Molecular evidence for transferrin receptor 2 expression in all FAB subtypes of acute myeloid leukemia

Κollia, Panagoula; Σαμαρά, Μαρία; Stamatopoulos, Kostas; Belessi, Chrysoula; Stavroyianni, Niki; Tsompanakou, Aliki; Athanasiadou, Anastasia; Vamvakopoulos, Nicholas C.; Laoutaris, Nikos; Anagnostopoulos, Achilles; Fassas, Αthanasios

doi:10.1016/s0145-2126(03)00100-0

Cited by 24 publications

(20 citation statements)

References 8 publications

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“…Transferrin receptor (TfR), a transmembrane glycoprotein, expresses on the surface of rapidly proliferative cells and in tumor cells of various kinds such as hepatoma carcinoma cells and leukemia cells [1][2][3][4][5][6][7] . Several studies have demonstrated that TfR was expressed more abundantly in malignant tissues than in their healthy counterparts [2,[4][5][6][7][8] .…”

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confidence: 99%

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Preparation and identification of scFv and bsFv against transferrin receptor

Liu

Xiao

Zhou

et al. 2008

J. Huazhong Univ. Sci. Technol. [Med. Sci.]

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To obtain single chain variable fragment (scFv) and bivalent single chain variable fragment (bsFv) against transferrin receptor, up-stream and down-stream primers were designed according to the complementary sequences of FR1 region of variable heavy (VH) and FR4 of variable light (VL), respectively, which contained inter-linker G4S and the restriction endonuclease SfiI, AscI and NotI. Two pieces of scFv fragments were first amplified through PCR and then inserted into plasmid pAB1, which could express scFv protein once induced by IPTG in the host bacteria. To express scFv and bsFv, E. coli TG1 was cultured in LB broth and was induced by IPTG. The restriction enzyme digestion map and DNA sequencing demonstrated that scFv and bsFv genes were successfully inserted into the expression plasmid. SDS-PAGE and Western blotting revealed the protein band at 35kD and 60kD, which were consistent with the molecular weight of scFv and bsFv respectively. Flow cytometry showed that scFv and bsFv harbored the specific binding activity with TfR expressed in various tumor cells, and the avidity of bsFv was higher than that of the parent scFv.

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confidence: 99%

“…Several studies have demonstrated that TfR was expressed more abundantly in malignant tissues than in their healthy counterparts [2,[4][5][6][7][8] . The serum soluble transferrin receptor (sTfR) levels in the hepatoma and haematologic malignancies were significantly increased [9] .…”

mentioning

confidence: 99%

Preparation and identification of scFv and bsFv against transferrin receptor

Liu

Xiao

Zhou

et al. 2008

J. Huazhong Univ. Sci. Technol. [Med. Sci.]

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“…Total cellular RNA isolation, cDNA preparation (after DNAse treatment), and RT-PCR amplification of cDNA sequences corresponding to the syncytin 1, syncytin 2, ASCT1 and ASCT2 mRNA transcripts were performed as previously described [23]. Qualitative assessment of isolated RNA was carried out, both spectrophotometrically and via 2% agarose gel electrophoresis.…”

Section: Qualitative Rt-pcr Assessment Of Syncytin 1 2 Asct1 and Ascmentioning

confidence: 99%

Syncytins expression in cultured trophoblast cells according to differentiation status

et al. 2011

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“…In contrast, TFR1 mRNA expression has been detected in all the lymphoid, myeloid and erythroid cell lines tested; the highest being observed in OCI-M1 erythroid cells. TFR2 mRNA was also detected in normal, early erythroid precursors and in primary myeloid leukemic blasts, especially derived from FAB M6 subtype [28,59,60]. At the level of protein synthesis, expression of TFR2 in normal erythroid cells was initially demonstrated by an immunohistochemical analysis using a polyclonal antibody [59]; however, it was subsequently shown by Western blot that TFR2 protein was not expressed at any stage of normal erythroid differentiation [61].…”

Section: Expression Pattern and Tissue Distributionmentioning

confidence: 99%

Transferrin receptor 2 is emerging as a major player in the control of iron metabolism

2007

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Our knowledge of mammalian iron metabolism has advanced dramatically over recent years. Iron is an essential element for virtually all living organisms. Its intestinal absorption and accurate cellular regulation is strictly required to ensure the coordinated synthesis of the numerous iron-containing proteins involved in key metabolic processes, while avoiding the uptake of excess iron that can lead to organ damage. A range of different proteins exist to ensure this fine control within the various tissues of the body. Among these proteins, transferrin receptor (TFR2) seems to play a key role in the regulation of iron homeostasis. Disabling mutations in TFR2 are responsible for type 3 hereditary hemochromatosis (Type 3 HH). This review describes the biological properties of this membrane receptor, with a particular emphasis paid to the structure, function and cellular localization. Although much information has been garnered on TFR2, further efforts are needed to elucidate its function in the context of the iron regulatory network.

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Molecular evidence for transferrin receptor 2 expression in all FAB subtypes of acute myeloid leukemia

Cited by 24 publications

References 8 publications

Preparation and identification of scFv and bsFv against transferrin receptor

Preparation and identification of scFv and bsFv against transferrin receptor

Syncytins expression in cultured trophoblast cells according to differentiation status

Transferrin receptor 2 is emerging as a major player in the control of iron metabolism

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