ライフサイエンスコーパス: BSAP

1 BSAP (Pax5) is an essential transcription factor for ear

2 BSAP activated the promoter in transfected cells, and th

3 BSAP failed to trans-activate CD19 promoter constructs i

4 BSAP has been shown previously to be important for B cel

5 BSAP knockdown led to an increase in the expression of m

6 BSAP may play an additional role later in development, s

7 BSAP regulates transcription of several genes expressed

8 As a paradigm for these interactions, Pax-5 (BSAP) assembles ternary complexes with Ets proteins on t

9 observed for the transcription factors Pax-5/BSAP, Bob-1, and Ikaros, but this was not a general prop

10 m, we identified importin alpha1 (Rch1) as a BSAP-interacting protein.

11 Combining structural investigation of a BSAP-1-receptor complex with mutational analysis, we unv

12 , we show that deletion of the CTD abrogates BSAP-1 bactericidal activity by preventing receptor bind

13 ivator protein (BSAP) site, the low affinity BSAP site, a SP1/Egr-1 site termed the CD19 GC box, and

14 PU.1 and BSAP are transcription factors crucial for proper B-cell

15 Although PU.1 and BSAP can physically interact through their respective DN

16 In addition, hXBP-1 and BSAP levels were inversely correlated along the early st

17 gulate 3'alpha E(hs1,2), including Oct-1 and BSAP, were identified, and their contribution to 3'alpha

18 Complex 3 and BSAP have identical cell-type specificities, as they are

19 and functional interactions between AML1 and BSAP and suggest that AML1 is an important factor for re

20 ivity in transfection studies where AML1 and BSAP synergistically activate blk promoter transcription

21 ranscription factor gene PAX5 (also known as BSAP) are a hallmark of B cell precursor acute lymphobla

22 The absence of positive factors such as BSAP accounts for at least part of the loss of mouse CD7

23 ts indicates that sequences flanking a and b BSAP-binding sites are essential for appropriate regulat

24 We demonstrate a direct connection between BSAP and B-lymphocyte-induced maturation protein 1 (Blim

25 Physical interaction between BSAP and importin alpha1 was detected in vitro by a glut

26 d repression, a physical interaction between BSAP and octamer-binding proteins was demonstrated using

27 However, when both BSAP-binding sites were mutated, the octamer and G-rich

28 t CD72 promoter activity was up-regulated by BSAP in plasmacytoma cells and T cells in a dose-depende

29 present in J chain-expressing plasma cells, BSAP repression could be overridden by positive-acting f

30 ied in both pro- and pre-B cells, while CRE, BSAP, and PU.1/pip sites within the 3'kappa enhancer und

31 f the 102 B-cell NHLs, 83 (81%) demonstrated BSAP expression.

32 In later B cell development, BSAP has been implicated in the regulation of 3' Ig enha

33 ors necessary for B lineage differentiation (BSAP, E12, E47, and Id) provide further support for desi

34 In EMSAs, BSAP antibody specifically recognized complex 3, and in

35 Pax5 encodes BSAP, a member of the paired box domain transcription fa

36 EML cells expressing BSAP/Pax5A successfully acquired the myeloid lineage mar

37 ed with retrovirus constitutively expressing BSAP/Pax5A began myeloid cell differentiation, but like

38 sensus binding site for transcription factor BSAP (B cell lineage-specific activator protein).

39 and have shown that the transcription factor BSAP (B-cell-specific activator protein) directly intera

40 gene PAX-5 encodes the transcription factor BSAP (B-cell-specific activator protein), which plays a

41 hat the B-cell-specific transcription factor BSAP (Pax-5) could bind to a conserved sequence critical

42 y, we reported that the transcription factor BSAP (PAX-5) regulates the murine RAG-2 promoter in B-ce

43 ll immune response, the transcription factor BSAP maintains its activator functions but is relieved o

44 hat the B cell-specific transcription factor BSAP/Pax5 binds to a second site, CBF2, in the E2RE.

