Specificity of the dynorphin-processing endoprotease: Comparison with prohormone convertases

Journal of Neurochemistry

Volumn 72, Issue 5, 1999, Pages 2120-2126

  Berman, Yemiliya ^a   Juliano, Luiz ^b   Devi, Lakshmi A ^a,c  

^a NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b FEDERAL UNIVERSITY OF SÃO PAULO   (Brazil)

^c NEW YORK UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Dynorphins; Enkephalin; Furin; Neuropeptide biosynthesis; Posttranslational processing; Prohormone convertases

Indexed keywords

DYNORPHIN; DYNORPHIN CONVERTING ENZYME; FURIN; LEUMORPHIN; NEUROPEPTIDE; PRORENIN; PROTEINASE; SYNTHETIC PEPTIDE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROLYSIS; MASS SPECTROMETRY; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN PROCESSING;

ASPARTIC ENDOPEPTIDASES; CYSTEINE ENDOPEPTIDASES; DYNORPHINS; FURIN; PEPTIDE FRAGMENTS; PROPROTEIN CONVERTASES; PROTEIN PROCESSING, POST-TRANSLATIONAL; SUBSTRATE SPECIFICITY; SUBTILISINS;

EID: 0032970381     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0722120.x     Document Type: Article

References (49)

1. Angliker H., Neumann U., Molloy S. S., and Thomas G. (1995) Internally quenched fluorogenic substrate for furin. Anal. Biochem. 224, 409-412.
2. Benjannet S., Mamarbachi A. M., Hamelin J., Savaria D., Munzer J. S., Chretien M., and Seidah N. G. (1998) Residues unique to the pro-hormone convertase PC2 modulate its autoactivation, binding to 7B2 and enzymatic activity. FEBS Lett. 428, 37-42.
3. Berman Y. L., Rattan A., and Devi L. A. (1994) Regional distribution of neuropeptide processing enzymes in adult rat brain. Biochimie 76, 245-250.
4. Berman Y. L., Juliano L., and Devi L. A. (1995) Purification and characterization of a dynorphin processing endoprotease. J. Biol. Chem. 270, 23845-23850.
5. Berman Y. L., Juliano L., Beavis R., and Devi L. A. (1997) Monobasic processing specificity of dynorphin converting enzyme, furin, prohormone convertase 1 and prohormone convertase 2. Soc. Neurosci. Abstr. 23, 2317.
6. Brenner C. and Fuller R. S. (1992) Structural and enzymatic characterization of a purified prohormone-processing enzyme: secreted soluble Kex2 protease. Proc. Natl. Acad. Sci. USA 89, 922-926.
7. Carmel A. and Yaron A. (1978) An intramolecularly quenched fluorescent tripeptide as a fluorogenic substrate of angiotensin-I-converting enzyme and of bacterial dipeptidyl carboxypeptidase. Eur. J. Biochem. 87, 265-273.
8. Chagas J. R., Juliano L., and Prado E. S. (1991) Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Anal. Biochem. 192, 419-425.
9. Chagas J. R., Hirata I. Y., Juliano M. A., Xiong W., Wang C., Chao J., Juliano L., and Prado E. S. (1992) Substrate specificities of tissue kallikrein and T-kininogenase: their possible role in kininogen processing. Biochemistry 31, 4969-4974.
10. Chesneau V., Pierottin A. R., Barre N., Creminon C., Tougard C., and Cohen P. (1994) Isolation and characterization of a dibasic selective metalloendopeptidase from rat testes that cleaves at the amino terminus of arginine residues. J. Biol. Chem. 269, 2056-2061.
11. Chu T. G. and Orlowski M. (1985) Soluble metalloendopeptidase from rat brain: action on enkephalin-containing peptides and other bioactive peptides. Endocrinology 116, 1418-1425.
12. Coates L. C. and Birch N. P. (1998) Differential cleavage of provasopressin by the major molecular forms of SPC3. J. Neurochem. 70, 1670-1678.
