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Gene Review

Ces1e  -  carboxylesterase 1E

Mus musculus

Synonyms: Carboxylesterase 1E, Eg, Egasyn, Es-22, Es22, ...
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High impact information on Es22

  • Organophosphorous compounds, which are potent inhibitors of egasyn-esterase activity, caused a rapid dissociation of the high molecular weight egasyn-microsomal beta-glucuronidase complex when administered in vivo or when added in vitro to microsomal suspensions [1].
  • These experiments implicate the egasyn-esterase active site in attachment of microsomal beta-glucuronidase to egasyn by a novel mechanism that, in turn, compartmentalizes beta-glucuronidase within the endoplasmic reticulum [1].
  • The hydrophilic nature of both the complex and free egasyn was confirmed by phase separation experiments with the detergent Triton X-114 [2].
  • The results indicate that the relative availability of egasyn determines the balance between glucuronidase incorporation into membranes and that into lysosomes [3].
  • By means of a recently developed radioimmunoassay for egasyn, the relationship between microsomal glucuronidase levels and egasyn levels has been examined in various adult tissues, during postnatal development in liver, and after androgen induction of glucuronidase in kidney [3].

Biological context of Es22


Anatomical context of Es22


Associations of Es22 with chemical compounds

  • We have now purfied egasyn by releasing it from antiglucuronidase immunoprecipitates of M forms under relatively mild conditions, such as treatment with deoxycholate or heating at 50 degrees [6].
  • Most of the antigenic sites of egasyn in homogenates of normal liver are masked after extraction with Triton X-100 and only become immunoreactive after exposure to deoxycholate [6].
  • Isolated egasyn is a glycoprotein of molecular weight about 64,000 and is not unusually hydrophobic in amino acid composition [6].
  • A procedure for the radioimmunoassay of egasyn was developed utilizing egasyn labeled with iodine 125 [6].
  • Taken together, these results suggest that (a) the egasyn-glucuronidase system may use a novel mechanism related to that of serine proteinases and their inhibitors in complex formation and in subsequent localization of glucuronidase within the ER and that (b) a possible function of ER glucuronidase is to modulate the esterase activity of egasyn [9].

Physical interactions of Es22

  • An accessory protein identical to mouse egasyn is complexed with rat microsomal beta-glucuronidase and is identical to rat esterase-3 [10].

Other interactions of Es22

  • Several phenotypes corresponded in relative mobility and relative isoelectric point among inbred strains to that recently reported for esterase-22 by Eisenhardt and von Deimling [(1982). Comp. Biochem. Physiol. 73B:719] [5].
  • Combined experiments measuring susceptibility to neuraminidase and to endoglycosidase H and specific binding to Ricinus communis lectin-agarose columns showed that the alterations in isoelectric point were associated with a decrease in complex oligosaccharides of lysosomal beta-glucuronidase in egasyn-positive mice [11].
  • This carboxylesterase consisted of 554 amino acid residues, and exhibited 43% and 42% similarities to the known mouse esterases Es-22 and pEs-N, respectively [12].

Analytical, diagnostic and therapeutic context of Es22


  1. Involvement of the esterase active site of egasyn in compartmentalization of beta-glucuronidase within the endoplasmic reticulum. Medda, S., Stevens, A.M., Swank, R.T. Cell (1987) [Pubmed]
  2. Lumenal location of the microsomal beta-glucuronidase-egasyn complex. Brown, J., Novak, E.K., Takeuchi, K., Moore, K., Medda, S., Swank, R.T. J. Cell Biol. (1987) [Pubmed]
  3. Relationships between levels of membrane-bound glucuronidase and the associated protein egasyn in mouse tissues. Lusis, A.J., Paigen, K. J. Cell Biol. (1977) [Pubmed]
  4. Characterization and functional expression of a cDNA encoding egasyn (esterase-22): the endoplasmic reticulum-targeting protein of beta-glucuronidase. Ovnic, M., Swank, R.T., Fletcher, C., Zhen, L., Novak, E.K., Baumann, H., Heintz, N., Ganschow, R.E. Genomics (1991) [Pubmed]
  5. Identity of esterase-22 and egasyn, the protein which complexes with microsomal beta-glucuronidase. Medda, S., von Deimling, O., Swank, R.T. Biochem. Genet. (1986) [Pubmed]
  6. Isolation, characterization, and radioimmunoassay of murine egasyn, a protein stabilizing glucuronidase membrane binding. Lusis, A.J., Tomino, S., Paigen, K. J. Biol. Chem. (1976) [Pubmed]
  7. Expression of egasyn-esterase in mammalian cells. Sequestration in the endoplasmic reticulum and complexation with beta-glucuronidase. Novak, E.K., Baumann, H., Ovnic, M., Swank, R.T. J. Biol. Chem. (1991) [Pubmed]
  8. Egasyn, a protein which determines the subcellular distribution of beta-glucuronidase, has esterase activity. Medda, S., Swank, R.T. J. Biol. Chem. (1985) [Pubmed]
  9. The propeptide of beta-glucuronidase. Further evidence of its involvement in compartmentalization of beta-glucuronidase and sequence similarity with portions of the reactive site region of the serpin superfamily. Li, H., Takeuchi, K.H., Manly, K., Chapman, V., Swank, R.T. J. Biol. Chem. (1990) [Pubmed]
  10. An accessory protein identical to mouse egasyn is complexed with rat microsomal beta-glucuronidase and is identical to rat esterase-3. Medda, S., Takeuchi, K., Devore-Carter, D., von Deimling, O., Heymann, E., Swank, R.T. J. Biol. Chem. (1987) [Pubmed]
  11. The egasyn gene affects the processing of oligosaccharides of lysosomal beta-glucuronidase in liver. Swank, R.T., Pfister, K., Miller, D., Chapman, V. Biochem. J. (1986) [Pubmed]
  12. Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver. Aida, K., Moore, R., Negishi, M. Biochim. Biophys. Acta (1993) [Pubmed]
  13. Identification and androgen regulation of egasyn in the mouse epididymis. Abou-Haila, A., Orgebin-Crist, M.C., Skudlarek, M.D., Tulsiani, D.R. Biochim. Biophys. Acta (1998) [Pubmed]
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