Expression levels of hsc70 and hsp60 are developmentally regulated during B‐cell maturation and not associated to childhood c‐ALL at presentation or relapse

Wehner, Peder Skov; Nielsen, Bendt; Hokland, Marianne

doi:10.1034/j.1600-0609.2003.00107.x

Cited by 12 publications

(12 citation statements)

References 56 publications

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“…Our study revealed significantly higher Hsp60 gene expression in the peripheral blood of patients, at the time of leukemia diagnosis, compared with healthy controls. Our gene expression data agrees with the observations of Wehner et al [37] who demonstrated that Hsp60 protein expression did not differ between bone marrow samples of pediatric patients during onset or relapse of c-ALL and healthy controls. Contrary to the findings of Wehner et al [37], Emura et al [38] found a positive association between the level of intrinsic expression of Hsp60 and an unfavorable prognosis for newly diagnosed patients with AML.…”

Section: Discussionsupporting

confidence: 95%

Heat-shock protein expression in leukemia

et al. 2010

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Heat-shock proteins (Hsps) are thought to play a role in the development of cancer and to modulate tumor response to cytotoxic therapy. In this study, Hsp27, Hsp60, Hsp90α, and HspBP1 gene expression was investigated in human leukemia cell lines as well as in leukemia cells derived from patients with the onset of the disease. Hsp70 membrane expression and expression of Hsp27, Hsp60, Hsp70, Hsp90α, and HspBP1 genes were also tested in samples from leukemia patients. Relative Hsps gene expression was examined in human leukemia cell lines and also in patients, using real-time quantitative reverse-transcriptase polymerase chain reaction (RT-PCR). Hsp70 cell surface expression was studied in patients with leukemia onset using flow cytometry. All tested cell lines showed significantly increased expression of Hsp60, Hsp90α, and HspBP1 genes compared with a cohort of healthy controls; additionally there was increased Hsp27 expression except for Jurkat and CCRF cells. Significantly higher gene expression of Hsp27, Hsp60, Hsp90α, and HspBP1 was observed in the peripheral blood of patients compared with bone marrow and healthy control samples, while Hsp70 expression was without any significant difference among cohorts. Hsp70 cell surface expression was found on defrosted and cultured leukemia cells but not on unprocessed biological samples from patients. Leukemia cells showed a heterogeneous pattern of Hsp gene expression among leukemia cell lines as well as in peripheral blood and bone marrow of patients.

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Section: Discussionsupporting

confidence: 95%

Heat-shock protein expression in leukemia

et al. 2010

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“…Studies conducted in lymphocytes isolated from human peripheral blood mononuclear cells reported that Hsc70 expression regulates the development of B lymphocytes and is a potential target of tyrosine kinase activity in T lymphocytes. It has been associated with increases in inflammation and susceptibility to autoimmunity as well as regulating the myocardial immune response [37][38][39][40].…”

Section: Co-chaperoningmentioning

confidence: 99%

An analysis of the phosphoproteome of immune cell lines exposed to the immunomodulatory mycotoxin deoxynivalenol

Costa

Keen

Wild

et al. 2011

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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a b s t r a c t a r t i c l e i n f oThe mycotoxin deoxynivalenol (DON) commonly contaminates cereal grains. It is ubiquitous in the Western European diet, although chronic, low-dose effects in humans are not well described, but immunotoxicity has been reported. In this study, two-dimensional gel electrophoresis was used to identify phosphoproteomic changes in human B (RPMI1788) and T (Jurkat E6.1) lymphocyte cell lines after exposure to modest concentrations of DON (up to 500 ng/mL) for 24 h. Proteins identified as having altered phosphorylation state post-treatment (C-1-tetrahydrofolate synthase, eukaryotic elongation factor 2, nucleoside diphosphate kinase A, heat shock cognate 71 kDa protein, eukaryotic translation initiation factor 3 subunit I and growth factor receptor-bound protein 2) are involved in regulation of metabolic pathways, protein biosynthesis and signaling transduction. All exhibited a greater than 1.4-fold change, reproducible in three separate experiments consisting of 36 gels in total. Flow cytometry validated the observations for eukaryotic elongation factor 2 and growth factor receptor-bound protein 2. These findings provide further insights as to how low dose exposure to DON may affect human immune function and may have potential as mechanismbased phosphoprotein biomarkers for DON exposure.

