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Biochem Biophys Res Commun. 1996 Aug 5;225(1):243-9.

Cloning and expression of a human placenta inositol 1,3,4,5-tetrakisphosphate and phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase.

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  • 1Interdisciplinary Research Institute (IRIBHN), Universit√© Libre de Bruxelles, Belgium.


Distinct inositol and phosphatidylinositol polyphosphate 5-phosphatases have recently been cloned. Primers were designated coding for highly conserved amino acid regions that are shared between sequences of 5-phosphatases. We used degenerate primers to amplify polymerase chain reaction products from rat brain cDNA. A product with a novel sequence was identified and used to clone a 4.9 kb cDNA from human placenta cDNA libraries (hp51CN). COS-7 cells transfected with a C-terminal truncated form of this cDNA showed an increase in Ins(1,3,4,5)P4 and PtdIns(3,4,5)P3 hydrolyzing activity, but not in Ins(1,4,5)P3 5-phosphatase. Enzymatic activity was inhibited in the presence of 2,3-bisphosphoglycerate and p-hydroxymercuribenzoate. The presence of an SH2 domain and proline-rich sequence motifs within hp51CN suggests that this 5-phosphatase interacts with various proteins in signal transduction.

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