Defective cAMP-dependent phosphorylation of intact T lymphocytes in active systemic lupus erythematosus.
The present study was undertaken to establish whether cAMP-dependent phosphorylation of endogenous substrates is impaired in T lymphocytes from subjects with active systemic lupus erythematosus ( SLE). In normal human T lymphocytes, the cell-permeable cAMP analog, N6,O2'-dibutyryladenosine 3',5'-cyclic monophosphate, induced phosphorylation of substrates with molecular masses of 17.5, 23/25, 33.5 kDa on one-dimensional SDS/PAGE. Maximal phosphorylation occurred at 60 min. In contrast to healthy T cells, the extent of substrate phosphorylation achieved in active SLE T cells (n = 8) was only 15% at 60 min in the 17.5-kDa substrate, 21% in the 23/25-kDa substrate, and 9% in the 33.5-kDa substrate. The rheumatic disease controls (rheumatoid arthritis; primary Sjögren syndrome; n = 8) exhibited a mean 72%, 124%, and 85%, respectively, of phosphorylation observed in healthy T cells. Because the only known mechanism by which cAMP acts is via cAMP-dependent protein kinase (protein kinase A), these data raise the possibility of a defect at the level of this kinase in SLE T lymphocytes.[1]References
- Defective cAMP-dependent phosphorylation of intact T lymphocytes in active systemic lupus erythematosus. Hasler, P., Schultz, L.A., Kammer, G.M. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
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