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Gene Review

Acp1  -  acid phosphatase 1, soluble

Rattus norvegicus

Synonyms: LMW-PTP, LMW-PTPase, Low molecular weight cytosolic acid phosphatase, Low molecular weight phosphotyrosine protein phosphatase
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Disease relevance of Acp1

  • The amino acids involved in transition-state stabilization for cysteinylphosphate hydrolysis were confirmed by the x-ray structure of the Yersinia PTPase complexed with vanadate, a transition-state mimic that binds covalently to the active-site cysteine [1].
  • Engineering site-specific amino acid substitutions into the protein-tyrosine phosphatase (PTPase) PTP1 and the dual-specific vaccinia H1-related phosphatase (VHR), has kinetically isolated the two chemical steps of the reaction and provided a rare opportunity for examining transition states and directly observing the phosphoenzyme intermediate [1].
  • To test the hypothesis that the transmembrane PTPase LAR can modulate insulin receptor signaling in vivo, antisense RNA expression was used to specifically suppress LAR protein levels by 63% in the rat hepatoma cell line, McA-RH7777 [2].
  • Many protein-tyrosine phosphatases (PTPases) have now been identified, but little is known about PTPase expression and regulation in vascular tissue and in vascular disease [3].
  • In contrast to the glomerular lesion, PTPase mRNA expression was not induced in experimental tubulointerstitial nephritis [4].

Psychiatry related information on Acp1


High impact information on Acp1

  • Our results indicate that alloxan diabetes in the rat is associated with an increase in the activity of a large, membrane-associated PTPase which accounts for only a small proportion of insulin receptor tyrosine dephosphorylation [6].
  • Nonetheless, increased activity of this PTPase may oppose tyrosine kinase-mediated insulin signal transmission, thus contributing to insulin resistance [6].
  • Hepatic PTPase activity was measured using two artificial substrates phosphorylated on tyrosine: reduced, carboxyamidomethylated, and maleylated lysozyme (P-Tyr-RCML) and myelin basic protein (P-Tyr-MBP), as well as an autophosphorylated 48-kD insulin receptor tyrosine kinase domain (P-Tyr-IRKD) [6].
  • Rats that were made alloxan diabetic exhibited a significant increase in hepatic membrane (detergent-soluble) PTPase activity measured with P-Tyr-MBP, without a change in activity measured with P-Tyr-RCML or the P-Tyr-IRKD [6].
  • Phosphotyrosine phosphatase (PTPase) activity in rat liver was measured using a phosphopeptide substrate containing sequence identity to the major site of insulin receptor autophosphorylation [7].

Chemical compound and disease context of Acp1


Biological context of Acp1


Anatomical context of Acp1


Associations of Acp1 with chemical compounds


Enzymatic interactions of Acp1

  • Additionally, protein tyrosine phosphatase (PTPase) activities towards immobilized phosphorylated insulin receptor or phosphorylated IRS-1 of membrane (MF) and cytosolic fractions (CF) of these tissues were measured [19].

Regulatory relationships of Acp1

  • Because Stat factors are known to be inactivated by protein tyrosine phosphatases (PTPase), we showed that a PTPase is able to eliminate the DNA binding of hepatic Stat3.(ABSTRACT TRUNCATED AT 250 WORDS)[20]
  • PTPase activity was regulated by both acute and chronic insulin and IGF-I treatment [21].
  • In conclusion, inhibition of PTPase activity by pV stimulates basal and inhibits arginine-induced glucagon release [22].
  • We conclude that pancreatic acinar membranes possess a low-molecular-mass PTPase which is stimulated by somatostatin analogs at concentrations involving activation of membrane somatostatin receptors [23].

Other interactions of Acp1

  • A novel cytoplasmic protein-tyrosine phosphatase (PTPase) designated PTP20 was isolated from a PC12 cDNA library and shown to positively regulate the differentiation process in PC12 cells [24].
  • Previously we found that rat mesangial cells express 3CH134/CL100 protein-tyrosine phosphatase (PTPase) in response to reactive oxygen intermediates (ROIs), and we now extend these studies to glomerulonephritis (GN), where ROI have been demonstrated to play a role [4].
  • These studies indicate that three PTPases with markedly divergent structures have the catalytic potential to dephosphorylate both insulin and EGF receptors in intact cells and that redundant PTPase activity may occur in vivo [25].
  • Overexpression of the PTPLP decreased the basal PTPase activity of COS-7 cells for Raytide [26].
  • To identify PTPases that are recruited to the activated TrkA receptor, we used an in-gel PTPase assay to examine the presence of PTPases in TrkA immunoprecipitates [27].