45 of the B-cell-specific transcription factor BSAP/Pax5A in regulating B-lymphoid-restricted gene expr

46 identified as the Pax5 transcription factor, BSAP, which recognizes a negative regulatory motif in th

47 ndent mechanism whereby activator motifs for BSAP had a 20-fold higher binding affinity than represso

48 different amounts of expression plasmids for BSAP showed that CD72 promoter activity was up-regulated

49 Previous studies have suggested a role for BSAP-interacting proteins in the regulation of the funct

50 These studies identify a role for BSAP/Pax5A in suppressing the response to myeloid growth

51 Binding sites for BSAP have been identified in the promoters of multiple g

52 alization to green fluorescent protein (GFP)-BSAP fusion proteins.

53 ific transcription factors including Ikaros, BSAP, PU.1, and octamer binding proteins, as well as DNA

54 A predicted NLS in BSAP (NKRKRDE, located at amino acids 195-201 in the cen

55 The NLS sequence in BSAP conferred nuclear localization to green fluorescent

56 We also show that PU.1 can inhibit BSAP transactivation and that this repression requires P

57 Western blot analysis showed a 52-kD BSAP band in B-cell lines, but not in non-B-cell or plas

58 l zone lymphoma cases showed negative or low BSAP levels, and 17 of 24 (71%) large B-cell lymphomas d

59 ormal lymphoid tissues showed strong nuclear BSAP expression in mantle zone B cells, less intense rea

60 sical cases showed weak nuclear or nucleolar BSAP reactions in a fraction of the tumor cells.

61 of B, T, and myeloid cells, while absence of BSAP results in an early block in B-cell differentiation

62 s down-regulated by the concerted actions of BSAP, octamer, and G-rich DNA-binding proteins.

63 is opposed by the downregulatory actions of BSAP.

64 Mutations eliminating the binding of BSAP in reporter constructs also eliminated the increase

65 lly, we provide evidence that the binding of BSAP prevents USF and B-MEF2 from interacting with the J

66 AP binding in mature B cells, the binding of BSAP was undetectable in those plasma cells.

67 ely driven by the C-terminal domain (CTD) of BSAP-1 using a combination of in vivo competition assays

68 he N-terminal paired (DNA-binding) domain of BSAP also conferred nuclear localization when coupled to

69 The NLS sequence in the central domain of BSAP binds to the C-terminal 98-amino acid fragment of i

70 eracts with the paired DNA-binding domain of BSAP, a B cell-specific transcription factor.

71 mechanisms and significance of the effect of BSAP on isotype switching are discussed.

72 To directly examine the effects of BSAP on isotype switching, we use a tetracycline-regulat

73 's lymphoma (NHL), a detailed examination of BSAP expression in NHL has not been previously reported.

74 roteins in the regulation of the function of BSAP.

75 ng both repressor and activator functions of BSAP during a B cell immune response.

76 It is not until the levels of BSAP decrease during the antigen-driven stages of B cell

77 The levels of BSAP progressively decrease in response to IL-2 and this

78 ering RNA-mediated repression, the levels of BSAP were decreased in vitro in the NZB-derived malignan

79 CLL patient B-cell expression levels of BSAP were increased compared with control sources of B c

80 The high levels of BSAP, especially those found in large-cell lymphomas and

81 Overexpression of BSAP in these cells reversed the positive regulation and

82 its effects on switching, overexpression of BSAP inhibits germline alpha RNA expression and the tran

83 We find that overexpression of BSAP inhibits switching to IgA in I.29 mu cells stimulat

84 Compared with the presence of BSAP binding in mature B cells, the binding of BSAP was

85 Thus, IL-2 regulation of BSAP concentration may provide a mechanism for controlli

86 manner by an IL-2-induced down-regulation of BSAP RNA expression.

87 tial reversal of PU.1-mediated repression of BSAP.

88 The possible roles of BSAP and PU.1 antagonistic activities in hematopoietic d

89 This selective targeting of BSAP activities was shown to be regulated by a concentra

90 a factor with properties similar to those of BSAP (B-cell-specific activator protein).

91 d serum osteocalcin but did not alter NTx or BSAP concentration.

92 e-regulated expression system to overexpress BSAP in the surface IgM+ I.29 mu B cell line, a mouse ce

93 Pax5 (BSAP) is essential for B cell development and acts both

94 The transcription factor Pax5 (BSAP) is required for the expression of a B-cell-specifi

95 he B-cell-specific transcription factor Pax5/BSAP.

