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Phosphoinositide synthesis and degradation in isolated rat liver peroxisomes
Author(s) -
Jeynov Boyan,
Lay Dorothee,
Schmidt Frank,
Tahirovic Sabina,
Just Wilhelm W.
Publication year - 2006
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.2006.09.058
Subject(s) - peroxisome , organelle , phosphatase , phosphatidylinositol , biochemistry , biology , in vivo , pi , kinase , phosphorylation , microbiology and biotechnology , chemistry , receptor
Analyzing peroxisomal phosphoinositide (PId # ) synthesis in highly purified rat liver peroxisomes we found synthesis of phosphatidylinositol 4‐phosphate (PtdIns4 P ), PtdIns(4,5) P 2 and PtdIns(3,5) P 2 . PtdIns3 P was hardly detected in vitro, however, was observed in vivo after [ 32 P]‐phosphate labeling of primary rat hepatocytes. In comparison with other subcellular organelles peroxisomes revealed a unique PId pattern suggesting peroxisomal specificity of the observed synthesis. Use of phosphatase inhibitors enhanced the amount of PtdIns4 P . The results obtained provide evidence that isolated rat liver peroxisomes synthesize PIds and suggest the association of PId 4‐kinase and PId 5‐kinase and PId 4‐phosphatase activities with the peroxisomal membrane.
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