 uorescence analysis showed the expression of JAM-B on murine and human lymphatic endothelial cells.

192 n, we recently reported on the expression of JAM-C in Schwann cells (SCs) and its importance for the

193 identify the localization and expression of JAM-C, ZO-1, N-cadherin, and ezrin in cultures of human

194 orts on previously undetected expressions of JAM-C, namely on perineural cells, and in line with noci

195 This study investigates the fate of JAM-A during inflammatory TJ complex remodeling and para

196 ggest a significant sub-functionalisation of JAM-B and JAM-C orthologues with respect to binding stre

197 To characterize cell-specific functions of JAM-A in atherosclerosis, we used apolipoprotein E-defic

198 N-glycosylation of JAM-A is required for the protein's ability to reinforce

199 Finally, we show that N-glycosylation of JAM-A regulates leukocyte adhesion and LFA-1 binding.

200 We generated mice with inactivation of JAM-C.

201 Inclusion of JAM-C as a sole marker on lineage-negative BM cells yiel

202 ccelerate the kinetics of internalization of JAM-A, N-cadherin, and occludin versus controls.

203 GF-beta3-induced increase in the kinetics of JAM-A and occludin endocytosis was abolished, making the

204 Furthermore, knockdown of JAM-A using short interfering RNAs enhanced the invasive

205 The level of JAM-C expression defines B-cell differentiation stages a

206 down decreases the S-palmitoylation level of JAM-C.

207 ratory MDA-MB-468 cells have lower levels of JAM-A on the cell surface.

208 AN nephrosis increased the protein levels of JAM-A, occludin, cingulin, and ZO-1 several-fold in glom

209 e least, are found to express high levels of JAM-A, whereas the more migratory MDA-MB-468 cells have

210 In cultured cells, loss of JAM-A caused an approximately 30% decrease in transepith

211 Furthermore, loss of JAM-A could be used as a biomarker for aggressive breast

212 stent with findings in other organs, loss of JAM-A decreased beta1 integrin expression and impaired f

213 Additionally, loss of JAM-A resulted in elevated mucosal and serum IgA that wa

214 Loss of JAM-A, Afadin, or PDZ-GEF2, but not ZO-1 or PDZ-GEF1, si

215 Overexpression of JAM-A in MDA-MB-231 cells inhibited both migration and i

216 ese results suggest that S-palmitoylation of JAM-C can be potentially targeted to control cancer meta

217 Palmitoylation of JAM-C promotes its localization to tight junctions and i

218 Finally, we show that phosphorylation of JAM-A at Ser-284 is required for RhoA activation in resp

219 vely at the TJs, and S285 phosphorylation of JAM-A is required for the development of a functional ep

220 ly conserved Phe(-2) and Ser(-3) residues of JAM.

221 rge molecules, revealing a potential role of JAM-A in controlling perijunctional actin cytoskeleton i

222 These data demonstrate a direct role of JAM-A in mechanosignaling and control of RhoA and implic

223 These findings support a key role of JAM-A in promoting tight junction homeostasis and lung b

224 e present study, we investigated the role of JAM-C in homing of human B cells, using a xenogeneic non

225 To determine the role of JAM-C in leukocyte retention in the RA synovium, in vitr

226 To investigate the role of JAM-C in neuronal functions further, mice with a specifi

227 Our results highlight the novel role of JAM-C in recruiting and retaining leukocytes in the RA s

228 On injury, the enhanced susceptibility of JAM-A(-/-) mice to edema correlated with increased, tran

229 f de novo AML patients at diagnosis based on JAM-C-expressing cells frequencies in the blood served a

230 the apical surface, and it was dependent on JAM-A.

231 ST fibroblasts and to RA ST was dependent on JAM-C.

232 We found that tension imposed on JAM-A activates RhoA, which leads to increased cell stif

233 n fully polarized cells, S285-phosphorylated JAM-A is localized exclusively at the TJs, and S285 phos

234 inase (Csk) binds to tyrosine phosphorylated JAM-A through its Src homology 2 domain.

235 trongly suggest that tyrosine-phosphorylated JAM-A is a Csk-binding protein and functions as an endog

236 to primordial junctions, aPKC phosphorylates JAM-A at S285 to promote the maturation of immature cell

237 Our data suggest that aPKC phosphorylates JAM-A at S285 to regulate cell-cell contact maturation,

238 l interfering RNA oligonucleotides prevented JAM-A relocalization, suggesting that macropinocytosis a

239 on of p38 MAPK and of the junctional protein JAM-A.

240 aphragms contain the tight junction proteins JAM-A (junctional adhesion molecule A), occludin, and ci

241 itis (OA), and normal ST samples to quantify JAM-C expression.

242 ation of microRNA (miR)-145, which repressed JAM-A.

243 equivocal evidence for the involvement of SC JAM-C in the fine organization of peripheral nerves and

244 ce with a specific deletion of JAM-C in SCs (JAM-C SC KO) were generated.

