Selective growth response to IL‐3 of a human leukaemic cell line with megakaryoblastic features

Avanzi, Gian Carlo; Lista, Patrizia; Giovinazzo, Bruna; Miniero, R; Saglio, Giuseppe; Benetton, G; Coda, Renato; Cattoretti, Giorgio; Pegoraro, Luigi

doi:10.1111/j.1365-2141.1988.tb02374.x

Cited by 285 publications

(116 citation statements)

References 32 publications

(9 reference statements)

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“…We therefore performed virus-binding assays to investigate the ability of our SCF-eco viruses to bind to the c-kit-expressing cell line, MO7e. 22 As shown in the left panel of Figure 2A, anti-SU monoclonal antibody did not detect binding of normal ecotropic retrovirus to MO7e cells. Using SCF-eco virus, however, we observed a clear shift in fluorescence (Figure 2A right), indicating that the engineered virus was bound to the c-kit ϩ target cells.…”

Section: Redirection Of Retroviral Bindingmentioning

confidence: 80%

“…TF-1 was supplemented with 1 ng/mL granulocyte-macrophage colonystimulating factor (GM-CSF). The human megakaryoblastic leukemia cell line MO7e 22 was maintained in RPMI supplemented with 20% FCS and 10 ng/mL GM-CSF or shifted into medium without GM-CSF but containing 100 ng/mL SCF for experiments where c-kit expression was down-regulated.…”

Section: Human Cell Linesmentioning

confidence: 99%

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Targeted retroviral transduction of c-kit+ hematopoietic cells using novel ligand display technology

Chandrashekran

Gordon

Casimir

2004

Blood

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Gene therapy for a wide variety of disorders would be greatly enhanced by the development of vectors that could be targeted for gene delivery to specific populations of cells. We describe here high-efficiency targeted transduction based on a novel targeting strategy that exploits the ability of retroviruses to incorporate host cell proteins into the surface of the viral particle as they bud through the plasma membrane. Ecotropic retroviral particles produced in cells engineered to express the membrane-bound form of stem cell factor ( IntroductionThe development of retroviral vectors that are targeted to transduce only specific cell types has been the goal of many investigators working in the field of gene therapy. [1][2][3][4][5] The availability of such vectors would revolutionize the field, opening up new avenues for gene therapy in acquired and inherited disorders by enabling in vivo delivery of therapeutic molecules to specific populations of target cells. Novel approaches to drug delivery and for use in vaccines also become possible through display of molecules on the retroviral surface. Over a period of around a decade, however, this goal has proven highly elusive. Virtually all attempts to target specific cell types have logically focused on modification of the retroviral envelope protein, as this complex glycoprotein is established to determine viral host range and facilitate virus entry though membrane fusion. 2,4,5 These modifications can be the simple substitution of the envelope protein for one from another retrovirus or other enveloped virus, such as vesicular stomatitis virus (VSV) 6 , a process referred to as pseudotyping. 2 More recently, attempts have been made to deliberately engineer envelope proteins to redirect their binding to new cell surface molecules. 4 This has involved making N-terminal extensions, insertions, or replacements to regions of the envelope protein. Commonly used modifications have been incorporation of growth factor-binding regions [7][8][9][10][11][12] or the addition of single-chain antibodies. [13][14][15][16][17] While many of these modifications have successfully redirected viral binding, this has invariably been achieved at the expense of infectivity to the extent that targeted binding actually inhibited viral entry. This property has actually been used to advantage in an approach referred to as "inverse targeting." 10,18 A number of reports, however, have indicated that low levels of targeted transduction may be achievable by coexpression of an ecotropic envelope in conjunction with the modified envelope protein. 7,9,16,19 To circumvent the problems associated with envelope modification, we have developed an alternative strategy, exploiting the natural budding mechanism of the virus to insert new binding ligands into the viral surface. We describe here successful and efficient specific targeting of transduction to human cells expressing stem cell factor (SCF) receptor (c-kit) by ecotropic retroviruses bearing surface stem cell factor. Materials and methods Cytokine...

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Section: Redirection Of Retroviral Bindingmentioning

confidence: 80%

Section: Human Cell Linesmentioning

confidence: 99%

Targeted retroviral transduction of c-kit+ hematopoietic cells using novel ligand display technology

Chandrashekran

Gordon

Casimir

2004

Blood

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“…We studied the properties of our HD-Ad5/35 vectors in Mo7e cells, a growth-factor dependent CD34 + erythroleukemia cell line that is often used as a model for erythroid progenitor cells [27]. Cells were infected with HD-Ad5/35.Tet-1 and HD-Ad5/35.Tet-2 at increasing MOIs, and the percentage of GFP expressing cells as well as mean GFP fluorescence levels were measured 24 hours later in the presence and absence of 100 ng/ml Dox (Fig.3).…”

Section: Resultsmentioning

confidence: 99%

Tightly regulated gene expression in human hematopoietic stem cells after transduction with helper-dependent Ad5/35 vectors

Wang

Cao

Wohlfahrt

et al. 2008

Experimental Hematology

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Objective-Inducible and transient expression of transcription factors, growth factors, or mitogenic factors can be used to influence proliferation or differentiation of hematopoietic progenitor/stem cells (HSCs). Furthermore, transient expression of proteins with site-specific endonuclease activity, potentially, can support targeted integration of exogenous transgenes into specific sites in the genome, a task that is currently a focus in development of gene therapy vectors. Methods-We

