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Gene Review

PPA1  -  pyrophosphatase (inorganic) 1

Homo sapiens

Synonyms: HEL-S-66p, IOPPP, Inorganic pyrophosphatase, PP, PP1, ...
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Disease relevance of PPA1


Psychiatry related information on PPA1


High impact information on PPA1

  • The inactive cytosolic form of PP-1 (PP-1I) can be activated in vitro through the glycogen synthase kinase-3-catalyzed phosphorylation of its inhibitory subunit (inhibitor-2), but the physiological significance is unclear.(ABSTRACT TRUNCATED AT 400 WORDS)[7]
  • The activities of PP-1 and PP-2B are controlled by the second messengers cyclic AMP and calcium [7].
  • Yotiao, an NMDA receptor-associated protein, bound the type I protein phosphatase (PP1) and the adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA) holoenzyme [8].
  • Hence, yotiao is a scaffold protein that physically attaches PP1 and PKA to NMDA receptors to regulate channel activity [8].
  • The main regulatory step takes place at the level of ADP-glucose synthesis, a reaction catalyzed by ADP-Glc pyrophosphorylase (PPase) [9].

Chemical compound and disease context of PPA1


Biological context of PPA1


Anatomical context of PPA1


Associations of PPA1 with chemical compounds

  • Inorganic pyrophosphatase (pyrophosphate phosphohydrolase, EC from human erythrocyte hemolysates has been purified up to 10 000-fold [21].
  • We determined total PP-1 activity in muscle biopsies from insulin-sensitive and -resistant nondiabetic Pima Indians [24].
  • Tautomycin, an inhibitor of PP1, inhibited blue light-induced H(+) pumping, phosphorylation of the plasma membrane H(+)-ATPase in guard cell protoplasts, and stomatal opening [25].
  • The growth arrest and DNA damage-inducible protein, GADD34, was identified by its interaction with human inhibitor 1 (I-1), a protein kinase A (PKA)-activated inhibitor of type 1 protein serine/threonine phosphatase (PP1), in a yeast two-hybrid screen of a human brain cDNA library [3].
  • The phospho-CREB (P-CREB) phosphatase activity present in nuclear extracts coelutes with protein Ser/Thr phosphatase type 2A (PP2A) on Mono Q, amino-hexyl Sepharose, and heparin agarose columns and was chromatographically resolved from nuclear protein Ser/Thr-phosphatase type 1 (PP1) [26].

Regulatory relationships of PPA1

  • Unexpectedly, Alk PPase inhibited aromatase activity in a dose-dependent manner in the presence, as well as in the absence, of ATP/Mg/Ca [27].

