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Gene Review

Cpe  -  carboxypeptidase E

Mus musculus

Synonyms: CPE, CPH, Carboxypeptidase E, Carboxypeptidase H, Cph-1, ...
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Disease relevance of Cpe


Psychiatry related information on Cpe


High impact information on Cpe

  • The temporal control of CPEB phosphorylation suggests a mechanism in which CPE-containing mRNA translation is stimulated at pachytene and metaphase I [6].
  • An inherited defect in the fat/fat mouse which affects the processing of proinsulin, and probably also many other prohormones, due to a point mutation in carboxypeptidase E has recently been identified and has begun to provide new insights into the functional integration of the individual processing steps [7].
  • Polyadenylation-induced translation of oocyte mRNAs requires the cis-acting CPE sequence and the CPE-binding protein CPEB [8].
  • Carboxypeptidase e: a surprise player in protein sorting [9].
  • Cpe(fat)/Cpe(fat) mice have a naturally occurring point mutation within the carboxypeptidase E gene that inactivates this enzyme, leading to an accumulation of many neuroendocrine peptides containing C-terminal basic residues [10].

Chemical compound and disease context of Cpe

  • Specific inhibitors of nitric oxide synthetase, lipoxygenase or cyclo-oxygenase did not influence either the CPE or growth kinetics of HSV-1, suggesting that neither reactive nitrogen intermediates nor arachidonic acid metabolites were involved in the antiviral mechanism of TNF [11].

Biological context of Cpe


Anatomical context of Cpe

  • Altered neuropeptide processing in prefrontal cortex of Cpe (fat/fat) mice: implications for neuropeptide discovery [13].
  • Electron microscopy of retinas from Cpe fat/fat mice revealed significantly reduced spherule size, but normal synaptic ribbons and synaptic vesicle density, implicating a reduction in total number of vesicles per synapse in the photoreceptors of these animals [14].
  • Immunofluorescence analysis of epitope-tagged CPE revealed Ser202CPE to be present primarily in secretory vesicles, whereas Pro202CPE was localized to the endoplasmic reticulum and not the secretory vesicle-like structures [15].
  • When expressed in AtT-20 cells, a mouse pituitary-derived cell line, CPE with Pro202 and Phe202 were not secreted [15].
  • To know whether CPE is implicated in proinsulin sorting, pancreatic islets were isolated from CPE-deficient Cpefat/Cpefat mice and Cpefat/+ controls, pulse-labeled ([3H]leucine), and then chased in basal medium (90 min) to examine constitutive secretion followed by medium with secretagogues (60 min) to stimulate regulated secretion [16].

Associations of Cpe with chemical compounds

  • Although the transgenic mice were born in the expected frequency, 21 of 22 proSAAS transgenic Cpe (fat/fat) mice died between 11 and 26 weeks of age, presumably due to greatly elevated blood glucose [17].
  • We conclude that lack of CPE in islet beta-cells results in a marked decrease in processing of proIAPP at its NH(2) (but not COOH) terminus that is associated with attenuated levels of PC2 and (pro)7B2 and a great reduction in formation of mature amidated IAPP [18].
  • These results demonstrate that CPE is required for the correct processing of arginine- and glycine-extended CCK in all major regions of the mouse brain [19].
  • Whereas CPE-like activity is detected in homogenates of Cpefat/Cpefat mouse tissues, the majority of this activity is not due to CPE based on the sensitivity to p-chloromercuriphenyl sulfonate [20].
  • Taken together, these data suggest that CPE is completely inactive in the Cpefat/Cpefat mice, and that all of the CPE-like activity is due to other carboxypeptidases such as carboxypeptidase D. Levels of Leu-enkephalin in Cpefat/Cpefat mouse brain are approximately 5-fold lower than those in control brain [20].

Regulatory relationships of Cpe


Other interactions of Cpe

  • Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells [18].
  • Concordant deregulation of Cpe and Cpd in abnormal placentas of interspecies hybrids before the onset of IHPD phenotype and recapitulation of some phenotypes of IHPD hyperplastic placentas in Cpe mutant placentas suggests that these two genes are causally involved in IHPD and may function as speciation genes in the genus Mus [2].
  • Microarray-based transcriptional profiling of Cpe mutant placentas identified only a very small number of genes with altered expression, including Dtprp, which belongs to the prolactin gene family [2].
  • Several proSAAS-derived peptides were previously identified in the brain and pituitary of the Cpe(fat)/Cpe(fat) mouse based on the accumulation of C-terminally extended peptides due to the absence of enzymatically active carboxypeptidase E, a peptide-processing exopeptidase [21].
  • Effect of carboxypeptidase E deficiency on progastrin processing and gastrin messenger ribonucleic acid expression in mice with the fat mutation [22].