96 n (NTx), bone-specific alkaline phosphatase (BSAP), and phylloquinone concentrations were measured at

97 s with the B cell-specific activator protein BSAP/Pax5.

98 we therefore investigated the model protein BSAP-1 and determined which of its domains is involved i

99 5/B cell lineage specific activator protein (BSAP) is a B lineage-specific regulator that controls th

100 y B cell lineage-specific activator protein (BSAP) site, the low affinity BSAP site, a SP1/Egr-1 site

101 B cell-specific activator protein (BSAP), a transcription factor that silences J chain tran

102 t B-cell lineage specific activator protein (BSAP), also known as paired box 5 (PAX5), controls MCOLN

103 B cell lineage-specific activator protein (BSAP), encoded by the Pax 5 gene, is a critical modulato

104 B-cell lineage-specific activator protein (BSAP), encoded by the Pax-5 gene, is critical for B-cell

105 n factor, B-cell-specific activator protein (BSAP), represses the murine immunoglobulin heavy-chain 3

106 on factor B cell-specific activator protein (BSAP).

107 B cell-specific activator protein (BSAP)/Pax-5 is a paired domain DNA-binding protein expre

108 soform of B cell-specific activator protein (BSAP, or Pax5) in MM cells while performing differential

109 [EBF] and B cell specific activator protein [BSAP]).

110 3' enhancer and associated binding proteins, BSAP represses PU.1 function by a distinct mechanism.

111 epression of Pax-5 is sufficient to regulate BSAP targets CD19 and J chain and is necessary but not s

112 e transcription of the germline epsilon RNA, BSAP has been hypothesized to be involved in regulation

113 olation on a multimerized PU.1 binding site, BSAP targets a portion of the PU.1 transactivation domai

114 This antimicrobial molecule, termed BSAP-1, is secreted from the cell in outer membrane vesi

115 cted to lymphomas of B-cell lineage and that BSAP expression varies in B-cell subsets and subtypes of

116 We conclude that BSAP expression is largely restricted to lymphomas of B-

117 In summary, our research demonstrates that BSAP receptor recognition is driven by their CTD and pav

118 We find here that BSAP can repress 3' enhancer activity.

119 an hXBP-1 reporter construct indicated that BSAP downregulates the hXBP-1 promoter.

120 Functional assays showed that BSAP mediates the silencing of the J chain gene during t

121 mmunoprecipitation assay, we have shown that BSAP directly interacts with the Dleu2 promoter.

122 This study strongly suggests that BSAP-FP II interaction plays a critical role in determin

123 The BSAP inhibitory domain (residues 358 to 385) is needed f

124 d the promoter in transfected cells, and the BSAP site was occupied in a tissue-specific manner in vi

125 an E-box motif immediately upstream from the BSAP site on the J chain promoter.

126 Mutations in the AT box or in the BSAP sites did not affect CD19 reporter construct activi

127 include the 3' region of the CRE motif, the BSAP motif, and the region 3' of the E2A motif.

128 transcription factor PU.1 is a target of the BSAP-mediated repression.

129 T- and null-cell lymphomas reacted with the BSAP antisera, whereas in Hodgkin's disease, 2 of 4 (50%

130 eins enables CTD-driven interaction with the BSAP-1 receptor.

131 coactivator protein p300 can eliminate this BSAP-mediated repression.

132 Thus, BSAP/Pax5A was constitutively expressed in the multipote

133 ecognized complex 3, and in vitro translated BSAP could bind to an hXBP promoter fragment.

134 Moreover, in plasma cells, when BSAP is not expressed, 3' alpha E(hs1,2) is active, and

135 ighest levels of hXBP-1 mRNA were found when BSAP was not expressed, in pre-Pro-B cells and in plasma

136 rather than the affinity, determined whether BSAP operated as an activator or repressor.

137 tes the enhancer in pre-B and B cells, while BSAP is a repressor in pre-B cells and an activator at t

138 Physical interaction of AML1 with BSAP correlates with functional cooperativity in transfe

139 ition of histone deacetylation combined with BSAP knockdown increased miR-15a/16-1 expression, and al