Protein phosphatase 2A plays a critical role in interleukin-2-induced beta 2-integrin dependent homotypic adhesion in human CD4+ T cell lines
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Protein phosphatase 2A plays a critical role in interleukin-2-induced beta 2-integrin dependent homotypic adhesion in human CD4+ T cell lines. / Brockdorff, J; Nielsen, M; Svejgaard, A; Dobson, P; Röpke, C; Geisler, C; Odum, N.
In: Cytokine, Vol. 9, No. 5, 1997, p. 333-9.Research output: Contribution to journal › Journal article › Research › peer-review
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T1 - Protein phosphatase 2A plays a critical role in interleukin-2-induced beta 2-integrin dependent homotypic adhesion in human CD4+ T cell lines
AU - Brockdorff, J
AU - Nielsen, M
AU - Svejgaard, A
AU - Dobson, P
AU - Röpke, C
AU - Geisler, C
AU - Odum, N
N1 - Keywords: Antigens, CD18; CD4-Positive T-Lymphocytes; Cell Adhesion; Cell Line; Cyclins; Humans; Interleukin-2; Okadaic Acid; Phosphoprotein Phosphatases; Protein Phosphatase 2
PY - 1997
Y1 - 1997
N2 - Besides its function as a growth factor for T lymphocytes, interleukin 2 (IL-2) induces beta 2-integrin mediated adhesion, migration, and extravasation of T lymphocytes. It is, however, largely unknown how IL-2 receptors (IL-2R) are coupled to the beta 2-integrin adhesion pathway. Because IL-2 modulates enzymatic activity and/or subcellular distribution of serine/threonine phosphatases 1 and 2A (PP1/PP2A) in T cells, we examined the role of these phosphatases in IL-2 induced homotypic adhesion in antigen specific human CD4+ T cell lines. We show that calyculin A, a potent inhibitor of PP1 and PP2A, blocks PP1/PP2A activity and IL-2 induced adhesion, whereas cyclosporin A, an inhibitor of protein serine/threonine phosphatase 2B (PP2B), does not, suggesting that PP1 and/or PP2A are involved in IL-2 induced adhesion. Endothall, which preferentially inhibits PP2A, strongly inhibited cytokine induced adhesion, whereas the structurally related compound 1,4-dimethylendothall had no effect on either phosphatase activity or the adhesion response. Okadaic acid, which preferentially inhibits PP2A, almost completely blocked IL-2-induced adhesion, whereas tautomycin, a potent inhibitor of PP1, had no inhibitory effect on cytokine induced adhesion at concentrations which strongly inhibited phosphatase activity. In conclusion, these data provide evidence that PP2A plays a critical role in IL-2-induced beta 2-integrin-dependent adhesion of human T cell lines.
AB - Besides its function as a growth factor for T lymphocytes, interleukin 2 (IL-2) induces beta 2-integrin mediated adhesion, migration, and extravasation of T lymphocytes. It is, however, largely unknown how IL-2 receptors (IL-2R) are coupled to the beta 2-integrin adhesion pathway. Because IL-2 modulates enzymatic activity and/or subcellular distribution of serine/threonine phosphatases 1 and 2A (PP1/PP2A) in T cells, we examined the role of these phosphatases in IL-2 induced homotypic adhesion in antigen specific human CD4+ T cell lines. We show that calyculin A, a potent inhibitor of PP1 and PP2A, blocks PP1/PP2A activity and IL-2 induced adhesion, whereas cyclosporin A, an inhibitor of protein serine/threonine phosphatase 2B (PP2B), does not, suggesting that PP1 and/or PP2A are involved in IL-2 induced adhesion. Endothall, which preferentially inhibits PP2A, strongly inhibited cytokine induced adhesion, whereas the structurally related compound 1,4-dimethylendothall had no effect on either phosphatase activity or the adhesion response. Okadaic acid, which preferentially inhibits PP2A, almost completely blocked IL-2-induced adhesion, whereas tautomycin, a potent inhibitor of PP1, had no inhibitory effect on cytokine induced adhesion at concentrations which strongly inhibited phosphatase activity. In conclusion, these data provide evidence that PP2A plays a critical role in IL-2-induced beta 2-integrin-dependent adhesion of human T cell lines.
U2 - 10.1006/cyto.1996.0173
DO - 10.1006/cyto.1996.0173
M3 - Journal article
C2 - 9195132
VL - 9
SP - 333
EP - 339
JO - Cytokine
JF - Cytokine
SN - 1043-4666
IS - 5
ER -
ID: 8545678