Protein tyrosine phosphorylation and calcium signaling in thyroid FRTL-5 cells
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...
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Published in | Journal of cellular physiology Vol. 175; no. 2; pp. 211 - 219 |
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Language | English |
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01.05.1998
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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. J. Cell. Physiol. 175:211–219, 1998. © 1998 Wiley‐Liss, Inc. |
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AbstractList | 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. 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. J. Cell. Physiol. 175:211–219, 1998. © 1998 Wiley‐Liss, Inc. |
Author | Dugué, Benoit Törnquist, Kid Ekokoski, Elina |
Author_xml | – sequence: 1 givenname: Kid surname: Törnquist fullname: Törnquist, Kid organization: Department of Biosciences, Division of Animal Physiology, University of Helsinki, Helsinki, Finland – sequence: 2 givenname: Benoit surname: Dugué fullname: Dugué, Benoit organization: Minerva Foundation Institute for Medical Research, Helsinki, Finland – sequence: 3 givenname: Elina surname: Ekokoski fullname: Ekokoski, Elina organization: Department of Biosciences, Division of Animal Physiology, University of Helsinki, Helsinki, Finland |
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Snippet | 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... 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... |
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SubjectTerms | Adenosine Triphosphate - pharmacology Animals Arachidonic Acid - metabolism Calcium - pharmacokinetics Calcium-Calmodulin-Dependent Protein Kinases - metabolism Cell Line DNA - biosynthesis Genistein - pharmacology Pertussis Toxin Phosphorylation Protein-Tyrosine Kinases - physiology Proto-Oncogene Proteins c-fos - metabolism Rats Signal Transduction - physiology Tetradecanoylphorbol Acetate - pharmacology Thapsigargin - pharmacology Thyroid Gland - physiology Tyrosine - metabolism Vanadates - pharmacology Virulence Factors, Bordetella - pharmacology |
Title | Protein tyrosine phosphorylation and calcium signaling in thyroid FRTL-5 cells |
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