ライフサイエンスコーパス: JAM

1 JAM function by interacting with other proteins through

2 JAM-A (junctional adhesion molecule A) is a transmembran

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

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

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

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

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

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

9 JAM-A or CD9 knockdown impairs endothelial cell migratio

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

11 JAM-A redistribution was associated with internalization

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

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

14 JAM-A-deficient platelets showed increased aggregation a

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

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

17 JAM-C has been implicated in leukocyte transendothelial

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

55 Junctional adhesion molecule-A (JAM-A), an epithelial tight junction protein, plays an i

56 glycans and junctional adhesion molecule-A (JAM-A), triggering uptake into the endocytic compartment

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

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

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

60 presence of neutralizing antibodies against JAM-C.

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

62 studies of the JAM family members JAM-A and JAM-C have expanded the roles of these proteins to inclu

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

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

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

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

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

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

69 both alpha-linked sialic acid (alpha-SA) and JAM-A cell-surface receptors.

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

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

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

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

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

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

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

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

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

79 s on the same cell, and interactions between JAM and cell surface receptors expressed on adjacent cel

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

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

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

83 C/EBP-alpha that is positively modulated by JAM-A, a component of tight junctions that acts through

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

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

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

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

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

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

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

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

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

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

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

95 ng routes of junctional adhesion molecule-C (JAM-C).

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

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

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

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

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

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

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

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

104 he Hz6F4 family preferentially binds dimeric JAM-A.

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

106 Dynamic JAM-C trafficking and degradation are necessary for junc

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

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

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

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

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

112 (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

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

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

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

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

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

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

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

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

121 The enhanced JAM-A binding by virions following alpha-SA engagement i

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

123 Finally, JAM-A-C/EBP-alpha-mediated regulation of claudin-5 was l

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

125 plaques, and displays increased avidity for JAM-A relative to the parental virus, mimicking properti

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 Mechanistically, JAM-A promoted C/EBP-alpha expression through suppressio

154 er, recent studies of the JAM family members JAM-A and JAM-C have expanded the roles of these protein

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

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

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

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

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

160 proteins and junctional adhesion molecules (JAM) in cancer suggested a tumor-suppressive role where

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

178 Genetic deletion of JAM-A in mice significantly increased vascular permeabil

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

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

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

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

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

184 er the expression of claudin-5 downstream of JAM-A, to thus enhance vascular barrier function.

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

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

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

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

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

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

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

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

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

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 discuss these context-dependent functions of JAM in a variety of cancers and highlight key areas that

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

199 th the pro- and antitumorigenic functions of JAM.

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

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

202 We generated mice with inactivation of JAM-C.

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

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

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

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

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

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

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

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

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

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

216 Phosphorylation of JAM-A Y280 and increased permeability correlated with re

217 ier defects and inhibited phosphorylation of JAM-A Y280 in vitro.

218 chanism by which tyrosine phosphorylation of JAM-A Y280 regulates epithelial barrier function during

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

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

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

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

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

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

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

226 ions, we report that the cytoplasmic tail of JAM-A is tyrosine phosphorylated (p-Y280) in association

227 point of regulation is the ubiquitylation of JAM-C by the E3 ligase Casitas B-lineage lymphoma (CBL),

228 lications in furthering our understanding of JAM in cancer and provide a paradigm for exploring addit

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

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

231 PN13 as a major kinase and phosphatase for p-JAM-A Y280, respectively.

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

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

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

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

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

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

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

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

240 creased permeability correlated with reduced JAM-A association with active Rap2.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

256 We found that JAM-C cotraffics with receptors associated with changes

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

272 However, recent studies of the JAM family members JAM-A and JAM-C have expanded the rol

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

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

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

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

277 -SA favors a strong multivalent anchorage to JAM-A.

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

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

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

281 llowing alpha-SA engagement is comparable to JAM-A binding by infectious subvirion particles (ISVPs)

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 stand the molecular mechanisms through which JAM-A expression regulates tight junction organization t

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

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

296 F2 colocalized and coimmunoprecipitated with JAM-A.

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

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.