Analytical, diagnostic and therapeutic context of Cpe


  1. Cholesterol gallstone formation in overweight mice establishes that obesity per se is not linked directly to cholelithiasis risk. Bouchard, G., Johnson, D., Carver, T., Paigen, B., Carey, M.C. J. Lipid Res. (2002) [Pubmed]
  2. Carboxypeptidase E in the mouse placenta. Singh, U., Yu, Y., Kalinina, E., Konno, T., Sun, T., Ohta, H., Wakayama, T., Soares, M.J., Hemberger, M., Fundele, R.H. Differentiation (2006) [Pubmed]
  3. Altered processing of procholecystokinin in carboxypeptidase E-deficient fat mice: differential synthesis in neurons and endocrine cells. Lacourse, K.A., Friis-Hansen, L., Samuelson, L.C., Rehfeld, J.F. FEBS Lett. (1998) [Pubmed]
  4. Altered biosynthesis of neuropeptide processing enzyme carboxypeptidase E after brain ischemia: molecular mechanism and implication. Zhou, A., Minami, M., Zhu, X., Bae, S., Minthorne, J., Lan, J., Xiong, Z.G., Simon, R.P. J. Cereb. Blood Flow Metab. (2004) [Pubmed]
  5. Peptidomics of Cpe fat/fat mouse hypothalamus: effect of food deprivation and exercise on peptide levels. Che, F.Y., Yuan, Q., Kalinina, E., Fricker, L.D. J. Biol. Chem. (2005) [Pubmed]
  6. Regulated CPEB phosphorylation during meiotic progression suggests a mechanism for temporal control of maternal mRNA translation. Tay, J., Hodgman, R., Sarkissian, M., Richter, J.D. Genes Dev. (2003) [Pubmed]
  7. Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases. Rouillé, Y., Duguay, S.J., Lund, K., Furuta, M., Gong, Q., Lipkind, G., Oliva, A.A., Chan, S.J., Steiner, D.F. Frontiers in neuroendocrinology. (1995) [Pubmed]
  8. CPEB-mediated cytoplasmic polyadenylation and the regulation of experience-dependent translation of alpha-CaMKII mRNA at synapses. Wu, L., Wells, D., Tay, J., Mendis, D., Abbott, M.A., Barnitt, A., Quinlan, E., Heynen, A., Fallon, J.R., Richter, J.D. Neuron (1998) [Pubmed]
  9. Carboxypeptidase e: a surprise player in protein sorting. Kling, J. Nat. Biotechnol. (1997) [Pubmed]
  10. Identification of peptides from brain and pituitary of Cpe(fat)/Cpe(fat) mice. Che, F.Y., Yan, L., Li, H., Mzhavia, N., Devi, L.A., Fricker, L.D. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  11. The antiviral activity of tumour necrosis factor on herpes simplex virus type 1: role for a butylated hydroxyanisole sensitive factor. Lidbury, B.A., Ramshaw, I.A., Rolph, M.S., Cowden, W.B. Arch. Virol. (1995) [Pubmed]
  12. Augmented responses to ozone in obese carboxypeptidase E-deficient mice. Johnston, R.A., Theman, T.A., Shore, S.A. Am. J. Physiol. Regul. Integr. Comp. Physiol. (2006) [Pubmed]
  13. Altered neuropeptide processing in prefrontal cortex of Cpe (fat/fat) mice: implications for neuropeptide discovery. Lim, J., Berezniuk, I., Che, F.Y., Parikh, R., Biswas, R., Pan, H., Fricker, L.D. J. Neurochem. (2006) [Pubmed]
  14. Carboxypeptidase E is required for normal synaptic transmission from photoreceptors to the inner retina. Zhu, X., Wu, K., Rife, L., Cawley, N.X., Brown, B., Adams, T., Teofilo, K., Lillo, C., Williams, D.S., Loh, Y.P., Craft, C.M. J. Neurochem. (2005) [Pubmed]
  15. Induced and spontaneous mutations at Ser202 of carboxypeptidase E. Effect on enzyme expression, activity, and intracellular routing. Varlamov, O., Leiter, E.H., Fricker, L. J. Biol. Chem. (1996) [Pubmed]
  16. Proinsulin targeting to the regulated pathway is not impaired in carboxypeptidase E-deficient Cpefat/Cpefat mice. Irminger, J.C., Verchere, C.B., Meyer, K., Halban, P.A. J. Biol. Chem. (1997) [Pubmed]
  17. Obesity and diabetes in transgenic mice expressing proSAAS. Wei, S., Feng, Y., Che, F.Y., Pan, H., Mzhavia, N., Devi, L.A., McKinzie, A.A., Levin, N., Richards, W.G., Fricker, L.D. J. Endocrinol. (2004) [Pubmed]
  18. Role of carboxypeptidase E in processing of pro-islet amyloid polypeptide in {beta}-cells. Marzban, L., Soukhatcheva, G., Verchere, C.B. Endocrinology (2005) [Pubmed]
  19. Adult carboxypeptidase E-deficient fat/fat mice have a near-total depletion of brain CCK 8 accompanied by a massive accumulation of glycine and arginine extended CCK: identification of CCK 8 Gly as the immediate precursor of CCK 8 in rodent brain. Wang, W., Cain, B.M., Beinfeld, M.C. Endocrine (1998) [Pubmed]
  20. Carboxypeptidase E activity is deficient in mice with the fat mutation. Effect on peptide processing. Fricker, L.D., Berman, Y.L., Leiter, E.H., Devi, L.A. J. Biol. Chem. (1996) [Pubmed]
  21. ProSAAS processing in mouse brain and pituitary. Mzhavia, N., Berman, Y., Che, F.Y., Fricker, L.D., Devi, L.A. J. Biol. Chem. (2001) [Pubmed]
  22. Effect of carboxypeptidase E deficiency on progastrin processing and gastrin messenger ribonucleic acid expression in mice with the fat mutation. Udupi, V., Gomez, P., Song, L., Varlamov, O., Reed, J.T., Leiter, E.H., Fricker, L.D., Greeley, G.H. Endocrinology (1997) [Pubmed]
  23. Beta-cell lines derived from transgenic Cpe(fat)/Cpe(fat) mice are defective in carboxypeptidase E and proinsulin processing. Varlamov, O., Fricker, L.D., Furukawa, H., Steiner, D.F., Langley, S.H., Leiter, E.H. Endocrinology (1997) [Pubmed]
  24. Radiosensitivity of small-cell lung cancer xenografts compared with activity of c-myc, N-myc, L-myc, c-raf-1 and K-ras proto-oncogenes. Rygaard, K., Slebos, R.J., Spang-Thomsen, M. Int. J. Cancer (1991) [Pubmed]
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