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Gene Review

CPE  -  carboxypeptidase E

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Disease relevance of CPE

  • When either virus obtained from CPE(surv) cells that had spontaneously lost the sg RNA or virus from which defective particles had been removed was used to establish persistently infected cells, these cells were also protected from the CPE after superinfection with cp CSFV [1].
  • However, when naive cells were infected with supernatants from CPE(surv)cells that contained defective virus particles, the CPE reappeared within three to five virus passages, indicating that the sg RNA retained its cytopathogenic potential [1].
  • Bovine enterovirus CPE at different multiplicities of infection in the absence of viral RNA synthesis [2].
  • Moreover, the rIFN-as could inhibit infectious bovine rhinotracheitis virus replication in the MDBK cell line using CPE inhibition method [3].
  • Enkephalin convertase demonstrated in the pituitary and adrenal gland by [3H]guanidinoethylmercaptosuccinic acid autoradiography: dehydration decreases neurohypophyseal levels [4].

High impact information on CPE

  • Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form, which differ slightly in relative molecular mass (Mr) [5].
  • Here, to investigate whether the CPE activities in the various tissues are produced from a single gene, purified CPE was partially sequenced and oligonucleotide probes were used to isolate a clone encoding CPE from a bovine pituitary complementary DNA library [5].
  • The predicted amino-acid sequence of the cDNA clone contains the partially determined sequences of CPE, several pairs of basic amino acids and displays some homology with both carboxypeptidases A and B. Restriction analysis of bovine genomic DNA suggests only one gene for CPE [5].
  • Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules [5].
  • These results support the hypothesis that pro-CPH is processed and activated during axonal transport from neuronal perikarya of SON to nerve terminals of the posterior pituitary [6].

Chemical compound and disease context of CPE


Biological context of CPE

  • N-POMC when added to the assays did not inhibit the aggregation of CPE with prolactin or insulin, indicating that these interactions do not involve a binding site for N-POMC [7].
  • To further explore the possibility that CPE serves to mediate the association of content proteins with the membrane during granule biogenesis, the binding of CPE to granule content proteins was investigated using an in vitro aggregation assay in which the selective precipitation of granule content proteins is induced by titration of the pH to <6 [7].
  • Pro-insulin bound CPE with similar kinetics [8].
  • Pro-enkephalin, but not CGA bound to CPE with similar IC50 as pro-insulin and N-POMC1-26 [8].
  • Subcultivation of the persistently infected cultures led to virus replication followed by CPE and then cell regrowth [9].

Anatomical context of CPE

  • Synthetic COOH-terminal peptides 11-24 residues in length are able to bind to bovine pituitary membranes and can be extracted by conditions that extract the membrane-bound form of CPE [10].
  • Taken together, these results are consistent with a model in which the decreasing pH and increasing Ca2+ levels in the trans Golgi network induce the aggregation of CPE, which contributes to the sorting of this protein into regulated pathway secretory vesicles [11].
  • The mouse anterior pituitary-derived cell line AtT-20 has been widely used to study the biosynthesis and secretion of peptide hormones, such as ACTH, and peptide-processing enzymes, such as carboxypeptidase-E (CPE) [12].
  • Applications of this rapid and sensitive radiometric assay to detect CPE in cultured cells and in subcellular fractions of the pituitary are described [13].
  • This study evaluated the attachment, chemoattractive, proliferative and mineralization inductive potential of a bovine cementum extract (CPE) on newborn murine dental follicle cells (MDFC) in vitro [14].

Associations of CPE with chemical compounds

  • The aggregation of M2-CPE does not explain the apparent membrane binding of this protein since the aggregate is solubilized by 1% Triton X-100 at pH 5.5 or by pH 6.0, whereas M2-CPE is not extracted from membranes under these conditions [11].
  • Also, CPD does not elute from a substrate affinity column when the pH is raised to 8, which elutes CPE, although CPD can subsequently be eluted by arginine [15].
  • Cholesterol depletion resulted in dissociation of CPE from secretory granule membranes and decreased the binding of prohormones to membranes [16].
  • In vivo cholesterol depletion using lovastatin resulted in the lack of sorting of CPE and its cargo to the regulated secretory pathway [16].
  • Both the 21-residue COOH-terminal peptide and the purified membrane form of CPE, but not the soluble form, partition into Triton X-114 only at low pH (pH less than 6) [10].

Physical interactions of CPE

  • CPE has been shown to bind to an amino-terminal peptide of pro-opiomelanocortin (N-POMC) at pH 5.5 and hypothesized to be critically involved in the targeting of hormones such as POMC to the regulated secretory pathway [Cool, D. R., Normant, E., Shen, F., Chen, H. C., Pannell, L., Zhang, Y., and Loh, Y. P. (1997) Cell 88, 73-83] [7].
  • In addition, CPE co-precipitated at pH 5.8 with purified prolactin and with insulin, which homophillically self-aggregate yet are structurally distinct from N-POMC [7].

