ライフサイエンスコーパス: PTPmu

1 PTPmu expression in the optic tectum occurred as a smoot

2 PTPmu has been shown previously to interact with the E-c

3 PTPmu has been shown to regulate cadherin-mediated cell

4 PTPmu is a RPTP that mediates cell aggregation and is ex

5 PTPmu is expressed in the chick retina during developmen

6 PTPmu was expressed in postconfluent human pulmonary art

7 PTPmu wedge Tat peptide had no effect on PC12 cells but

8 PTPmu, an Ig superfamily receptor protein-tyrosine phosp

9 PTPmu-VE-cadherin interactions were demonstrated through

10 eceptor for activated protein C kinase) as a PTPmu interacting protein.

11 Using conventional peptide chemistry, a PTPmu-targeted peptide was linked to a chelator that had

12 e outgrowth of retinal ganglion neurons on a PTPmu substrate, whereas LAR wedge peptide had no effect

13 a differential response of RGC neurites to a PTPmu substrate was also observed: RGCs of temporal reti

14 y proteolysis generates catalytically active PTPmu fragments that contribute to migration and surviva

15 In addition, PTPmu was found in a complex with N-cadherin in retinal

16 ast two-hybrid screen to identify additional PTPmu interacting proteins.

17 te common antigen-related (LAR) receptor and PTPmu, contain a wedge-shaped helix-loop-helix located n

18 In contrast, PTP-PEST, Shp2, and PTPmu did not interact with these proteins, suggesting t

19 ial cells when homophilic binding to another PTPmu molecule on an apposing cell was not possible, res

20 we have demonstrated directly that the anti-PTPmu antibody BK2 that we used initially did not cross-

21 ical significance of the association between PTPmu and N-cadherin, the expression level and enzymatic

22 When given a choice between PTPmu and a second substrate, the growth cones of tempor

23 ve mutant form of v-Src, the complex between PTPmu and E-cadherin was dynamic, and conditions that re

24 We observed a direct interaction between PTPmu and E-cadherin after coexpression in Sf9 cells.

25 ce the observation of an interaction between PTPmu and E-cadherin in vitro and in vivo, further empha

26 ted that the association we observed between PTPmu and the cadherin-catenin complex in immunoprecipit

27 ompetes IQGAP1 binding to Rho GTPases blocks PTPmu-mediated neurite outgrowth.

28 catalytic activity and adhesion mediated by PTPmu regulate lamination of the retina, emphasizing the

29 This single Gd-containing PTPmu agent was more effective than our previous version

30 In contrast, PTPmu was permissive for growth of nasal neurites.

31 In subconfluent cell cultures, PTPmu resides in an intracellular membrane pool; however

32 herin and catenins but do not mediate either PTPmu- or E-cadherin-dependent adhesion.

33 ave shown that the association of endogenous PTPmu and RACK1 in a lung cell line is increased at high

34 ell-cell contact, which may be important for PTPmu-dependent signaling in response to cell-cell adhes

35 signaling pathways, we used a series of GST-PTPmu fusion proteins, including catalytically inactive

36 To gain a better understanding of how PTPmu is regulated, we examined the importance of the co

37 and substrate trapping mutants, to identify PTPmu-interacting proteins.

38 These data indicate PTPmu may regulate Rho-GTPase-dependent functions of IQG

39 this article, overexpression of full-length PTPmu is shown to suppress migration and survival of gli

40 he receptor protein-tyrosine phosphatase mu (PTPmu) is a homophilic adhesion protein thought to regul

41 he receptor protein tyrosine phosphatase mu (PTPmu) is a homophilic cell adhesion molecule.

42 ention of a protein tyrosine phosphatase mu (PTPmu)-targeted, molecular magnetic resonance (MR) contr

43 y, receptor protein tyrosine phosphatase Mu, PTPmu, is expressed in precursor and early, differentiat

44 the Rho GTPases, Cdc42 and Rac1, as a novel PTPmu-interacting protein.

45 onstrate that amino acid residues 765-958 of PTPmu, which include the juxtamembrane domain and 35 res

46 KC could be playing a role in the ability of PTPmu to restore E-cadherin-dependent adhesion.

47 e expression level and enzymatic activity of PTPmu were perturbed in retinal explant cultures.

48 These characteristics of PTPmu, which are consistent with a role in cell-cell adh

49 To aid in the further characterization of PTPmu signaling pathways, we used a series of GST-PTPmu

50 adherin were associated with dissociation of PTPmu from the complex.

51 globulin domain affected the distribution of PTPmu in subconfluent endothelial cells when homophilic

52 eraction between the intracellular domain of PTPmu and RACK1, a receptor for activated protein kinase

53 The extracellular domain of PTPmu contains motifs commonly found in cell adhesion mo

54 The intracellular domain of PTPmu contains two conserved catalytic domains, only the

55 The membrane-proximal catalytic domain of PTPmu was used as bait.

56 the presence of the intracellular domains of PTPmu to restore E-cadherin-mediated adhesion.

57 Downregulation of PTPmu expression through antisense techniques resulted i

58 The signaling pathway downstream of PTPmu is unknown; therefore, we used a yeast two-hybrid

59 expression both by regulating expression of PTPmu and by organizing a multimolecular complex contain

60 Re-expression of PTPmu restored cell adhesion to PTPmu and to E-cadherin.

61 Expression of PTPmu-extra (which lacks most of the cytoplasmic domain)

62 The unique features of PTPmu make it an attractive molecule to transduce signal

63 The full-length form of PTPmu is down-regulated in human glioblastoma.

64 pression of a catalytically inactive form of PTPmu significantly decreased neurite outgrowth on N-cad

65 A mutant form of PTPmu that is catalytically inactive was re-expressed, a

66 , or a catalytically inactive mutant form of PTPmu, and homophilic adhesion was blocked by using a fu

67 lytically active and inactive mutant form of PTPmu.

