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  • Title: Identification of four lipocortin proteins and phosphorylation of lipocortin I by protein kinase C in cytosols of porcine thyroid cell cultures.
    Author: Antonicelli F, Omri B, Breton MF, Rothhut B, Russo-Marie F, Pavlovic-Hournac M, Haye B.
    Journal: FEBS Lett; 1989 Dec 04; 258(2):346-50. PubMed ID: 2532154.
    Abstract:
    Four proteins of the lipocortin family, lipocortin I (35 kDa), lipocortin II (36 kDa), lipocortin V (32 kDa) and lipocortin VI (67-70 kDa), were identified in the cytosols of 2-day-old cultures of thyroid cells. Only lipocortin I was phosphorylated in vitro in fully differentiated, thyroid stimulating hormone-treated cells (0.1 mU/ml). Protein kinase C was the only kinase activity which phosphorylated lipocortin I. Phosphorylation shifted its pI from 6.9 to 6.6. The in vitro phosphorylation of lipocortin I was impaired in cultures exposed for 2 days to phorbol ester (10(-7) M), although it was present in both the cytosol and the particulate fraction of these cells.
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