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Real-time Live Imaging of T-cell Signaling Complex Formation
Published on: June 23, 2013
Signal transduction in T lymphocytes of SLE patients: lectin-activated phosphorylation on tyrosine
C Matache1, M Stefănescu, A Onu
1Cantacuzino Institute, Bucharest, Romania.
Abstract:
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.
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