ABSTRACT
In this work, LiYF4:Yb0.25 3+/Er0.01 3+/Tm0.01 3+/Ho0.01 3+@LiYF4:Yb0.2 3+ upconverting nanoparticles (UCNP) were used as luminescent materials for the preparation of molecular imprinting polymer nanocomposites. Three luminescent molecularly imprinted polymer (MIP) nanocomposites were prepared by in situ polymerization. The relationship between the functional monomers, templates, and upconversion nanoparticles was investigated. Two hydrophilic monomers (acrylic acid (AA) and acrylamide (AAm)) and one hydrophobic monomer (N-tert-butylacrylamide (TBAm)) were employed as functional monomers, while one amino acid (cysteine) and two proteins (albumin and hemoglobin) were employed as the templates to investigate the effect of their interaction with LiYF4:Yb3+/Er3+/Ho3+/Tm3+@LiYF4:Yb3+ core/shell UCNPs on the polymerization process, luminescence properties, and adsorption capacity. The results showed that the UCNPs were embedded in the polymeric matrix to form an irregular quasimicrospherical UCNPs@MIP with diameters ranging from several hundred nanometers to several micrometers depending on the functional monomer. The quenching effect was more pronounced for the adsorption of hemoglobin with UCNPs@MIP compared to cysteine and albumin. In addition, the adsorption capacities of the AA- and AAm-made UCNPs@MIP were greater than those of TBAm-made UCNPs@MIP. The rebinding of the templates onto UCNPs@MIP was very fast and approached equilibrium within 30 min, indicating that the synthesized UCNPs@MIP can be employed as fluorescent probes to offer rapid detection of molecules.
ABSTRACT
The purpose of this study was to elucidate the function of protein kinase C (PKC) alpha in human hepatocellular carcinoma (HCC). Histoimmunopathologic techniques were used to determine the localization and/or expression of PKCalpha, phospho-mitogen-acrivated protein kinase (MEK) and multidrug resistance 1 (MDR1) in HCC biopsies. Expression of PKCalpha, phospho-MEK and MDR1 was significantly increased in the region of HCC location compared with the non-tumor location. The HCC tissues were classified as cytosolic type, where PKCalpha was deposited in the cytoplasm in > 50% of cells, or membranous type for others. The results showed that the higher expression levels of phospho-MEK and MDR1 in HCC location were significantly associated with those patients whose cells were of the membranous type. Moreover, the expression of MDR1 in HCC location was also significantly associated with the phospho-MEK, and was significantly higher in the patients with anti-HCV negative readings. The results indicate that elevated expression of MDR1 in HCC patients with non-HCV infection may be mediated through PKC signaling pathway.
Subject(s)
ATP Binding Cassette Transporter, Subfamily B, Member 1/metabolism , Carcinoma, Hepatocellular/metabolism , Hepatitis B/complications , Hepatitis C/complications , Liver Neoplasms/metabolism , Mitogen-Activated Protein Kinase Kinases/metabolism , Protein Kinase C-alpha/metabolism , Adult , Aged , Aged, 80 and over , Biopsy , Carcinoma, Hepatocellular/pathology , Carcinoma, Hepatocellular/virology , Cell Membrane/metabolism , Cytoplasm/metabolism , Female , Humans , Liver Neoplasms/pathology , Liver Neoplasms/virology , Male , Middle Aged , Retrospective Studies , Signal Transduction/physiologyABSTRACT
The purpose of this study was to elucidate the protein kinase C (PKC) alpha distribution in human hepatocellular carcinoma (HCC). The histoimmunopathologic technique was used to determine the localization and expression of PKCalpha in HCC biopsies. The HCC tissues were classified as cytosolic type (PKCalpha deposited in the cytoplasm in > 50% of cells) and membranous type for the remaining ones. There was a significant association of the membranous type with non-hepatitis C virus (HCV) infected patients. Moreover, the expression of PKCalpha in this type was significantly higher in HCC cells than that in the adjacent non-tumor liver cells. The result indicated that PKCalpha may play an important role in carcinogenesis of HCC patients with HBV infection and/or non-HCV infection.
Subject(s)
Carcinoma, Hepatocellular/enzymology , Liver Neoplasms/enzymology , Protein Kinase C-alpha/metabolism , Adult , Aged , Biopsy , Carcinoma, Hepatocellular/pathology , Female , Hepatitis B Surface Antigens/analysis , Hepatitis C/enzymology , Hepatitis C/immunology , Hepatitis C Antibodies/analysis , Humans , Immunohistochemistry , Liver Neoplasms/pathology , Male , Middle AgedABSTRACT
Variations in the activity of protein kinase C (PKC) have been observed in different types of tumors. Although these inconsistent findings may be attributed to the alterations of individual PKC isoforms, the effects of general anesthetic may not be neglected. In this study, biopsies and surgical specimens were obtained from patients with HCC, and the levels of PKCalpha were analyzed by immunohistochemistry. PKCalpha expression in biopsies was mainly revealed on the cell membrane of hepatocytes whereas that in the surgical specimens was in the cytosol and on the membrane. In both types of specimens, the PKCalpha level in HCC was significantly higher than that in the adjacent non-tumorous tissue. Moreover, the level of PKCalpha in biopsies was significantly higher than that in surgical specimens of the corresponding tissue type. These findings suggested that general anesthetics may significantly affect the expression of PKCalpha, and the effects of anesthetics should not be neglected in observations which were made only based on surgical specimens.