Other interactions of CPE


Analytical, diagnostic and therapeutic context of CPE


  1. Porcine cells persistently infected with classical swine fever virus protected from pestivirus-induced cytopathic effect. Mittelholzer, C., Moser, C., Tratschin, J.D., Hofmann, M.A. J. Gen. Virol. (1998) [Pubmed]
  2. Bovine enterovirus CPE at different multiplicities of infection in the absence of viral RNA synthesis. Levine, R.A., Wolff, D.A. Intervirology (1979) [Pubmed]
  3. Interferon-alpha Genes from Bos and Bubalus bubalus. Shi, X., Xia, C., Pan, B., Wang, M. Anim. Biotechnol. (2006) [Pubmed]
  4. Enkephalin convertase demonstrated in the pituitary and adrenal gland by [3H]guanidinoethylmercaptosuccinic acid autoradiography: dehydration decreases neurohypophyseal levels. Strittmatter, S.M., Lynch, D.R., De Souza, E.B., Snyder, S.H. Endocrinology (1985) [Pubmed]
  5. Cloning and sequence analysis of cDNA for bovine carboxypeptidase E. Fricker, L.D., Evans, C.J., Esch, F.S., Herbert, E. Nature (1986) [Pubmed]
  6. Carboxypeptidase H in the hypothalamo-neurohypophysial system: evidence for processing and activation of a prohormone-processing enzyme during axonal transport. Hook, V.Y., Affolter, H.U., Palkovits, M. J. Neurosci. (1990) [Pubmed]
  7. Carboxypeptidase E, a peripheral membrane protein implicated in the targeting of hormones to secretory granules, co-aggregates with granule content proteins at acidic pH. Rindler, M.J. J. Biol. Chem. (1998) [Pubmed]
  8. Carboxypeptidase E is a sorting receptor for prohormones: binding and kinetic studies. Cool, D.R., Loh, Y.P. Mol. Cell. Endocrinol. (1998) [Pubmed]
  9. Persistent infection with bovine herpesvirus-1 (infectious bovine rhinotracheitis virus) in cultured hamster cells. Michalski, F.J., Hsiung, G.D. In vitro. (1976) [Pubmed]
  10. Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC Fricker, L.D., Das, B., Angeletti, R.H. J. Biol. Chem. (1990) [Pubmed]
  11. Calcium- and pH-dependent aggregation of carboxypeptidase E. Song, L., Fricker, L.D. J. Biol. Chem. (1995) [Pubmed]
  12. Secretion and regulation of a neuropeptide-processing enzyme by AtT-20 cells. Devi, L. Endocrinology (1992) [Pubmed]
  13. Comparison of a spectrophotometric, a fluorometric, and a novel radiometric assay for carboxypeptidase E (EC and other carboxypeptidase B-like enzymes. Fricker, L.D., Devi, L. Anal. Biochem. (1990) [Pubmed]
  14. Bovine cementum extract influences murine dental follicle cells in vitro. Arzate, H., Aguilar-Mendoza, M.E., Esponda Aguilar, C., Portilla Robertson, J. Arch. Med. Res. (1997) [Pubmed]
  15. Purification and characterization of carboxypeptidase D, a novel carboxypeptidase E-like enzyme, from bovine pituitary. Song, L., Fricker, L.D. J. Biol. Chem. (1995) [Pubmed]
  16. Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor. Dhanvantari, S., Loh, Y.P. J. Biol. Chem. (2000) [Pubmed]
  17. Regulation of carboxypeptidase E. Effect of pH, temperature and Co2+ on kinetic parameters of substrate hydrolysis. Greene, D., Das, B., Fricker, L.D. Biochem. J. (1992) [Pubmed]
  18. Cell culture studies with a cytopathic bovine rotavirus. McNulty, M.S., Allan, G.M., McFerran, J.B. Arch. Virol. (1977) [Pubmed]
  19. Antiserum raised in pigs against canine distemper virus and its utility in diagnostic procedures for morbillivirus infections (canine distemper, phocine distemper, rinderpest). Zaghawa, A., Liess, B., Frey, H.R. Zentralblatt Veterinarmedizin Reihe B (1990) [Pubmed]
  20. [3H]guanidinoethylmercaptosuccinic acid binding to tissue homogenates. Selective labeling of enkephalin convertase. Strittmatter, S.M., Lynch, D.R., Snyder, S.H. J. Biol. Chem. (1984) [Pubmed]
  21. Poly(N-acetyllactosaminyl) oligosaccharides of chromaffin granule membrane glycoproteins. Margolis, R.U., Fischer-Colbrie, R., Margolis, R.K. J. Neurochem. (1988) [Pubmed]
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