The addition of heteroatoms to pristine
carbon quantum dots (CQDs)
change their structure and optical properties. In this study, fluorine
(F)- and chlorine (Cl)-doped CQDs are prepared by the one-step green
hydrothermal route from sodium fluoride, sodium chloride, urea, and
citric acid as the starting precursors. Microscopy analysis reveals
that the average size of these quantum dots is 5 ± 2 nm, whereas
the chemical study shows the existence of C–F and C–Cl
bonds. The produced F- and Cl-doped CQDs have fluorescence quantum
yields of 0.151 and 0.284, respectively, at an excitation wavelength
of 450 nm. Charge transfer resistance of F- and Cl-doped CQDs films
is 2 orders of magnitude higher than in the pristine CQD films. Transport
band gap of the doped CQDs is 2 eV bigger than that of pristine CQDs.
Radical scavenging activity shows very good antioxidant activity of
doped CQDs. Antibacterial testing reveals poor antibacterial activity
against Staphylococcus aureus and Escherichia coli. The F- and Cl-doped CQDs are successfully
used as fluorescent probes for cell imaging as shown by confocal microscopy.
Hypoxia is a phenomenon often arising in solid tumours, linked to aggressive malignancy, bad prognosis and resistance to therapy. Hypoxia-inducible factor-1 has been identified as a key mediator of cell and tissue adaptation to hypoxic conditions through transcriptional activation of many genes involved in glucose metabolism and other cancer-related processes, such as angiogenesis, cell survival and cell invasion. Cyclic adenosine 3′5′-monophosphate is one of the most ancient and evolutionarily conserved signalling molecules and the cAMP/PKA signalling pathway plays an important role in cellular adaptation to hypoxia. We have investigated possible new mechanisms behind hypoxic activation of the cAMP/PKA pathway. For the first time, we have shown that hypoxia induces transcriptional up-regulation of the system of adenylyl cyclases, enzymes responsible for cAMP production, in a panel of carcinoma cell lines of various origin. Our data prove functional relevance of the hypoxic increase of adenylyl cyclases VI and VII at least partially mediated by HIF-1 transcription factor. We have identified adenylyl cyclase VI and VII isoforms as mediators of cellular response to hypoxia, which led to the elevation of cAMP levels and enhanced PKA activity, with an impact on cell migration and pH regulation.
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