68 resence of cadherin in immunoprecipitates of PTPmu obtained with three antibodies that recognize dist

69 A peptide inhibitor of PTPmu function blocks fragment-induced glioblastoma cell

70 ser extent Rac1, enhances the interaction of PTPmu and IQGAP1.

71 n human lung microvascular ECs, knockdown of PTPmu through RNA interference dramatically impaired bar

72 mporal axons expressing the highest level of PTPmu.

73 domain in regulation of the localization of PTPmu and the importance of such control for the mainten

74 munoglobulin domain impaired localization of PTPmu to the cell-cell contacts in endothelial and epith

75 tic cleavage is shown to be the mechanism of PTPmu down-regulation in glioblastoma cells.

76 Proteolysis of PTPmu generates a series of proteolytic fragments, inclu

77 hort hairpin RNA-mediated down-regulation of PTPmu fragments decreases glioblastoma cell migration an

78 Since the timing of PTPmu expression correlates with the peak period of reti

79 ral retina were unable to extend neurites on PTPmu compared with neurites of nasal retina.

80 Fluorescent beads coated with LAR or PTPmu wedge peptides demonstrated PTP-specific homophili

81 All conditions that perturbed PTPmu dramatically disrupted retinal histogenesis.

82 at the receptor protein tyrosine phosphatase PTPmu associates with the cadherin-catenin complex in va

83 The receptor protein-tyrosine phosphatase PTPmu is a member of the Ig superfamily of cell adhesion

84 receptor-type protein tyrosine phosphatase, PTPmu is a cell adhesion molecule that mediates cell agg

85 s the receptor protein-tyrosine phosphatase, PTPmu, whereas LNCaP prostate carcinoma cells do not.

86 Only proteolyzed PTPmu fragments are detected in human glioblastomas.

87 One such receptor PTP, PTPmu, is highly expressed in lung tissue and is almost

88 RPTP R2B subfamily, which includes PTPkappa, PTPmu and PCP-2.

89 s incubated with purified recombinant PTPmu, PTPmu directly bound to VE-cadherin.

90 lecular complex containing PKCbetaII, RACK1, PTPmu, beta-catenin, and E-cadherin.

91 erin was incubated with purified recombinant PTPmu, PTPmu directly bound to VE-cadherin.

92 RGC axons innervate anterior tectal regions, PTPmu may regulate the formation of topographic projecti

93 Finally, application of soluble PTPmu to retinal cultures resulted in the collapse of te

94 These data suggest that loss of cell surface PTPmu by proteolysis generates catalytically active PTPm

95 In this study, we demonstrate that PTPmu promotes neurite outgrowth of retinal ganglion cel

96 This study demonstrates that PTPmu association with RACK1 is disrupted by the presenc

97 These data indicate that PTPmu specifically regulates signals required for neurit

98 In this study, we observed that PTPmu expression in RGC axons occurs as a step gradient,

99 We observed that PTPmu interacted with N-cadherin, E-cadherin, and cadher

100 Together, these results suggest that PTPmu plays a dual role in the regulation of neurite out

101 Together, these studies suggest that PTPmu regulates the PKC pathway to restore E-cadherin-de

102 cones of temporal neurites clustered at the PTPmu border and stalled, thus avoiding additional growt

103 had no effect on PC12 cells but blocked the PTPmu-dependent phenotype of neurite outgrowth of retina

104 Protein kinase C is a component of the PTPmu signaling pathway utilized to regulate these event

105 nd suggest that IQGAP1 is a component of the PTPmu signaling pathway.

106 lled, thus avoiding additional growth on the PTPmu substrate.

107 Therefore, PTPmu is expressed in human pulmonary vascular endotheli

108 Therefore, PTPmu may be one of the proteins that recruits RACK1 to

109 Therefore, PTPmu may specifically signal to temporal RGC axons to c

110 Following complexation with Gd, this PTPmu-targeted molecular contrast agent containing a sin

111 -expressed, and it also restored adhesion to PTPmu and to E-cadherin.

112 xpression of PTPmu restored cell adhesion to PTPmu and to E-cadherin.

113 the cytoplasmic domain) induced adhesion to PTPmu but not to E-cadherin, demonstrating a requirement

114 ross-reactivity between BK2, our antibody to PTPmu, and cadherins.

115 ses encoding either an antisense sequence to PTPmu, wild-type PTPmu, or a catalytically inactive muta

116 When glutathione S-transferase-PTPmu was incubated with purified recombinant VE-cadheri

117 Overexpression of wild-type PTPmu decreased tyrosine phosphorylation of VE-cadherin.

118 crovascular ECs, overexpression of wild-type PTPmu enhanced barrier function.

119 er an antisense sequence to PTPmu, wild-type PTPmu, or a catalytically inactive mutant form of PTPmu,

120 We therefore studied whether PTPmu, in pulmonary vascular endothelia, associates with

121 E-cadherin was required for association with PTPmu in WC5 cells.

122 We demonstrate that RACK1 interacts with PTPmu when co-expressed in a recombinant baculovirus exp