The aim of this study was to evaluate the quality of residual liquid-based preparation (LBP) sample after cytopathologic diagnosis. Cervical swab, body fluid, and thyroid fine-needle aspiration (FNA) samples preserved in ThinPrep PreservCyt solution were tested. Samples kept frozen at -80 °C and stored at room temperature were tested 12 months after the initial sample collection. Gel electrophotography of GAPDH multiplex PCR, RNA integrity number (RIN) values obtained from Agilent bioanalyzer, cytomorphologic changes, and immunohistochemical staining (cytokeratin, thyroid transcription factor-1 (TTF-1), and D2-40) were used for the evaluation of sample quality. All available samples showed successful amplification products in multiplex PCR. However, RNAs in all residual samples were degraded with low RIN values (RIN < 4). RIN values decreased rapidly when samples were stored at room temperature in LBP medium. Cytomorpholoic evaluation and immunohistochemical staining results revealed no change regardless of storage time or storage temperature. In conclusion, RNAs stored in LBP medium degraded quickly at room temperature. Residual alcohol-based LBP cytologic specimens stored at -80 °C and room temperature showed no change in DNA quality, cytomorphology, and immunoreactivity during at least one year of storage.
Several peptides, such as epidermal growth factor (EGF), heregulin (HRG) and transforming growth factor alpha (TGFα), are ligands for EGFR family. Heregulin beta 1 (HRG-ß1) binds to ErbB-3 and-4 and plays important roles in the proliferation and tumorigenesis of breast cancer cells. We investigated proteins through which HRG treatment affects matrix metalloproteinase (MMP)-9 activity. Breast cancer cell lines, including SK-Br3, MCF-7 and MDA-MB-231, were treated with HRG-ß1. After 24 h, the activity and expression levels of MMP-9 were increased, but MMP-2 activity was not changed. The increasing rates of MMP-9 activity and expression were most prominent in the SK-Br3 cell line. Upon treatment of SK-Br3 cells with HRG-ß1, phosphorylation of Akt was increased showing a peak at 30 min after treatment, and the level decreased after 6 h. The expression levels of Akt were not changed upon HRG-ß1 treatment. Phosphorylation of extracellular signal-regulated kinase 1/2 (ERK-1/2), downstream molecules of Akt, was also increased by HRG-ß1 treatment. Pretreatment of LY294002, PI3K inhibitor, or PD98059, MAPK inhibitor, partially blocked the heregulin-induced MMP-9 activity. Furthermore, MMP-9 was found to be secreted in human breast cancer tissues. The present results suggest that Akt and MAPK mediate HRG-ß1 signaling to MMP-9.
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