13. Day R., Lazure C., Basak A., Boudreault A., Limperis P., Dong W., and Lindberg I. (1998) Prodynorphin processing by proprotein convertase 2. J. Biol. Chem. 273, 829-836.
14. Devi L. A. (1991) Consensus sequence for processing of peptide precursors at monobasic sites. FEBS Lett. 280, 189-194.
15. Devi L. A. (1998) Dynorphin processing endoprotease, in Handbook of Proteolytic Enzymes (Woessner F., Rawling N., and Barrett A. J., eds), pp. 1449-1450. Academic Press, San Diego.
16. Devi L. and Goldstein A. (1989) Neuropeptide processing by single-step cleavage: conversion of leumorphin (dynorphin B-29) to dynorphin B. Biochem. Biophys. Res. Commun. 130, 1168-1176.
17. Devi L., Gupta P., and Fricker L. D. (1991) Subcellular localization, partial purification, and characterization of a dynorphin processing endopeptidase from bovine pituitary. J. Neurochem. 56, 320-329.
18. Docherty K. and Steiner D. F. (1982) Post-translational proteolysis in polypeptide hormone biosynthesis. Annu. Rev. Physiol. 44, 625-638.
19. Dupuy A., Lindberg I., Zhou Y., Akil H., Lazure C., Chretien M., Seidah N. G., and Day R. (1994) Processing of prodynorphin by the prohormone convertase PC1 results in high molecular weight intermediate forms. Cleavage at a single arginine residue. FEBS Lett. 337, 60-65.
20. Eipper B. A., Mains R. E., and Herbert E. (1986) Peptides in the nervous system. Trends Neurosci. 9, 463-468.
21. Fricker L. D. and Devi L. (1995) Enzymes involved in the synthesis of opioid peptides, in Pharmacology of Opioid Peptides (Tseng L. F., ed), pp. 87-107. Harwood Academic Press, Amsterdam.
22. Greco L., Daly L., Kim S., and Devi L. (1992) Dynorphin-processing endopeptidase in the rat anterior pituitary lactotrophic cell line, GH4C1. Neuroendocrinology 55, 351-356.
23. Gron H., Meldal M., and Breddam K. (1992) Extensive comparison of the substrate preferences of two subtilisins as determined with peptide substrates which are based on the principle of intramolecular quenching. Biochemistry 31, 6011-6018.
24. Hersh L. B., Gafford J. T., Powers J. C., Tanaka T., and Erdos E. G. (1983) Novel substrates for angiotensin I converting enzyme. Biochem. Biophys. Res. Commun. 110, 654-659.
25. Hirata I. S., Cexari M. H. S., Nakaie C. R., Boschcov P., Ito A. S., Juliano M. A., and Juliano L. (1994) Internally quenched fluorogenic protease substrates: solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs. Lett. Peptide Sci. 1, 299-308.
26. Jean F., Basak A., Rondeau N., Benjannet S., Hendy G. N., Seidah N. G., Chretien M., and Lazure C. (1993) Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells. Biochem. J. 292, 891-900.
27. Jean F., Boudreault A., Basak A., Seidah N. G., and Lazure C. (1995) Fluorescent peptidyl substrates as an aid in studying the substrate specificity of human prohormone convertase PC1 and human furin and designing a potent irreversible inhibitor. J. Biol Chem. 270, 19225-19231.
28. Johanning K., Juliano M. A., Juliano L., Lazure C., Lamango N. S., Steiner D. F., and Lindberg I. (1998) Specificity of prohormone convertase 2 on proenkephalin and proenkephalin-related substrates. J. Biol. Chem. 273, 22672-22680.
29. Jutras I., Seidah N. G., Reudelhuber T. L., and Brechler V. (1997) Two activation states of the prohormone convertase PC1 in the secretory pathway. J. Biol. Chem. 272, 15184-15188.
30. Laslop A., Weiss C., Savaria D., Eiter C., Tooze S. A., Seidah N. G., and Winkler H. (1998) Proteolytic processing of chromogranin B and secretogranin II by prohormone convertases. J. Neurochem. 70, 374-383.