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“…42) Flot2 protein is assembled in a complex that contains activated glycosylphosphatidylinositol-linked cell adhesion molecules. Over expression of flot2 resulted in induction of filopodia.…”

Section: Immunohistochemical Analysis Of Ezrin In Rat Placentamentioning

confidence: 99%

Differential Expression of Ezrin and CLP36 in the Two Layers of Syncytiotrophoblast in Rats

Higuchi

Iizasa

Sai

et al. 2010

Biological & Pharmaceutical Bulletin

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The syncytiotrophoblast in the placenta serves as an interface for efficient maternal-fetal exchange of nutrients, metabolites and xenobiotic compounds, and membrane transport processes play pivotal roles in efficient uptake of certain compounds and in exclusion of others; this is referred to as the blood-placenta barrier. 1,2) In humans, the syncytiotrophoblast is derived from cell fusion of the progenitor cytotrophoblast and consists a polar single epithelium. The apical and basal plasma membranes of the syncytiotrophoblast face the maternal blood and the endothelial cells of the fetal blood vessels, respectively. Specific localization of transporters in the apical and the basal plasma membranes of the syncytiotrophoblast is important for plancental function in terms of vectorial transport of substrates. For example, ATP-binding cassette transporters, such as P-glycoprotein (P-gp) and breast cancer resistance protein, are localized in the apical membrane of the syncytiotrophoblast, where they restrict the entry of xenobiotics, including digoxin, saquinavir, vinblastine, topotecan and mitoxantrone.3) On the other hand, organic anion transporting polypeptide 2B1 is localized in the basal membrane of the syncytiotrophoblast and mediates uptake of dehydroepiandrosterone sulphate from fetal blood to placenta. 4)The postsynaptic density 95 (PSD-95)/Discs-large/zonula occludens-1 (ZO-1) (PDZ) domain-containing scaffold proteins, such as PDZ domain containing 1 (PDZK1) and Na ϩ /H ϩ exchanger regulatory factor 1 (NHERF1) , play a role in the association and functional regulation of organic anion transporters in the apical membranes of the renal proximal epithelial cells.5) It has also been reported that PDZK1 functions as a regulator for oligopeptide transporter (PEPT) 2 and organic cation/carnitine transporter 2, through direct interaction with their C-termini. 6,7) However, the mechanisms that control the polar distribution of proteins in the syncytiotrophoblast are still unclear.In mouse and rat, however, the labyrinthine part of the placenta is the principal site of maternal-fetal exchange. The labyrinthine wall, which lies between the maternal blood space and fetal vessels, is composed of three trophoblast layers, 1,[8][9][10] i.e., the porous cytotrophoblast layer, and the maternal-side and fetal-side syncytiotrophoblast layers (also called SynI and SynII, respectively). It is suggested that connexin 26 gap-junctional channels and transporters allow diffusion of nutrients between the two syncytiotrophoblast layers.11-13) Therefore, it is considered that the apical membrane of SynI and the basal membrane of SynII correspond to the apical and basal membranes of human syncytiotrophoblast, respectively, although the physiological role of the double epithelial layers, in contrast to the single epithelial cell layer in humans, remains unclear.We established conditionally immortalized rat syncytiotrophoblast cell lines, TR-TBT 18d-1 and TR-TBT 18d-2 from The syncytiotrophoblast, which regulates maternal-fetal transfer ...

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Expression levels of hsc70 and hsp60 are developmentally regulated during B‐cell maturation and not associated to childhood c‐ALL at presentation or relapse

Cited by 12 publications

References 56 publications

Heat-shock protein expression in leukemia

Heat-shock protein expression in leukemia

An analysis of the phosphoproteome of immune cell lines exposed to the immunomodulatory mycotoxin deoxynivalenol

Differential Expression of Ezrin and CLP36 in the Two Layers of Syncytiotrophoblast in Rats

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