[Application of an immunoenzyme test (ELISA) for the detection of toxinogenesis in Corynebacterium diphtheriae].
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Biomedical subjects
Publications and source records attributed to M Stefănescu.
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Experimental ventricular preexcitation type WPW was performed in five dogs, through an artificial bypass, an electric conductor, made of copper, with a diameter of 8 mm and 12 cm in length. Whenever the conductor was put in contact with both the atrial and the ventricular wall, a WPW electrocardiogram pattern was obtained. This work has been done to better localize with epicardial mapping the site of preexcitation for surgical purposes.
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In fifteen patients with WPW syndrome the standard electrocardiogram, the vector cardiogram and the precordial map were used togther in order to better localize the ventricular pre-excitation. These three noninvasive techniques permit a more precise location of the accessory pathway in WPW syndrome.
A comparative study of signal transduction through tyrosine phosphorylation process in peripheral blood lymphocytes from SLE patients and healthy subjects reveal some modifications in the phosphorylation pattern of SLE T lymphocytes. Thus, the level of constitutive tyrosine phosphorylation in resting SLE T lymphocytes is higher than in lymphocytes from healthy subjects. In SLE T lymphocytes, a cellular proteic substrate with an apparent molecular weight of about 37 kDa is constitutively phosphorylated. Some differences in the pattern of phosphorylation are obvious in lectin (Con A, PHA)-activated T lymphocytes. Thus, Con A activation enhances the phosphorylation of cellular substrates with molecular weight in the range of 55-80 kDa from SLE T lymphocytes. Moreover, the 21 kDa substrate is also hyperphosphorylated after PHA activation of SLE lymphocytes.
Integrin-mediated activation of monocytes is an important aspect involved in the increase of proinflammatory cytokine messages. Tyrosine phosphorylation of proteins is one of the earliest events involved in these processes: Therefore, we selected two inhibitors, one for tyrosine kinases (quercitin) and another for tyrosine phosphatases (sodium orthovanadate) and we studied their capacity to modulate monocyte adhesion to fibronectin. Our results showed that quercitin strongly inhibits both tyrosine phosphorylation and cell adhesion. Sodium orthovanadate induces a modest increase of tyrosine phosphorylation and a weak enhancement of cell adhesion. When a combination of the two inhibitors was used, the tyrosine phosphorylation level displayed a strong enhancement. In contrast, cell adhesion was inhibited, but to the same degree. These observations indicate that tyrosine kinases may be more important than tyrosine phosphatases in the modulation of cell adhesion by flavonoid compounds.