Analytical, diagnostic and therapeutic context of Acp1


  1. Visualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysis. Denu, J.M., Lohse, D.L., Vijayalakshmi, J., Saper, M.A., Dixon, J.E. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  2. Insulin receptor signaling is augmented by antisense inhibition of the protein tyrosine phosphatase LAR. Kulas, D.T., Zhang, W.R., Goldstein, B.J., Furlanetto, R.W., Mooney, R.A. J. Biol. Chem. (1995) [Pubmed]
  3. Protein-tyrosine phosphatases in the vessel wall: differential expression after acute arterial injury. Wright, M.B., Seifert, R.A., Bowen-Pope, D.F. Arterioscler. Thromb. Vasc. Biol. (2000) [Pubmed]
  4. Oxidative stress-inducible protein tyrosine phosphatase in glomerulonephritis. Feng, L., Xia, Y., Seiffert, D., Wilson, C.B. Kidney Int. (1995) [Pubmed]
  5. Protein tyrosine phosphatase activity in insulin-resistant rodent Psammomys obesus. Meyerovitch, J., Balta, Y., Ziv, E., Sack, J., Shafrir, E. Int. J. Exp. Diabetes Res. (2002) [Pubmed]
  6. Differential regulation of multiple hepatic protein tyrosine phosphatases in alloxan diabetic rats. Boylan, J.M., Brautigan, D.L., Madden, J., Raven, T., Ellis, L., Gruppuso, P.A. J. Clin. Invest. (1992) [Pubmed]
  7. Hepatic phosphotyrosine phosphatase activity and its alterations in diabetic rats. Meyerovitch, J., Backer, J.M., Kahn, C.R. J. Clin. Invest. (1989) [Pubmed]
  8. Are protein-tyrosine phosphatases specific for phosphotyrosine? Zhang, Z.Y. J. Biol. Chem. (1995) [Pubmed]
  9. Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction. Hengge, A.C., Sowa, G.A., Wu, L., Zhang, Z.Y. Biochemistry (1995) [Pubmed]
  10. cDNA cloning of a cytosolic protein tyrosine phosphatase (RKPTP) from rat kidney. Moriyama, T., Kawanishi, S., Inoue, T., Imai, E., Kaneko, T., Xia, C., Takenaka, M., Noguchi, T., Kamada, T., Ueda, N. FEBS Lett. (1994) [Pubmed]
  11. Enhancement or induction of neurite formation by a protein tyrosine phosphatase inhibitor, 3,4-dephostatin, in growth factor-treated PC12h cells. Fujiwara, S., Watanabe, T., Nagatsu, T., Gohda, J., Imoto, M., Umezawa, K. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  12. Identification of a neuregulin and protein-tyrosine phosphatase response element in the nicotinic acetylcholine receptor epsilon subunit gene: regulatory role of an Rts transcription factor. Sapru, M.K., Florance, S.K., Kirk, C., Goldman, D. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  13. Protein tyrosine phosphatases expressed in the developing rat brain. Sahin, M., Hockfield, S. J. Neurosci. (1993) [Pubmed]
  14. Regulation of an hepatic low-M(r) membrane-associated protein-tyrosine phosphatase. Tappia, P.S., Atkinson, P.G., Sharma, R.P., Sale, G.J. Biochem. J. (1993) [Pubmed]
  15. Abundance of low molecular weight phosphotyrosine protein phosphatase in the nerve-ending fraction in the brain. Tanino, H., Yoshida, J., Yamamoto, R., Kobayashi, Y., Shimohama, S., Fujimoto, S. Biol. Pharm. Bull. (1999) [Pubmed]
  16. Tyrosine phosphorylation of p97 regulates transitional endoplasmic reticulum assembly in vitro. Lavoie, C., Chevet, E., Roy, L., Tonks, N.K., Fazel, A., Posner, B.I., Paiement, J., Bergeron, J.J. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  17. Activation of p42 MAP kinase and the release of oocytes from cell cycle arrest. Shibuya, E.K., Boulton, T.G., Cobb, M.H., Ruderman, J.V. EMBO J. (1992) [Pubmed]
  18. Active site labeling of a receptor-like protein tyrosine phosphatase. Pot, D.A., Dixon, J.E. J. Biol. Chem. (1992) [Pubmed]
  19. Ramipril increases the protein level of skeletal muscle IRS-1 and alters protein tyrosine phosphatase activity in spontaneously hypertensive rats. Krützfeldt, J., Raasch, W., Klein, H.H. Naunyn Schmiedebergs Arch. Pharmacol. (2000) [Pubmed]
  20. Rapid activation of the Stat3 transcription complex in liver regeneration. Cressman, D.E., Diamond, R.H., Taub, R. Hepatology (1995) [Pubmed]
  21. Regulation of protein tyrosine phosphatases by insulin and insulin-like growth factor I. Kenner, K.A., Hill, D.E., Olefsky, J.M., Kusari, J. J. Biol. Chem. (1993) [Pubmed]
  22. Glucagon release is regulated by tyrosine phosphatase and PI3-kinase activity. Chen, J., Ostenson, C.G. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  23. Stimulation of a membrane tyrosine phosphatase activity by somatostatin analogues in rat pancreatic acinar cells. Colas, B., Cambillau, C., Buscail, L., Zeggari, M., Esteve, J.P., Lautre, V., Thomas, F., Vaysse, N., Susini, C. Eur. J. Biochem. (1992) [Pubmed]
  24. The novel protein-tyrosine phosphatase PTP20 is a positive regulator of PC12 cell neuronal differentiation. Aoki, N., Yamaguchi-Aoki, Y., Ullrich, A. J. Biol. Chem. (1996) [Pubmed]
  25. Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system. Hashimoto, N., Zhang, W.R., Goldstein, B.J. Biochem. J. (1992) [Pubmed]
  26. Cloning and expression of protein tyrosine phosphatase-like protein derived from a rat pheochromocytoma cell line. Kambayashi, Y., Takahashi, K., Bardhan, S., Inagami, T. Biochem. J. (1995) [Pubmed]
  27. Transient association of the phosphotyrosine phosphatase SHP-2 with TrkA is induced by nerve growth factor. Goldsmith, B.A., Koizumi, S. J. Neurochem. (1997) [Pubmed]
  28. Angiotensin II stimulates protein tyrosine phosphatase activity through a G-protein independent mechanism. Brechler, V., Reichlin, S., De Gasparo, M., Bottari, S.P. Recept. Channels (1994) [Pubmed]
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