Disease relevance of INPP1

• We used recombinant Baculovirus harboring the cDNA of bovine inositol polyphosphate 1-phosphatase to infect Spodoptera frugiperda (Sf9) insect cells [1].
• Changes of lymphocyte subpopulations in jejunal and ileal Peyer's patches (JPP and IPP) of six calves inoculated with Salmonella dublin were investigated at 9 hours, 1, 2, 3 and 7 days post inoculation (p.i.) using immunohistochemistry [2].

High impact information on INPP1

• Inositol polyphosphate 1-phosphatase, an enzyme of the phosphatidylinositol signaling pathway, catalyzes the hydrolysis of the 1-position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate [3].
• We find that the enzyme is present, but not exclusively, in the nucleus of Madin-Darby bovine kidney cells, and also in COS-7 and HeLa cells that were transiently transfected with a cDNA encoding bovine inositol polyphosphate 1-phosphatase [4].
• We recently described inositol polyphosphate 1-phosphatase, an enzyme which cleaves the 1-phosphate from inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3) (Inhorn, R. C., and Majerus, P. W. (1987) J. Biol. Chem. 262, 15946-15952) [5].
• Inositol polyphosphate 1-phosphatase accounts for greater than 80% of the hydrolytic activity in all tissues studied except brain, where inositol polyphosphate 4-phosphatase is the major enzyme that hydrolyzes Ins(1,3,4)P3 [5].
• Inositol polyphosphate 1-phosphatase, a Mg2+-dependent, lithium ion-inhibited enzyme, specifically hydrolyzes Ins(1,3,4)P3 to Ins(3,4)P2 and Ins(1,4)P2 to Ins 4-P (Inhorn, R. C., Bansal, V. S., and Majerus, P. W. (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 2170-2174) [6].

Biological context of INPP1

• These motifs may correspond to binding sites within IMP and IPP for inositol phosphates or for lithium, since both substances are bound by these proteins [7].

Anatomical context of INPP1

• [3H]inositol polyphosphate metabolism in muscarinic cholinoceptor-stimulated airways smooth muscle: accumulation of [3H]inositol 4,5 bisphosphate via a lithium-sensitive inositol polyphosphate 1-phosphatase [8].
• In peripheral blood and in all tissues, except IPP the values for B cells (sIgM+) were low [9].

Associations of INPP1 with chemical compounds

• Neither the oxygen-hemoglobin dissociation curve nor the Hill coefficient, n, of fetal or adult bovine hemoglobin was affected by uric acid riboside (UAR), 2,3-diphosphoglyceric acid (2,3-DPG), adenosine triphosphate (ATP), or inositol pentaphosphate (IPP) [10].

Analytical, diagnostic and therapeutic context of INPP1

• Crystallization and initial X-ray crystallographic characterization of recombinant bovine inositol polyphosphate 1-phosphatase produced in Spodoptera frugiperda cells [1].

References