Electronic microarray technique for detection of nine base substitutions including single-nucleotide polymorphisms in the human OGG1 gene.
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Cell Line, Tumor↗
Biomedical subjects
Christine Teixeira
Publications and source records attributed to Christine Teixeira.
Integration of DAG signaling systems mediated by PKC-dependent phosphorylation of RasGRP3.
Members of the RasGRP family of Ras activators have C1 domains that bind diacylglycerol (DAG) and DAG analogs such as the tumor-promoting phorbol esters. RasGRP members could be responsible for some of the DAG signaling processes that have previously been attributed to protein kinase C (PKC). We found that RasGRP3 is selectively expressed in B cells, suggesting that RasGRP3 might function downstream of the B-cell receptor (BCR). Indeed, stimulation of Ramos B cells with the DAG analog phorbol ester myristate (PMA) results in the association of RasGRP3 with the membrane fraction. However, we also made the unexpected observation that RasGRP3 is phosphorylated, coincident with Ras activation after stimulation. When inhibitors of PKC are present, Ras activation is attenuated, and this attenuation correlates with an inhibition of RasGRP3 phosphorylation. RasGRP3 is phosphorylated in vitro by PKC-theta and PKC-beta2. When ectopically coexpressed in HEK-293 cells, a dominant-activated mutant of PKC-theta phosphorylates RasGRP3 and enhances Ras-Erk signaling. These results provide the first indication for a functional interaction between a RasGRP family member and a dissimilar DAG binding protein. A convergent DAG signaling system could be important in fine-tuning Ras signaling during B-cell development or during the humoral immune response.
Animals↗
Studies of cisplatin and hemoglobin interactions using nanospray mass spectrometry and liquid chromatography with inductively-coupled plasma mass spectrometry.
Interactions of cisplatin with hemoglobin (Hb) were studied using both nanoelectrospray mass spectrometry (nanoESI-MS) and a combination of size exclusion high performance liquid chromatography with inductively coupled plasma mass spectrometry (HPLC-ICPMS). Size exclusion HPLC separation of free and protein-bound cisplatin followed by simultaneous monitoring of 195Pt and 57Fe demonstrated the presence of Hb-bound Pt complexes. Nanospray quadrupole time-of-flight mass spectrometry studies of the Hb-cisplatin complexes further demonstrated the specific binding of cisplatin to the alpha-chain, heme-alpha, beta-chain, and heme-beta units of hemoglobin. Accurate mass measurements and tandem mass spectrometry information confirmed the Hb-cisplatin complexes. The formation of Hb-cisplatin complexes was observed at the sub-microM to microM concentration levels of cisplatin, which are relevant to clinical levels. These findings and the techniques developed for cisplatin-Hb interaction studies are useful for understanding of drug-protein interactions.
Antineoplastic Agents↗