Abstract:
:We examined the importance of tyrosine kinase(s) on the ATP-evoked Ca2+ entry and DNA synthesis of thyroid FRTL-5 cells. ATP rapidly and transiently tyrosine phosphorylated a 72-kDa protein(s). This phosphorylation was abolished by pertussis toxin and by the tyrosine kinase inhibitor genistein, and was dependent on Ca2+ entry. Pretreatment of the cells with genistein did not affect the release of sequestered Ca2+, but the capacitative Ca2+ or Ba2+ entry evoked by ATP or thapsigargin was attenuated. Pretreatment of the cells with orthovanadate enhanced the increase in intracellular free Ca2+ ([Ca2+]i), whereas the Ba2+ entry was not increased. Phorbol 12-myristate 13-acetate (PMA) phosphorylated the same protein(s) as did ATP. Genistein inhibited the ATP-evoked phosphorylation of MAP kinase and attenuated both the ATP- and the PMA-evoked DNA synthesis. However, genistein did not inhibit the ATP-evoked expression of c-fos. Furthermore, genistein enhanced the ATP-evoked release of arachidonic acid. Thus, ATP activates a tyrosine kinase via a Ca2+-dependent mechanism. A genistein-sensitive mechanism participates, in part, in the ATP-evoked activation of DNA synthesis. Genistein inhibits only modestly capacitative Ca2+ entry in FRTL-5 cells.
journal_name
J Cell Physioljournal_title
Journal of cellular physiologyauthors
Törnquist K,Dugué B,Ekokoski Edoi
10.1002/(SICI)1097-4652(199805)175:2<211::AID-JCP1subject
Has Abstractpub_date
1998-05-01 00:00:00pages
211-9issue
2eissn
0021-9541issn
1097-4652pii
10.1002/(SICI)1097-4652(199805)175:2<211::AID-JCP1journal_volume
175pub_type
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