Other interactions of PPA1


Analytical, diagnostic and therapeutic context of PPA1


  1. Peripheral pulmonary adenocarcinomas with bronchioloalveolar features: immunophenotypes correlate with histologic patterns. Ritter, J.H., Boucher, L.D., Wick, M.R. Mod. Pathol. (1998) [Pubmed]
  2. The neutrophil-activating protein (HP-NAP) of Helicobacter pylori is a protective antigen and a major virulence factor. Satin, B., Del Giudice, G., Della Bianca, V., Dusi, S., Laudanna, C., Tonello, F., Kelleher, D., Rappuoli, R., Montecucco, C., Rossi, F. J. Exp. Med. (2000) [Pubmed]
  3. Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Connor, J.H., Weiser, D.C., Li, S., Hallenbeck, J.M., Shenolikar, S. Mol. Cell. Biol. (2001) [Pubmed]
  4. Subcellular distribution of inorganic pyrophosphatase activity in various normal and neoplastic cell types. Shatton, J.B., Williams, A., Weinhouse, S. Cancer Res. (1983) [Pubmed]
  5. Progranulin Mutations in Primary Progressive Aphasia: The PPA1 and PPA3 Families. Mesulam, M., Johnson, N., Krefft, T.A., Gass, J.M., Cannon, A.D., Adamson, J.L., Bigio, E.H., Weintraub, S., Dickson, D.W., Hutton, M.L., Graff-Radford, N.R. Arch. Neurol. (2007) [Pubmed]
  6. Enhanced expression of protein phosphatase 2A associated with hyper-phosphorylation of histone H1 in Alzheimer's disease brain. Mori, S., Cao, Y., Sogawa, K., Kondo, K., Sakai, T., Hino, N., Yamashiro, H., Okada, M., Miyamoto, K., Kawaguchi, Y., Mashiba, T., Norimatsu, H. Res. Commun. Mol. Pathol. Pharmacol. (2003) [Pubmed]
  7. The structure and regulation of protein phosphatases. Cohen, P. Annu. Rev. Biochem. (1989) [Pubmed]
  8. Regulation of NMDA receptors by an associated phosphatase-kinase signaling complex. Westphal, R.S., Tavalin, S.J., Lin, J.W., Alto, N.M., Fraser, I.D., Langeberg, L.K., Sheng, M., Scott, J.D. Science (1999) [Pubmed]
  9. ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis. Ballicora, M.A., Iglesias, A.A., Preiss, J. Microbiol. Mol. Biol. Rev. (2003) [Pubmed]
  10. RET Is Constitutively Activated by Novel Tandem Mutations that Alter the Active Site Resulting in Multiple Endocrine Neoplasia Type 2B. Cranston, A.N., Carniti, C., Oakhill, K., Radzio-Andzelm, E., Stone, E.A., McCallion, A.S., Hodgson, S., Clarke, S., Mondellini, P., Leyland, J., Pierotti, M.A., Whittaker, J., Taylor, S.S., Bongarzone, I., Ponder, B.A. Cancer Res. (2006) [Pubmed]
  11. A eukaryotic type serine/threonine kinase and phosphatase in Streptococcus agalactiae reversibly phosphorylate an inorganic pyrophosphatase and affect growth, cell segregation, and virulence. Rajagopal, L., Clancy, A., Rubens, C.E. J. Biol. Chem. (2003) [Pubmed]
  12. Dephosphorylation of Rb (Thr-821) in response to cell stress. Krucher, N.A., Rubin, E., Tedesco, V.C., Roberts, M.H., Sherry, T.C., De Leon, G. Exp. Cell Res. (2006) [Pubmed]
  13. Increased myofibrillar protein phosphatase-1 activity impairs rat aortic smooth muscle activation after hypoxia. Teoh, H., Zacour, M., Wener, A.D., Gunaratnam, L., Ward, M.E. Am. J. Physiol. Heart Circ. Physiol. (2003) [Pubmed]
  14. Purification and characterization of two proteins with inorganic pyrophosphatase activity from Desulfovibrio vulgaris: rubrerythrin and a new, highly active, enzyme. Liu, M.Y., Le Gall, J. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  15. A de novo case of trisomy 10p: gene dosage studies of hexokinase, inorganic pyrophosphatase and adenosine kinase. Snyder, F.F., Lin, C.C., Rudd, N.L., Shearer, J.E., Heikkila, E.M., Hoo, J.J. Hum. Genet. (1984) [Pubmed]
  16. Assignment of the inorganic pyrophosphatase gene locus (PP) to chromosome 10 in man. McAlpine, P.J., Mohandas, T., Ray, M., Wang, H., Hamerton, J.L. Cytogenet. Cell Genet. (1976) [Pubmed]
  17. Differential expression of four members of the H+-ATPase gene family during dormancy of vegetative buds of peach trees. Gévaudant, F., Pétel, G., Guilliot, A. Planta (2001) [Pubmed]
