Evangelisches Krankenhaus Bielefeld GmbH

Bielefeld, Germany

Evangelisches Krankenhaus Bielefeld GmbH

Bielefeld, Germany
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Zimmermann M.,Charité - Medical University of Berlin | Kappert K.,Charité - Medical University of Berlin | Stan A.C.,Evangelisches Krankenhaus Bielefeld GmbH
Neuroscience Letters | Year: 2010

Aim of this study was to examine the dipeptide transport of β-Ala-Lys-Ne{open}-AMCA in the human glioma cell line U373-MG and its potential regulation by diverse hormones and culture media. A mixed glial primary cell culture of the newborn rat served as reference cell system. β-Ala-Lys-Ne{open}-AMCA (β-Ala-Lys-Ne{open}-7-amino-4-methyl-coumarin-3-acetic acid) is a highly specific reporter substrate to investigate the dipeptide transport system PepT2. We were able to demonstrate that U373-MG cells express PepT2-mRNA and translocate β-Ala-Lys-Ne{open}-AMCA via PepT2 into the cytoplasm. Previous results demonstrated that β-Ala-Lys-Ne{open}-AMCA specifically accumulates in differentiated and dedifferentiated astrocytes but neither in differentiated nor dedifferentiated oligodendrocytes and in neurons. U373-MG cells were incubated with estradiol, testosterone, thyronine, dexamethasone, dibutyryl cyclic adenosine monophosphate and tetradecanoylphorbol acetate in order to detect potential substance-dependent changes in dipeptide uptake. There was no significant increase or decrease of β-Ala-Lys-Ne{open}-AMCA-uptake after stimulation. Northern blot analyses confirmed that PepT2-mRNA is expressed in U373-MG and glial cells but showed no regulation of PepT2-mRNA expression in both cell types. Future investigations might offer the opportunity of an anti-tumor therapy with cytotoxic agents linked to a dipeptide-derivative such as β-Ala-Lys. © 2010 Elsevier Ireland Ltd.

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