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Biomedical subjects

A Nanbo

Publications and source records attributed to A Nanbo.

5 recordsLinked to original sources
PubMed2001

The role of EBERs in oncogenesis.

Epstein-Barr virus (EBV)-encoded small non-polyadenylated RNAs (EBERs) are the most abundant viral transcripts in latently EBV-infected cells. However, until recently, their roles in viral infection were totally unknown. It now appears that EBERs play a key role in maintaining the malignant phenotypes of Burkitt's lymphoma (BL) cells. The EBERs confer clonability in soft agarose, tumourigenicity in mice, and resistance to apoptosis against various stimuli in BL. Furthermore, EBERs induce transcription of interleukin-10, which acts as an autocrine growth factor of BL. These studies open the way toward the new concept that RNA molecules can act in oncogenesis.

Base Sequence↗
PubMed2001

Bactericidal/permeability-increasing protein promotes complement activation for neutrophil-mediated phagocytosis on bacterial surface.

The neutrophil bactericidal/permeability-increasing protein (BPI) has both bactericidal and lipopolysaccharide-neutralizing activities. The present study suggests that BPI also plays an important role in phagocytosis of Escherichia coli by neutrophils through promotion of complement activation on the bacterial surface. Flow cytometric analysis indicated that fluorescein-labelled E. coli treated with BPI were phagocytosed in the presence of serum at two- to five-fold higher levels than phagocytosis of the bacteria without the treatment. In contrast, phagocytosis of the fluoresceined bacteria with or without treatment by BPI did not occur at all in the absence of serum. The phagocytosis stimulated by BPI and serum was dose-dependent. The effect of BPI on phagocytosis in the presence of serum was not observed on Gram-positive bacteria (Staphylococcus aureus). Interestingly, the complement C3b/iC3b fragments were deposited onto the bacterial surface also as a function of the BPI concentration under conditions similar to those for phagocytosis. Furthermore, the BPI-promoted phagocytosis was blocked completely by anti-C3 F(ab')(2) and partially by anti-complement receptor (CR) type 1 and/or anti-CR type 3. These findings suggest that BPI accelerates complement activation to opsonize bacteria with complement-derived fragments, leading to stimulation of phagocytosis by neutrophils via CR(s).

Antimicrobial Cationic Peptides↗
PubMed1999

Lipopolysaccharide stimulates HepG2 human hepatoma cells in the presence of lipopolysaccharide-binding protein via CD14.

Lipopolysaccharide (LPS)-binding protein (LBP), an opsonin for activation of macrophages by bacterial LPS, is synthesized in hepatocytes and is known to be an acute phase protein. Recently, cytokine-induced production of LBP was reported to increase 10-fold in hepatocytes isolated from LPS-treated rats, compared with those from normal rats. However, the mechanism by which the LPS treatment enhances the effect of cytokines remains to be clarified. In the present study, we examined whether LPS alone or an LPS/LBP complex directly stimulates the hepatocytes, leading to acceleration of the cytokine-induced LBP production. HepG2 cells (a human hepatoma cell line) were shown to express CD14, a glycosylphosphatidylinositol-anchored LPS receptor, by both RT/PCR and flow cytometric analyses. An LPS/LBP complex was an effective stimulator for LBP and CD14 production in HepG2 cells, but stimulation of the cells with either LPS or LBP alone did not significantly accelerate the production of these proteins. The findings were confirmed by semiquantitative RT/PCR analysis of mRNA levels of LBP and CD14 in HepG2 cells after stimulation with LPS alone and an LPS/LBP complex. In addition, two monoclonal antibodies (mAbs) to CD14 (3C10 and MEM-18) inhibited LPS/LBP-induced cellular responses of HepG2 cells. Furthermore, prestimulation of HepG2 cells with LPS/LBP augmented cytokine-induced production and gene expression of LBP and CD14. All these findings suggest that an LPS/LBP complex, but not free LPS, stimulates HepG2 cells via CD14 leading to increased basal and cytokine-induced LBP and CD14 production.

Acute-Phase Proteins↗
PubMed1997

Lipopolysaccharide binding protein from normal human plasma purified with high efficiency.

Lipopolysaccharide (LPS)-binding protein (LBP) is an acute-phase plasma glycoprotein of 60 kDa which functions as an opsonin on activation of macrophages by bacterial LPS. The importance of LBP on the host defense against infection has been demonstrated. Human LBP has been purified from ascitic fluid or acute-phase serum. However, clinical samples often are not available, so we developed a method to purify LBP from normal plasma. The purification was accomplished by barium citrate precipitation, followed by three-step ion-exchange chromatography. The final step was Mono S cation-exchange chromatography, following Bio-Rex 70 and Mono Q chromatography, and it enabled the specific activity to increase overall 48,000-fold. This seems to be the first report of the use of Mono S column to purify LBP. The LBP obtained using these steps proved to be homogeneous by SDS-PAGE, Western blotting, and N-terminal sequence and amino acid composition analyses. The purification method established here will compensate when normal plasma with a low LBP content is available as the starting source.

Acute-Phase Proteins↗