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Polyphosphoinositide hydrolysis by phospholipase C is accelerated by thyrotropin releasing hormone (TRH) in clonal rat pituitary cells (GH 3 cells)
Author(s) -
Schlegel Werner,
Roduit Claude,
Zahnd Gaston R.
Publication year - 1984
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(84)80205-7
Subject(s) - phosphatidylinositol , phospholipase c , phospholipid , phospholipase , thyrotropin releasing hormone , medicine , endocrinology , phosphoinositide phospholipase c , chemistry , inositol , hydrolysis , biochemistry , phosphomonoesterase , hormone , biology , signal transduction , enzyme , membrane , phosphatase , receptor
Thyrotropin releasing hormone (TRH) accelerates the turnover of phosphatidylinositol in GH 3 cells (‘phospholipid response’). From the analysis of inositol phosphates in the presence of Li + which inhibits their dephosphorylation, it can be concluded that the hydrolysis of phosphatidylinositol 4,5‐biphosphate, and possibly of phosphatidylinositol 4‐phosphate by phospholipase C is markedly accelerated by TRH. It appears that this reaction initiates the acceleration of phosphatidylinositol turnover. The specificity of hormonally regulated phospholipase C reaction for polyphosphoinositides has important implications for the potential role of the phospholipid response as a mechanism of membrane signal transduction.