  18. Biologically active oxidized lipids (phytoprostanes) in the plant diet and parenteral lipid nutrition. Karg, K., Dirsch, V.M., Vollmar, A.M., Cracowski, J.L., Laporte, F., Mueller, M.J. Free Radic. Res. (2006) [Pubmed]
  19. Secretion, subcellular localization and metabolic status of inorganic pyrophosphate in human platelets. A major constituent of the amine-storing granules. Fukami, M.H., Dangelmaier, C.A., Bauer, J.S., Holmsen, H. Biochem. J. (1980) [Pubmed]
  20. Subcellular localization and properties of alkaline inorganic pyrophosphatase in human polymorphonuclear leucocytes. Raja, K.B., Smith, G.P., Peters, T.J. Clin. Chim. Acta (1981) [Pubmed]
  21. Purification and kinetic properties of human erythrocyte Mg2+-dependent inorganic pyrophosphatase. Thuillier, L. Biochim. Biophys. Acta (1978) [Pubmed]
  22. PP1/PP2A Phosphatases Are Required for the Second Step of Pre-mRNA Splicing and Target Specific snRNP Proteins. Shi, Y., Reddy, B., Manley, J.L. Mol. Cell (2006) [Pubmed]
  23. Defective insulin response of phosphorylase phosphatase in insulin-resistant humans. Kida, Y., Raz, I., Maeda, R., Nyomba, B.L., Stone, K., Bogardus, C., Sommercorn, J., Mott, D.M. J. Clin. Invest. (1992) [Pubmed]
  24. Deficiency in phosphorylase phosphatase activity despite elevated protein phosphatase type-1 catalytic subunit in skeletal muscle from insulin-resistant subjects. Nyomba, B.L., Brautigan, D.L., Schlender, K.K., Wang, W., Bogardus, C., Mott, D.M. J. Clin. Invest. (1991) [Pubmed]
  25. Protein phosphatase 1 positively regulates stomatal opening in response to blue light in Vicia faba. Takemiya, A., Kinoshita, T., Asanuma, M., Shimazaki, K. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  26. Nuclear protein phosphatase 2A dephosphorylates protein kinase A-phosphorylated CREB and regulates CREB transcriptional stimulation. Wadzinski, B.E., Wheat, W.H., Jaspers, S., Peruski, L.F., Lickteig, R.L., Johnson, G.L., Klemm, D.J. Mol. Cell. Biol. (1993) [Pubmed]
  27. Interactions between kinases and phosphatases in the rapid control of brain aromatase. Balthazart, J., Baillien, M., Ball, G.F. J. Neuroendocrinol. (2005) [Pubmed]
  28. UDP-glucose pyrophosphorylase: up-regulation in hypertrophic cartilage and role in hyaluronan synthesis. Magee, C., Nurminskaya, M., Linsenmayer, T.F. Biochem. J. (2001) [Pubmed]
  29. Structural aspects of the effectiveness of bisphosphonates as competitive inhibitors of the plant vacuolar proton-pumping pyrophosphatase. Gordon-Weeks, R., Parmar, S., Davies, T.G., Leigh, R.A. Biochem. J. (1999) [Pubmed]
  30. Proteomic approach to substrates related to MAPK pathway in 293T cells. Zhang, G., Wang, S. Cell Biol. Int. (2007) [Pubmed]
  31. Type Ic, a novel glycogenosis. Underlying mechanism. Nordlie, R.C., Sukalski, K.A., Muñoz, J.M., Baldwin, J.J. J. Biol. Chem. (1983) [Pubmed]
  32. Association of the type 1 protein phosphatase PP1 with the A-kinase anchoring protein AKAP220. Schillace, R.V., Scott, J.D. Curr. Biol. (1999) [Pubmed]
  33. Synthesis of medium pyrophosphate by soluble mitochondrial F1 through dimethyl sulfoxide-water transitions. Tuena de Gómez-Puyou, M., Sandoval, F., Gómez-Puyou, A. J. Biol. Chem. (1995) [Pubmed]
  34. Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis. Zhuo, S., Clemens, J.C., Stone, R.L., Dixon, J.E. J. Biol. Chem. (1994) [Pubmed]
  35. Characterization of the mitotic phase pRb-directed protein phosphatase activity. Nelson, D.A., Ludlow, J.W. Oncogene (1997) [Pubmed]
  36. D1-Receptor, DARPP-32, and PP-1 in the primate corpus luteum and luteinized granulosa cells: evidence for phosphorylation of DARPP-32 by dopamine and human chorionic gonadotropin. Mayerhofer, A., Fritz, S., Grünert, R., Sanders, S.L., Duffy, D.M., Ojeda, S.R., Stouffer, R.L. J. Clin. Endocrinol. Metab. (2000) [Pubmed]
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