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Translocation of the α‐ and β‐isoforms of protein kinase C following activation of human T‐lymphocytes
Author(s) -
Kvanta Anders,
Jondal Mikael,
Fredholm Bertil B.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80618-d
Subject(s) - protein kinase c , chromosomal translocation , gene isoform , jurkat cells , diacylglycerol kinase , beta (programming language) , cytoplasm , microbiology and biotechnology , stimulation , pkc alpha , biology , concanavalin a , alpha (finance) , kinase , t cell , biochemistry , endocrinology , in vitro , immunology , medicine , gene , immune system , construct validity , nursing , patient satisfaction , computer science , programming language
We have analyzed how activation of human Jurkat T‐cells by the mitogenic lectin, concanavalin A (Con A), may affect the cellular distribution of the α‐ and β‐isoforms of protein kinase C (PKC) in T‐cells. In non‐stimulated cells almost all of the α‐ and β‐PKC was localized to the cytoplasmic compartment. Stimulation with Con A caused a transient translocation of both α‐ and β‐PKC from the cytoplasm to the cell membrane. The α‐ isoform appeared to be translocated to a somewhat greater extent and for a longer period of time that the β‐form. Translocation was maximal between 1 and 5 min for both of the isoforms. 30 min after stimulation, β‐PKC had returned to basal levels, whereas a substantial amount of α‐PKC remained associated with the particulate fraction. We conclude that activation of human T‐cells causes the translocation of at least two different isoforms of PKC, α‐PKC and β‐PKC.