Interleukin 7 receptor ligation stimulates tyrosine phosphorylation, inositol phospholipid turnover, and clonal proliferation of human B-cell precursors.

Uckun, Fatih M.; Dıbırdık, İlker; Smith, Ron S.; Tuel‐Ahlgren, Lisa; Chandan-Langlie, Mridula; Schieven, Gary L.; Waddick, Kevin G.; Hanson, Mildren; Ledbetter, Jeffrey A.

doi:10.1073/pnas.88.9.3589

Cited by 85 publications

(52 citation statements)

References 33 publications

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“…3A). Similar amounts of E2A proteins were detected in equal volumes (also containing similar amounts of protein) of the prepared nuclear and cytoplasmic fractions of two pro-B-cell lines (FL-8.2 and FL112) which were derived from fetal liver (59,60), two mature B-cell lines (Raji and BJAB), the plasma cell line (ARH-77) (Fig. 3A), and the CESS cell line (data not shown).…”

Section: E2 Site Inmentioning

confidence: 75%

E2A expression, nuclear localization, and in vivo formation of DNA- and non-DNA-binding species during B-cell development.

Jacobs¹,

Vierra²,

Nelson³

1993

Mol. Cell. Biol.

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A monoclonal antibody (Yae) was characterized and shown to specifically recognize E2A proteins in vivo, including the E2A-Pbxl fusion gene products, p77E2'-Pbxl and p85E2-A-txl. E2A proteins of a predominant molecular mass of 72 kDa, which comigrated with in vitro-produced rat E12 and rat E47, were detected in human pro-B, pre-B, mature B, and plasma cell lines. The Yae antibody detected an E2A-containing pE2 enhancer element-binding complex (BCF-1) in pre-B-and mature B-cell lines in electrophoretic mobility shift assays which displayed a migration rate similar to that of in vitro-produced rat E12 and rat E47. A new E2A-containing iLE2-binding species (P-E2A) was identified in plasma cells by using electrophoretic mobility shift assays. E2A proteins were detected in pro-B cells but were unable to bind the ,uE2 site. These observations suggest that the tLE2 site is the target of stage-specific E2A regulatory complexes during B-cell development.Immunostaining analyses demonstrated the predominant nuclear localization of E2A proteins. Finally, we have identified an E2A form, designated I-E2A, which is unable to bind DNA. Our observations demonstrate novel in vivo mechanisms for the regulation of transcription by E2A proteins during B-cell development.

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Section: E2 Site Inmentioning

confidence: 75%

E2A expression, nuclear localization, and in vivo formation of DNA- and non-DNA-binding species during B-cell development.

Jacobs¹,

Vierra²,

Nelson³

1993

Mol. Cell. Biol.

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“…Moreover, the phosphopeptide patterns generated by V8 digestion of the 170-kDa proteins were identical to each other. Thus (28)(29)(30)(31)(32)(33). However, no substrate in the 170-kDa size range was described in any of these studies.…”

Section: Discussionmentioning

confidence: 92%

Common elements in interleukin 4 and insulin signaling pathways in factor-dependent hematopoietic cells.

Wang

Keegan

et al. 1993

Proc. Natl. Acad. Sci. U.S.A.

159

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Interleukin 4 (IL-4), insulin, and insulin-like growth factor I (IGF-I) efficiently induced DNA synthesis in the IL-3-dependent murine myeloid cell lines FDC-P1 and FDC-P2. Although these factors could not individually sustain long-term growth of these lines, a combination of IL-4 with either insulin or IGF-I did support continuous growth. The principal tyrosine-phosphorylated substrate observed in FDC cells stimulated with IL-4, previously designated 4PS, was of the same size (170 kDa) as the major substrate phosphorylated in response to insulin or IGF-I. These substrates had phosphopeptides of the same size when analyzed by digestion with Staphylococcus aureus V8 protease, and each tightly associated with the 85-kDa component of phosphatidylinositol 3-kinase after factor stimulation. IRS-1, the principal substrate phosphorylated in response to insulin or IGF-I stimulation in nonhematopoietic cells, is similar in size to 4PS. However, anti-IRS-1 antibodies failed to efficiently precipitate 4PS, and some phosphopeptides generated by V8 protease digestion of IRS-1 were distinct in size from the phosphopeptides of 4PS. Nevertheless, IL-4, insulin, and IGF-I were capable of stimulating tyrosine phosphorylation of IRS-1 in FDC cells that expressed this substrate as a result of transfection. These rmdings indicate that (i) IL-4, insulin, and IGF-I use signal transduction pathways in FDC lines that have at least one major feature in common, the rapid tyrosine phosphorylation of 4PS, and (it) insulin and IGF

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“…There is a body of evidence supporting the essential role of IL-7 in promoting mouse precursor B cell growth . Although human B cell progenitors express the high affinity IL-7R [31], IL-7 was found to have a less crucial effect on human pro-B and pre-B cell growth [27,32]. Recently, this cytokine was shown to down-modulate RAG and TdT-genes and to up-regulate surface CD19 expression in normal human pre-B cells [33].…”

Section: Discussionmentioning

confidence: 99%

IL-7 sensitizes human pre-B cells but not pro-B cells to Fas/APO-1 (CD95)-mediated apoptosis

Lévy¹,

Benlagha²,

Buzyn³

et al. 1997

Clinical and Experimental Immunology

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SUMMARYHomeostasis of human B cell development is maintained by a complex network of cytoplasmic and surface expressed molecules. Abnormalities in this process may result in the expansion of malignant B cell precursors in B lineage acute lymphoblastic leukaemia (ALL). ALL cells share surface antigens with normal early precursor B cells. We have studied here the role of Fas/APO-1 (CD95) antigen on leukaemic precursor B cell line growth and survival, and the modulation of its effects by signals involved in normal early B cell development. Four ALL cell lines representative of the early steps of B cell differentiation are shown to express surface Fas/APO-1 (CD95) antigen and to undergo apoptosis in the presence of anti-Fas cross-linking antibodies. This effect is strongly enhanced when pre-B, but not pro-B cells, are pretreated with IL-7 but not with IL-2, IL-3, IL-4 or IL-10. Furthermore, pre-B cell death induced by anti-Fas antibodies in combination with IL-7 is increased upon pre-B receptor but not CD19 cross-linking. Bcl-2 and Bax protein expression is not influenced by IL-7 or pre-BR stimulation in either pro-B or pre-B cell lines. These results indicate that signals involved in normal early B cell development can modulate the Fas (CD95)-mediated apoptosis of leukaemic precursor B cells.

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Interleukin 7 receptor ligation stimulates tyrosine phosphorylation, inositol phospholipid turnover, and clonal proliferation of human B-cell precursors.

Abstract: ABSTRACT

Cited by 85 publications

References 33 publications

E2A expression, nuclear localization, and in vivo formation of DNA- and non-DNA-binding species during B-cell development.

E2A expression, nuclear localization, and in vivo formation of DNA- and non-DNA-binding species during B-cell development.

Common elements in interleukin 4 and insulin signaling pathways in factor-dependent hematopoietic cells.

IL-7 sensitizes human pre-B cells but not pro-B cells to Fas/APO-1 (CD95)-mediated apoptosis

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