Absence of functional EpoR expression in human tumor cell lines

Swift, Susan; Ellison, Aaron R.; Kassner, Paul D.; McCaffery, Ian; Rossi, John M.; Sinclair, Angus M.; Begley, C. Glenn; Elliott, Steven

doi:10.1182/blood-2009-10-248674

Cited by 91 publications

(117 citation statements)

References 41 publications

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“…8 Using a sensitive and specific monoclonal antibody (A82), and semi-quantitative western blotting with whole-cell lysates, scientists at Amgen recently demonstrated absence or low expression of EpoR protein (o100 EpoR dimers per cell) in 54 human tumor cell lines, whereas 7 other nonerythroid cell lines expressed between 400 and 3200 EpoR dimers per cell. 9 However, this study did not examine EpoR levels in myeloma cell lines or primary tumor cells.…”

Section: Evaluating Surface Erythropoietin Receptor In Multiple Myelomamentioning

confidence: 97%

“…9 First, we compared the specificity of FAB307P and A82 in the erythroid cell line, OCIM1, using shRNAs to generate sub-clones that express a 1% bovine serum albumin, 0.02% sodium azide, 250 mg/ml human immunoglobulin G (IgG), cells were incubated for 30 min on ice with 1 mg/ml FAB307P, a phycoerythrin (PE) conjugate, or 0.5 mg/ml A82. Cells stained with A82 were subsequently incubated for 30 min on ice with anti-rabbit IgG-PE (1 to 10 dilution, 111-116-144, Jackson Immunoresearch, West Grove, PA, USA).…”

Section: Evaluating Surface Erythropoietin Receptor In Multiple Myelomamentioning

confidence: 99%

“…range of EpoR levels (Mission shRNA system, Sigma Aldrich, St Louis, MO, USA). COLO677 cells 9 and Epo-dependent UT7EPO cells provided negative and positive controls, respectively. This experiment revealed that both FAB307P and A82 antibodies were sensitive and specific for detecting surface EpoR protein levels in this panel of cell lines (Figure 1a).…”

Section: Evaluating Surface Erythropoietin Receptor In Multiple Myelomamentioning

confidence: 99%

“…6 In view of these considerations, we decided to investigate the recovery of thymic function in 33 patients given Haplo-HSCT, including 27 treated for hematological malignancies, using signal joint (sj) and beta T-cell receptor excision circles (TRECs). 7,8 These tools have already shown to be able to provide useful information in studies addressing the issues of aging, HIV infection and HSCT 9 but not yet in the context of the risk of leukemia relapse after HSCT.…”

Section: Conflict Of Interestmentioning

confidence: 99%

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Evaluating surface erythropoietin receptor in multiple myeloma

et al. 2012

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In conclusion, our analysis in acute leukemia revealed mutations in the histone-modifying enzymes recently identified to be altered in other cancers, particularly UTX in ALL and MLL2 in AML, although not at a high incidence. Important to note is that UTX and MLL2 are part of the same protein complex and both MLL2 and UTX mutations may lead to similar phenotypic consequences in cancer cells. Also, MLL2 was not fully sequenced in our analysis, leaving open the possibility of additional mutations in AML. Nevertheless, our findings warrant further analyses within larger studies and most likely more comprehensive studies based on targeted or whole genome/exome next-generation sequencing approaches. Of interest, most of the UTX mutations observed in our study were found in clinically defined high-risk patients and at least 1 of those patients (05-046) eventually relapsed. Therefore, this observation might be of particular interest with regard to potential epigenetic treatment approaches, although the exact mechanisms of transformation in UTX-mutated ALL remain to be elucidated.

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Section: Evaluating Surface Erythropoietin Receptor In Multiple Myelomamentioning

confidence: 97%

Section: Evaluating Surface Erythropoietin Receptor In Multiple Myelomamentioning

confidence: 99%

Section: Evaluating Surface Erythropoietin Receptor In Multiple Myelomamentioning

confidence: 99%

Section: Conflict Of Interestmentioning

confidence: 99%

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Evaluating surface erythropoietin receptor in multiple myeloma

et al. 2012

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“…Swift et al [9] found that EpoR protein was barely detectable in 66 human tumor cell lines and EpoR signaling in response to rhEPO was not detected in non-erythroid cells. In another related study, surface EpoR was not detectable on the surface of endothelial, cardiac, neuronal or renal cells and there was no evidence of intracellular signaling induced by erythropoiesis-stimulating agents (ESA) despite the addition of very high doses of rhEPO [10].…”

Section: Epo and Epo Variantsmentioning

confidence: 99%

Erythropoietic neuroprotection: Holy Grail or potential to fail?

2011

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In this issue of Intensive Care Medicine, Simon et al. [1] report that pretreatment with a carbamylated erythropoietin fusion protein (cEPO-FC) is as effective as recombinant human EPO (rhEPO) in ameliorating spinal cord injury in a well-established porcine model of acute spinal cord ischemia and reperfusion. This new fusion protein contains two rhEPO molecules connected by the Fc region of human IgG 1 . Subsequent carbamylation of the EPO molecule is thought to improve the cytoprotective effects, while reducing side effects including hypertension and thrombosis [2]. EPO and EPO variantsSince the human EPO gene was cloned in 1985, several variants of the EPO molecule have been developed to improve its pharmacokinetic and pharmacodynamic characteristics and to separate its hemopoietic and neuroprotective properties [3]. Epoietin alpha and beta are rhEPOs and have minimal differences in their structure. A variety of EPO derivatives, including cEPO-FC, which target the erythropoietin receptor (EpoR), and mimetic compounds (such as EPO-peptide AB, helix B peptide and hematide) have been developed. Darbepoietin alpha is a hyperglycosylated analogue of EPO with a four-to fivefold lower erythropoietin receptor binding activity but a threefold longer serum half-life. Epoietin delta has been produced in a human cell line and has a human-type glycosylation pattern. CERA is a PEGylated form of epoietin beta with a long in vivo half-life. In addition, there are alternative means of enhancing endogenous EPO translation by preventing hypoxia-inducible factor-a degradation or GATA2 inhibition, thereby inducing endogenous EPO gene expression.

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Hematopoietic Growth and Coagulation Factors

Ho¹,

Gibaldi²

2013

Biotechnology and Biopharmaceuticals

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Absence of functional EpoR expression in human tumor cell lines

Cited by 91 publications

References 41 publications

Evaluating surface erythropoietin receptor in multiple myeloma

Evaluating surface erythropoietin receptor in multiple myeloma

Erythropoietic neuroprotection: Holy Grail or potential to fail?

Hematopoietic Growth and Coagulation Factors

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