PubMed · 2908641
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
L E Spitler. 1988. Clinical studies: solid tumors.. https://doi.org/10.1007/978-1-4613-1083-9_28
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Aspergillus ochraceus contaminates agricultural products and produces nephrotoxic, carcinogenic ochratoxin A (OTA), posing severe food safety hazards. A dual-signal lateral flow immunochromatographic assay (dLFIA) based on ZrO₂@C nanoprobes was established for quantitative detection of A. ochraceus biomass. A novel monoclonal antibody (mAb 4B4) was prepared as the capture antibody to immobilize A. ochraceus mycelial lysate antigen on the test line, and a rabbit polyclonal antibody (pAb G2801) as the detection antibody to modify ZrO₂@C composites (synthesized via UiO-66 pyrolysis) into 200 nm colorimetric/photothermal nanoprobes. This dLFIA achieved limits of detection of 0.164 μg/mL (colorimetric) and 0.517 μg/mL (photothermal). This efficient and reliable method allows quantitative analysis of A. ochraceus biomass, which is suitable for routine monitoring of fungal contamination in agro-food matrices.
Expression of HLA G may be a way for tumor cells to escape immuno-surveillance. HLA G is selectively expressed by extravillous trophoblast in the human placenta, a tissue that does not express HLA A or B molecules. It is tempting to propose that tumor cells resemble this unique HLA class I phenotype as they frequently lose classical HLA A, B and C class I expression. Such peculiar HLA class I distribution would in theory allow tumor cells to escape from T- and NK-cell cytotoxicity. To determine whether HLA G is expressed on tumor cells, we studied HLA G mRNA levels using RT-PCR and HLA G cell-surface expression by immunohistological techniques in a panel of 50 human solid tumor tissues, 31 tumor cell lines of different origin, 4 autologous mucosa samples and 3 peripheral white cell samples. We found mRNA transcripts of different HLA G isoforms in most of the samples studied. However, we did not detect cell-surface expression of HLA G using 3 specific monoclonal antibodies (MAbs; 87G, 01G and G223). HLA G was detected only in the U937 myelomonocytic cell line after stimulation with IFN-gamma. We favor the hypothesis that HLA G plays a minor role, if any, in providing an inhibitory signal to NK cells to escape immunosurveillance. We cannot, however, exclude the possibility that some other HLA G isoforms may be expressed in some tumors.
Attachment of cells to extracellular matrix components is critical for the regulation of hematopoiesis. CD43 is a mucin-like transmembrane sialoglycoprotein expressed on the surface of almost all hematopoietic cells. A highly extended structure of extracellular mucin with negative charge may function as a repulsive barrier to hematopoietic cells. However, some investigators have shown that CD43 has proadhesive properties, and engagement of CD43 has been reported to upregulate integrin-mediated cell adhesion in T cells. We found that cross-linking of CD43 with monoclonal antibodies (MoAbs) enhanced integrin alpha4beta1 (very late antigen [VLA]-4) and alpha5 beta1 (VLA-5)-dependent adhesion of human cord blood CD34(+) cells to fibronectin. CD34(+) CD38(hi), but not CD34(+)CD38(-/low) cells responded significantly to the stimulus, suggesting that committed, but not stem and more immature progenitors are sensitive to CD43-mediated activation of integrin. To elucidate the molecular mechanism leading to integrin activation, we used the growth factor-dependent cell line MO7e. Cross-linking of CD43 induced tyrosine phosphorylation of several intracellular molecules including the protein tyrosine kinase Syk, the proto-oncogene product Cbl, and phospholipase C (PLC)-gamma2 in MO7e cells. Moreover, protein tyrosine kinase inhibitor herbimycin A and PLC inhibitor U73122 both blocked CD43-induced enhancement of adhesion to fibronectin. These results indicate that signals mediated through CD43 may increase integrin affinity to fibronectin via a pathway dependent on protein tyrosine kinase and PLC-gamma activation in hematopoietic progenitors.