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“…Indeed, it has been shown that erythroid or megakaryocytic differentiation markers are expressed in UT-7 cells stimulated by Epo (49) or by thrombopoietin (50), respectively. TF-1 and HCD57 cells seem to be strictly committed in the erythroid differentiation pathway, whereas Mo7E cells exhibit megakaryocytic characteristics (38,39,41,51). T3Cl2 cells are Friend virus-transformed cells that correspond to erythroid cells blocked at the colony-forming unit erythroid/proerythroblast stage (52).…”

Section: Discussionmentioning

confidence: 99%

“…Before each experiment, the cells were serum-and growth factor-deprived by incubation overnight in Iscove's modified Dulbecco's medium (Life Technologies, Inc., catalog number 31980-022) containing 0.1% deionized bovine serum albumin. HCD57 cells (38), Mo7E cells (39), and TF-1 cells (40,41) were cultivated in ␣-minimal essential medium containing 5% fetal calf serum and complemented with 2 units/ml Epo (HCD57) or 2.5 ng/ml GM-CSF (Mo7E and TF-1). BaF3 (42) and FDCP-1 (43) cells were cultivated in the same medium complemented with 2.5% WEHI-conditioned medium as a source of IL-3.…”

Section: Methodsmentioning

confidence: 99%

Erythropoietin Induces the Tyrosine Phosphorylation of Insulin Receptor Substrate-2

Verdier

Chrétien

Billat

et al. 1997

Journal of Biological Chemistry

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In this report, we demonstrate that insulin receptor substrate-2 (IRS-2) is phosphorylated on tyrosine following treatment of UT-7 cells with erythropoietin. We have investigated the expression of IRS-1 and IRS-2 in several cell lines with erythroid and/or megakaryocytic features, and we observed that IRS-2 was expressed in all cell lines tested. In contrast, we did not detect the expression of IRS-1 in these cells. In response to erythropoietin, IRS-2 was immediately phosphorylated on tyrosine, with maximal phosphorylation between 1 and 5 min. Tyrosine-phosphorylated IRS-2 was associated with phosphatidylinositol 3-kinase and with a 140-kDa protein that comigrated with the phosphatidylinositol- Insulin receptor substrate-1 (IRS-1) 1 is a major substrate of the IGF-1 and insulin receptors (1). IRS-1 is a hydrophilic protein with a theoretical molecular mass of 131 kDa that migrates between 160 and 185 kDa on SDS-polyacrylamide gel electrophoresis partially because of a high serine phosphorylation state (2, 3). IRS-1 contains a pleckstrin homology domain, a PTB domain, and at least 20 potential tyrosine phosphorylation sites including nine YXXM motifs that are consensus binding sites for the SH2 domains of the regulatory subunit (p85) of PI 3-kinase (4). IRS-1 binds to the tyrosine-phosphorylated IGF-1 and insulin receptors through its PTB domain and becomes a docking protein for signaling proteins such as PI 3-kinase, Grb2, PTP1D, and Nck after tyrosine phosphorylation (5). Moreover, a recent report shows that the pleckstrin homology domain could also be involved in the association of IRS-1 with the insulin receptor (6). More recently, a second IRS protein was identified that was designated IRS-2 (7). This protein corresponds to the previously identified 4PS protein (for IL-4-induced phosphotyrosine substrate) (8, 9). IRS-2 exhibits a high structural similarity to IRS-1, with a strong conservation of the PTB and pleckstrin homology domains. Moreover, tyrosine phosphorylation sites shown to bind PI 3-kinase, Grb2, and PTP1D in IRS-1 are also conserved in IRS-2.Not only insulin and IGF-1 receptors, but also several cytokine and interferon receptors can induce tyrosine phosphorylation of IRS-1 or IRS-2 (9 -18). IRS-1 and IRS-2 activation by IL-4 is well documented. Indeed, it has been shown that IRS-1 and IRS-2 bind to a peptidic sequence of the activated IL-4 receptor with a typical NPXY PTB domain-binding motif (19), and IRS-1 or IRS-2 expression appears to be required for IL-4-induced mitogenesis (10). However, other cytokine receptors that induce the tyrosine phosphorylation of IRS-1 and IRS-2 do not possess typical PTB domain-binding motifs, and the mechanism of IRS-1 and IRS-2 activation by these receptors remains unknown.The erythropoietin (Epo) receptor also belongs to the cytokine receptor family (20,21). Epo binding to its receptor activates the receptor-associated JAK2 tyrosine kinase (22) and induces the tyrosine phosphorylation of the Epo receptor (23-26) and other proteins. Several intracellular signa...

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Selective growth response to IL‐3 of a human leukaemic cell line with megakaryoblastic features

Cited by 285 publications

References 32 publications

Targeted retroviral transduction of c-kit+ hematopoietic cells using novel ligand display technology

Targeted retroviral transduction of c-kit+ hematopoietic cells using novel ligand display technology

Tightly regulated gene expression in human hematopoietic stem cells after transduction with helper-dependent Ad5/35 vectors

Erythropoietin Induces the Tyrosine Phosphorylation of Insulin Receptor Substrate-2

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