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Aldosterone rapidly activates Src kinase in M‐1 cells involving the mineralocorticoid receptor and HSP84
Author(s) -
Braun Sabine,
Lösel Ralf,
Wehling Martin,
Boldyreff Brigitte
Publication year - 2004
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/j.febslet.2004.06.031
Subject(s) - aldosterone , proto oncogene tyrosine protein kinase src , mineralocorticoid receptor , autophosphorylation , endocrinology , medicine , chemistry , kinase , mineralocorticoid , src family kinase , biology , protein kinase a , biochemistry
We investigated the effect of aldosterone on Src kinase. In the kidney cell line, M‐1 aldosterone leads to a >2‐fold transient activation of Src kinase seen as early as 2 min after aldosterone administration. Maximal Src kinase activation was measured at an aldosterone concentration of 1 nM. In parallel to activation, autophosphorylation at Tyr‐416 of Src kinase increased. Src kinase activation was blocked by spironolactone. Aldosterone led to increased association of Src with HSP84. Furthermore, rapamycin blocked aldosterone‐induced Src activation. We conclude that Src activation by aldosterone is mediated through the mineralocorticoid receptor and HSP84.