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Gene Review

ACP1  -  acid phosphatase 1, soluble

Bos taurus

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Disease relevance of ACP1


High impact information on ACP1

  • The structure of the low-molecular-weight PTPase supports a reaction mechanism involving the conserved Cys 12 as an attacking nucleophile in an in-line associative mechanism [3].
  • The second PTPase like domains do not have detectable catalytic activity using a variety of substrates, but sequences within the second domains influence substrate specificity [4].
  • That suramin is a high affinity PTPase inhibitor is consistent with the observation that suramin treatment of cancer cell lines leads to an increase in tyrosine phosphorylation of several cellular proteins [5].
  • Suramin is a reversible and competitive PTPase inhibitor with Kis values in the low microM range, whereas the Kis for the dual specificity phosphatase VHR is at least 10-fold higher [5].
  • The low M(r) phosphotyrosine protein phosphatase (PTPase) and Yersinia enterocolitica PTPase are inactivated by nitric oxide-generating compounds [2].

Biological context of ACP1


Anatomical context of ACP1

  • The relationship between the ACP1 gene product, an 18kDa acid phosphatase (E.C. postulated to function as a protein tyrosyl phosphatase, and the cellular flavin mononucleotide (FMN) phosphatase has been examined in vitro and by using cultured Chinese hamster ovary (CHO) cells [11].
  • We conclude that this novel PTPase is active on cell type-specific signalling substrates that control normal and transformed fibroblast proliferation [10].
  • The PTPase inhibitor sodium orthovanadate did not prevent endothelial cell retraction or FAK, paxillin, or vinculin redistribution [9].
  • Focal adhesion contact disruption induced by adenosine-homocysteine is independent of PTPase or caspase activation [9].
  • Low molecular weight phosphotyrosine protein phosphatase from PC12 cells. Purification, some properties and expression during neurogenesis in vitro and in vivo [12].

Associations of ACP1 with chemical compounds


Regulatory relationships of ACP1


Analytical, diagnostic and therapeutic context of ACP1


  1. Differential role of four cysteines on the activity of a low M(r) phosphotyrosine protein phosphatase. Chiarugi, P., Marzocchini, R., Raugei, G., Pazzagli, C., Berti, A., Camici, G., Manao, G., Cappugi, G., Ramponi, G. FEBS Lett. (1992) [Pubmed]
  2. Nitric oxide causes inactivation of the low molecular weight phosphotyrosine protein phosphatase. Caselli, A., Camici, G., Manao, G., Moneti, G., Pazzagli, L., Cappugi, G., Ramponi, G. J. Biol. Chem. (1994) [Pubmed]
  3. The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase. Su, X.D., Taddei, N., Stefani, M., Ramponi, G., Nordlund, P. Nature (1994) [Pubmed]
  4. Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR. Streuli, M., Krueger, N.X., Thai, T., Tang, M., Saito, H. EMBO J. (1990) [Pubmed]
  5. Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases. Zhang, Y.L., Keng, Y.F., Zhao, Y., Wu, L., Zhang, Z.Y. J. Biol. Chem. (1998) [Pubmed]
  6. The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase. Camici, G., Manao, G., Cappugi, G., Modesti, A., Stefani, M., Ramponi, G. J. Biol. Chem. (1989) [Pubmed]
  7. Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-A resolution. Zhang, M., Van Etten, R.L., Stauffacher, C.V. Biochemistry (1994) [Pubmed]
  8. The role of Cys12, Cys17 and Arg18 in the catalytic mechanism of low-M(r) cytosolic phosphotyrosine protein phosphatase. Cirri, P., Chiarugi, P., Camici, G., Manao, G., Raugei, G., Cappugi, G., Ramponi, G. Eur. J. Biochem. (1993) [Pubmed]
  9. Protein tyrosine phosphatase-dependent proteolysis of focal adhesion complexes in endothelial cell apoptosis. Harrington, E.O., Smeglin, A., Newton, J., Ballard, G., Rounds, S. Am. J. Physiol. Lung Cell Mol. Physiol. (2001) [Pubmed]
  10. Negative growth control by a novel low M(r) phosphotyrosine protein phosphatase in normal and transformed cells. Ruggiero, M., Pazzagli, C., Rigacci, S., Magnelli, L., Raugei, G., Berti, A., Chiarugi, V.P., Pierce, J.H., Camici, G., Ramponi, G. FEBS Lett. (1993) [Pubmed]
  11. Analysis of the ACP1 gene product: classification as an FMN phosphatase. Fuchs, K.R., Shekels, L.L., Bernlohr, D.A. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  12. Low molecular weight phosphotyrosine protein phosphatase from PC12 cells. Purification, some properties and expression during neurogenesis in vitro and in vivo. Lucentini, L., Fulle, S., Ricciolini, C., Lancioni, H., Panara, F. Int. J. Biochem. Cell Biol. (2003) [Pubmed]
  13. Phosphotyrosine phosphatase activity associated with c-Src in large multimeric complexes isolated from adrenal medullary chromaffin cells. van Hoek, M.L., Allen, C.S., Parsons, S.J. Biochem. J. (1997) [Pubmed]
  14. Adenosine induces endothelial apoptosis by activating protein tyrosine phosphatase: a possible role of p38alpha. Harrington, E.O., Smeglin, A., Parks, N., Newton, J., Rounds, S. Am. J. Physiol. Lung Cell Mol. Physiol. (2000) [Pubmed]
  15. Probing the function of Asp128 in the lower molecular weight protein-tyrosine phosphatase-catalyzed reaction. A pre-steady-state and steady-state kinetic investigation. Wu, L., Zhang, Z.Y. Biochemistry (1996) [Pubmed]
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