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Cloning and sequence analysis of cDNA for bovine carboxypeptidase E

Nature volume 323, pages 461–464 (1986)Cite this article

Abstract

Carboxypeptidase E (enkephalin convertase) was first identified as the carboxypeptidase B-like enzyme involved in the biosynthesis of enkephalin in bovine adrenal chromaffin granules1. A similar enzyme is present in many brain regions1,2 and in purified secretory granules from rat pituitary3 and rat insulinoma4. Within the secretory granules, carboxypeptidase E (CPE) activity is found in both a soluble and a membrane-bound form1, 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. This cDNA hybridizes to bovine pituitary poly(A)+ RNAs of approximately 3.3, 2.6 and 2.1 kilobases (kb), with the 3.3-kb messenger RNA the predominant species. 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. This is consistent with a broad role for CPE in the biosynthesis of many neuropeptides.

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References

  1. Flicker, L. D. & Snyder, S. H. Proc. natn. Acad. Sci. U.S.A. 79, 3886–3890 (1982).

    Article  ADS  Google Scholar 

  2. Fricker, L. D., Supattapone, S. & Snyder, S. H. Life Sci. 31, 1841–1844 (1982).

    Article  CAS  Google Scholar 

  3. Hook, V. Y. H. & Loh, Y. P. Proc. natn. Acad. Sci. U.S.A. 81, 2776–2780 (1984).

    Article  ADS  CAS  Google Scholar 

  4. Docherty, K. & Hutton, J. C. FEBS Lett. 162, 137–141 (1983).

    Article  CAS  Google Scholar 

  5. Supattapone, S., Fricker, L. D. & Snyder, S. H. J. Neurochem. 42, 1017–1023 (1984).

    Article  CAS  Google Scholar 

  6. Fricker, L. D. & Snyder, S. H. J. biol. Chem. 258, 10950–10955 (1983).

    CAS  PubMed  Google Scholar 

  7. Lorenz, R. G. et al. Peptides (in the press).

  8. Caruthers, M. H. Science 230, 281–285 (1985).

    Article  ADS  CAS  Google Scholar 

  9. Okayama, H. & Berg, P. Molec. cell. Biol. 2, 161–170 (1982).

    Article  CAS  Google Scholar 

  10. Maniatis, T., Fitsch, E. F. & Sambrook, J. in Molecular Cloning (Cold Spring Harbor Laboratory, New York, 1982).

    Google Scholar 

  11. Lindberg, I., Yang, H. Y. T. & Costa, E. J Neurochem. 42, 1411–1419 (1984).

    Article  CAS  Google Scholar 

  12. Loh, Y. P., Parish, D. C. & Tuteja, R. J. biol. Chem. 260, 7194–7205 (1985).

    CAS  PubMed  Google Scholar 

  13. Chou, P. Y. & Fasman, G. D. A. Rev. Biochem. 47, 251–276 (1978).

    Article  CAS  Google Scholar 

  14. Schmid, M. F. & Herriott, J. R. J. molec. Biol. 103, 175–190 (1976).

    Article  CAS  Google Scholar 

  15. Rees, D. C., Lewis, M., Honzatko, R. B., Lipscomb, W. N. & Hardman, K. D. Proc. natn. Acad. Sci. U.S.A. 78, 3408–3412 (1981).

    Article  ADS  CAS  Google Scholar 

  16. Folk, J. E. in Enzymes (ed. Boyer, P. D.) 57–79 (Academic, New York, 1971).

    Google Scholar 

  17. Hindley, J. in DNA Sequencing (eds Work, T. S. & Burdon, R. H.) 121–229 (Elsevier, Amsterdam, 1983).

    Google Scholar 

Download references

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Authors and Affiliations

  1. Institute for Advanced Biomedical Research, Oregon Health Sciences University, 3181 SW Sam Jackson Park Road, Portland, Oregon, 97201, USA

    Lloyd D. Fricker & Edward Herbert

  2. Nancy Pritzker Laboratory, Stanford Medical Center, Stanford, California, 94395, USA

    Chris J. Evans

  3. Laboratories for Neuroendocrinology, Salk Institute for BiologicalStudies, 10010 North Torrey Pine Road, La Jolla, California, 92037, USA

    Fred S. Esch

Authors
  1. Lloyd D. Fricker
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  2. Chris J. Evans
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  3. Fred S. Esch
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  4. Edward Herbert
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Fricker, L., Evans, C., Esch, F. et al. Cloning and sequence analysis of cDNA for bovine carboxypeptidase E. Nature 323, 461–464 (1986). https://doi.org/10.1038/323461a0

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