31. Lindberg I., van den Hurk W., Bui C., and Batie C. J. (1995) Enzymatic characterization of immunopurified prohormone convertase 2: potent inhibition by a 7B2 fragment. Biochemistry 34, 5486-5493.
32. Lusson J., Benjannet S., Hamelin J., Savaria D., Chretien M., and Seidah N. G. (1997) The integrity of the RRGDL sequence of the proprotein convertase PC1 is critical for its zymogen and C-terminal processing and for its cellular trafficking. Biochem. J. 326, 737-744.
33. Mains R. E., Dickerson I. M., May V., Stoffers D. A., Perkins S. N., Ouafik L. H., Husten E. J., and Eipper B. A. (1990) Cellular and molecular aspects of peptide hormone biosynthesis. Front. Endocrinol. 11, 52-89.
34. Matayoshi E. D., Wang G. T., Krafft G. A., and Erickson J. (1990) Novel flurogenic substrates for assaying retroviral proteases by resonance energy transfer. Science 247, 954-958.
35. Meldal M. and Breddam K. (1991) Anthranilamide and nitrotyrosine as a donor-acceptor pair in internally quenched fluorescent substrates for endopeptidases: multicolumn peptide synthesis of enzyme substrates for subtilisin Carlsberg and pepsin. Anal. Biochem. 195, 141-147.
36. Nakayama K. (1997) Furin: a mammalian subtilisin/Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem. J. 327, 625-635.
37. Ng M. and Auld D. S. (1989) A fluorescent oligopeptide energy transfer assay with broad applications for neutral proteases. Anal. Biochem. 183, 50-56.
38. Orlowski M., Michaud C., and Chu T. G. (1988) A soluble metalloendopeptidase from rat brain: purification of the enzyme and determination of specificity with synthetic and natural peptides. Eur. J. Biochem. 135, 81-88.
39. Petanceska S., Zikherman J., Flicker L. D., and Devi L. (1993) Processing of prodynorphin in BRL-3A cells, a rat liver-derived cell line: implications for the specificity of processing neuropeptide-processing enzymes. Mol. Cell. Endocrinol. 94, 37-45.
40. Safavi A., Miller B. C., Cottam L., and Hersh L. B. (1996) Identification of gamma-endorphin generating enzyme as insulin-degrading enzyme. Biochemistry 35, 14318-14325.
41. Seidah N. G. (1995) The mammalian family of subtilisin/Kexin-like pro-protein convertases, in Intramolecular Chaperones and Protein Folding (Shinde U. and Inouye M., eds), pp. 181-203. R. G. Landes, Austin, Texas.
42. Seidah N. G. and Chretien M. (1994) Pro-protein convertases of subtilisin/kexin family. Methods Enzymol. 244, 175-188.
43. Seidah N. G., Chretien M., and Day R. (1994) The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions. Biochimie 76, 197-209.
44. Seidah N. G., Day R., Marcinkiewicz M., and Chretien M. (1998) Precursor convertases: an evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins. Ann. NY Acad. Sci. 839, 9-24.
45. Steiner D. F. (1991) The biosynthesis of biologically active peptides: a perspective, in Peptide Biosynthesis and Processing (Fricker L. D., ed), pp. 1-16. CRC Press, Boca Raton, Florida.
46. Steiner D. F. (1998) The proprotein convertases. Curr. Opin. Chem. Biol. 2, 31-39.
47. Tisljar U., Knight C. G., and Barrett A. J. (1990) An alternative quenched fluorescence substrate for pz-peptidase. Anal. Biochem. 186, 112-115.
48. Yaron A., Carmel A., and Karchalski-Katzer E. (1979) Intramolecularly quenched fluorogenic substrates for hydrolytic enzymes. Anal. Biochem. 95, 228-235.
49. Yasothornsrikul S., Toneff T., Hwang S.-R., and Hook V. Y. (1998) Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: relevance to prohormone processing. J. Neurochem. 70, 153-163.