245 Thus, sigma1-JAM-A interactions are unlikely to explain the differenc

246 Reovirus virions bind to soluble JAM-A and NgR1, while infectious disassembly intermediat

247 is found in soluble form and whether soluble JAM-C (sJAM-C) mediates angiogenesis.

248 lung, whereas treatment of mice with soluble JAM-C prevented melanoma lung metastasis.

249 bility and lesion formation, whereas somatic JAM-A deletion revealed no significant effects.

250 -C(-/-) mice as well as endothelial-specific JAM-C-deficient mice displayed significantly decreased B

251 Upon agonist stimulation, JAM-A is dephosphorylated on the tyrosine, allowing the

252 Targeting JAM-C could thus constitute a new therapeutic strategy t

253 n the RA synovium and suggest that targeting JAM-C may be important in combating inflammatory disease

254 CD9 acts as scaffold and assembles a ternary JAM-A-CD9-alphavbeta3 integrin complex from which JAM-A

255 We conclude that JAM-A normally limits platelet accumulation by inhibitin

256 We have previously demonstrated that JAM-A regulates cell migration by dimerization of the me

257 Finally, we demonstrated that JAM-C controls Src family kinase (SFK) activation in LSC

258 We found that JAM-C is present in soluble form in normal serum and ele

259 hemical and structural studies indicate that JAM-A forms cis-homodimers, the functional significance

260 Here we report that JAM-A associates directly with ZO-2 and indirectly with

261 Here, we report that JAM-A is physically and functionally associated with the

262 ection of lipopolysaccharide, we report that JAM-A(-/-) mice showed increased susceptibility to pulmo

263 In this study, we show that JAM-A associates with integrin alphaIIbbeta3 in resting

264 Here we show that JAM-A in resting platelets functions as an endogenous in

265 Our results show that JAM-C exists in soluble form and suggest that modulation

266 Here, we show that JAM-C expression defines a subset of leukemic cells endo

267 Here, we show that JAM-C undergoes S-palmitoylation on two juxtamembrane cy

268 These findings suggest that JAM-A dimerization facilitates formation of a complex wi

269 Further experiments suggest that JAM-A does not regulate actin turnover but modulates act

270 These results suggest that JAM-A regulates epithelial permeability via association

271 e cell migration, and evidence suggests that JAM-A may form homodimers between cells (in trans).

272 Analyses of cells expressing the JAM-A dimerization-defective mutant proteins revealed di

273 e head domain via epitopes distinct from the JAM-A-binding site.

274 CAR is a member of the JAM family of adhesion receptors and is located to both

275 and in line with nociception defects of the JAM-C SC KO animals, on finely myelinated sensory nerve

276 SFK activation was uniquely found within the JAM-C-expressing LSC compartment.

277 Thus, JAM-A recruits Csk to the integrin-c-Src complex in rest

278 Thus, JAM-B identifies a unique population of RGCs in which st

279 nfectious subvirion particles, which bind to JAM-A but bypass a requirement for proteolytic uncoating

280 nding to only a few receptors: IE binding to JAM-B decreased with age, while binding to CD36 and inte

281 cture of serotype 3 reovirus sigma1 bound to JAM-A reveals that both sigma1 proteins engage JAM-A wit

282 core gene expression signature correlated to JAM-C expression that reveals LSC heterogeneity.

283 events as supported by presentation of NE to JAM-C via the neutrophil adhesion molecule Mac-1.

284 sassembly intermediates (ISVPs) bind only to JAM-A.

285 Together, JAM-C represents a novel therapeutic target for melanoma

286 Mice with or without platelet-specific (tr)JAM-A-deficiency in an apolipoprotein e (apoe(-/-)) back

287 ts that bFGF induces signaling by triggering JAM-A dimerization.

288 We also demonstrate that T1L/T3DM2 utilizes JAM-A more efficiently than T1L.

289 ) was efficacious at causing loss of venular JAM-C and promoting neutrophil reverse transendothelial

290 elial cell area to the apical surface, where JAM-A played a role as a leukocyte adhesion molecule par

291 n the current study, we investigated whether JAM-C is found in soluble form and whether soluble JAM-C

292 -CD9-alphavbeta3 integrin complex from which JAM-A is released upon bFGF stimulation.

293 iency in JAM-A and bone marrow chimeras with JAM-A-deficient leukocytes.

294 Of importance, microspheres coated with JAM-A containing alanine substitutions to residues 43NNP

295 F2 colocalized and coimmunoprecipitated with JAM-A.

296 ent protein sigma1 alone and in complex with JAM-A.

297 f association of the Par6/Pals1 complex with JAM-C, thereby destabilizing apical ES to facilitate spe

298 we show that aPKC can interact directly with JAM-A in a PAR-3-independent manner.

299 d that both antibodies likely interfere with JAM-A engagement by steric hindrance.

300 similar to that observed with wild-type (WT) JAM-A.