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Oncogenes and Cancer
Published in Pimentel Enrique, Oncogenes, 2020
Mutated oncogenes with increased transforming potential are apparently present in a minor fraction of tumors occurring under natural conditions. A study of 29 patients with bladder, lung, and colon cancer, including analysis of 20 primary tumor tissues (biopsy specimens), was negative for the presence of mutations producing substitutions of the 12th amino acid in the p21 product of the c-H-ras gene.312 Mutation of c-K-ras would be more frequent than mutation of c-H-ras or c-N-ras in tumors. By DNA restriction length polymorphism studies mutation at the 12th codon of the c-K-ras proto-oncogene was detected in the primary tumor tissue of a squamous cell lung carcinoma removed from a 66-year-old man.46 The mutation present in this patient was of a somatic origin since it was present in the tumor tissue but not in normal tissue from the same patient. Another possible point mutation of c-K-ras was detected in the tumor from a patient with serous cystadenocarcinoma of the ovary by DNA transfection assay and demonstration of an altered electrophoretic mobility of the respective p21 protein product.305 Activation of c-K-ras has also been observed in a human pancreas carcinoma.313 Mutation at codon 12 of c-N-ras was detected in the tumor cells from a patient with acute myeloblastic leukemia at the outbreak of the clinical disease, determining a change from glycin to aspartic acid in the p21ras polypeptide product.314
Re-evaluation of the measurement of haptoglobin in human plasma samples
Published in Scandinavian Journal of Clinical and Laboratory Investigation, 2022
Maria Kløjgaard Skytthe, Anna Lahn Sørensen, Dorle Hennig, Maria Boysen Sandberg, Lars Melholt Rasmussen, Holger J. Møller, Karsten Skjødt, Jonas Heilskov Graversen, Søren Kragh Moestrup
Binding to CD163 of Hp2-2 and Hp1-1 with increasing ratio of Hb added was studied by surface plasmon resonance on a Biacore T200 instrument (Cytiva) essentially as described [13]. Briefly, CD163 was immobilized on a CM5 chip at different densities (0.0026, 0.02 and 0.029 pmol/mm2). Residual amounts of Hb and Hb-Hp complexes were removed from purchased Hp by IsdH-Sepharose [14] resulting in no CD163 binding of Hp prior to the addition of Hb. Increasing amounts of Hb complexes (with a molar concentration defined by the Hba-Hbb-dimer) were added to 400 nM Hb-depleted Hp1-1 and Hp2-2 (as defined by the concentration of the monomeric alpha-beta unit) in running buffer (10 mM HEPES, 150 mM NaCl, 3 mM CaCl2, and 0.05% Surfactant P-20, pH 7.4) to form Hp-Hb complexes. The chip was regenerated by two cycles of injection of 10 µL 10 mM Glycin, 20 mM EDTA, 500 mM NaCl, and 0.05% Tween20, pH 4.0. Data were analyzed using the BIAcore T200 Evaluation Software 3.1. All experiments were performed in independent triplicates of duplicates.
Retinal ganglion cell complex and visual evoked potentials in levetiracetam treatment
Published in Cutaneous and Ocular Toxicology, 2020
Dicle Hazirolan, Melih Duman, Selda Keskin Guler, Guner Uney, Firdevs Ornek
Levetiracetam is a broad-spectrum, second-generation AED. It is most commonly approved as adjunctive treatment or monotherapy of partial onset seizures with or without secondary generalisation. Other approved indications include adjunctive treatment of myoclonic seizures associated with juvenile myoclonic epilepsy and primary generalised tonic-clonic seizures associated with idiopathic generalised epilepsy1. It is a pyrolidone derivative and has a unique mechanisms of action. Unlike other AEDs, the mechanisms of action of levetiracetam appear to involve neuronal binding to synaptic vesicle protein 2 A, inhibiting calcium release from intraneuronal stores, opposing the activity of negative modulators of GABA- and glycin-gated currents and inhibiting excessive synchronised activity between neurons1. In addition, levetiracetam also inhibits N-type calcium channels1.
Data independent acquisition mass spectrometry of irradiated mouse lung endothelial cells reveals a STAT-associated inflammatory response
Published in International Journal of Radiation Biology, 2020
Jos Philipp, Wolfgang Sievert, Omid Azimzadeh, Christine von Toerne, Fabian Metzger, Anton Posch, Daniela Hladik, Prabal Subedi, Gabriele Multhoff, Michael J. Atkinson, Soile Tapio
Membranes were incubated with the primary antibody overnight at 4 °C. For detection, the blots were incubated for 2 h with the appropriate horseradish-peroxidase conjugated anti-rabbit or -mouse secondary antibody. Detection was performed by ECL Advance Western blotting detection kit (GE Healthcare GmbH, Solingen, Germany) quantified in a chemiluminescence reader ChemiDoc™ MP (Bio-Rad Laboratories GmbH) with the appropriate ImageLab 6.0.1 software. Blots were stripped for reprobing maximally twice with Stripping Buffer (0.2 M Glycin, 0.003 M SDS, 1/100 Tween20, pH 2.4).