Arginine and lysine aminopeptidase activities in chromaffin granules of bovine adrenal medulla: Relevance to prohormone processing

Journal of Neurochemistry

Volumn 70, Issue 1, 1998, Pages 153-163

  Yasothornsrikul, Sukkid ^a   Toneff, Thomas ^a   Hwang, Shin Rong ^a   Hook, Vivian Y H ^a  

^a UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

Author keywords

Aminopeptidases; Arginine; Enkephalin; Lysine; Neuropeptides; Prohormone processing

Indexed keywords

AMASTATIN; AMINOPEPTIDASE; AMINOPEPTIDASE INHIBITOR; ARGININE; ARPHAMENINE A; BESTATIN; HORMONE PRECURSOR; HYDROXYMERCURIBENZOIC ACID; LYSINE; MERCAPTOETHANOL; METENKEPHALIN; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

ADRENAL MEDULLA; ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CATTLE; CELLULAR DISTRIBUTION; CHROMAFFIN GRANULE; CONTROLLED STUDY; ENZYME ACTIVITY; METAL BINDING; NEUROSECRETORY CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING;

ANIMALIA; BOS TAURUS; BOVINAE;

EID: 0031982551     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1998.70010153.x     Document Type: Article

References (37)

1. Azaryan A. V. and Hook V. Y. H. (1994) Distinct properties of "prohormone thiol protease" (PTP) compared to cathepsins B, L, and H: evidence for PTP as a novel cysteine protease. Arch. Biochem. Biophys. 314, 171-177.
2. Azaryan A. V., Schiller M. Mende-Mueller L., and Hook V. Y. H. (1995a) Characteristics of the chromaffin granule aspartic proteinase involved in proenkephalin processing. J. Neurochem. 65, 1771-1779.
3. Azaryan A. V., Krieger T. J., and Hook V. Y. H. (1995b) Purification and characteristics of the candidate prohormone processing proteases PC2 and PC1/3 from bovine adrenal medulla chromaffin granules. J. Biol. Chem. 270, 8201-8208.
4. Cadel S., Pierotti A. R., Foulon T., Creminon C., Barre N., Segretain D., and Cohen P. (1995) Aminopeptidase-B in the rat testes: isolation, functional properties and cellular localization in the seminiferous tubules. Mol. Cell. Endocrinol. 110, 149-160.
5. Cadel S., Foulon V., Viron A., Balogh A., Midol-Monnet S., Noel N., and Cohen P. (1997) Aminopeptidase B from the rat testis is a bifunctional enzyme structurally related to leukotriene-A4 hydrolase. Proc. Natl. Acad. Sci. USA 94, 2963-2968.
6. Carmichael W. S., Stoddard S. L., O'Connor D. T., Yaksh T. L., and Tyce G. M. (1990) The secretion of catecholamines, chromogranin A and neuropeptide Y from the adrenal medulla of the cat via the adrenolumbar vein and thoracic duct: different anatomic routes based on size. Neuroscience 34, 433-440.
7. Castro M. G., Birch N. P., and Loh Y. P. (1989) Regulated secretion of pro-opiomelanocortin converting enzyme and an aminopeptidase B-like enzyme from dispersed bovine intermediate lobe pituitary cells. J. Neurochem. 52, 1619-1628.
8. Christie D., Batchelor D. C., and Palmer D. J. (1991) Identification of kex2-related proteases in chromaffin granules by partial amino acid sequence analysis. J. Biol. Chem. 255, 15679-15683.
9. Davidson H. W., Rhodes C. J., and Hutton J. C. (1988) Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic β cell via two distinct site-specific endopeptidases. Nature 333, 93-96.
10. Docherty K. and Steiner D. F. (1982) Post-translational proteolysis in polypeptide hormone biosynthesis. Annu. Rev. Physiol. 44, 625-638.
11. Flores M., Aristoy M. C., and Toldra F. (1993) HPLC purification and characterization of porcine muscle aminopeptidase B. Biochimie 75, 861-867.
12. Fricker L. D. (1991) Peptide processing exopeptidases: amino and carboxypeptidases involved with peptide biosynthesis, in Peptide Biosynthesis and Processing (Fricker L. D., ed), pp. 199-229. CRC Press, Boca Raton.
13. Fricker L. D. and Snyder S. H. (1982) Enkephalin convertase: purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules. Proc. Natl. Acad. Sci. USA 79, 3886-3890.
14. Gainer H., Russell J. T., and Loh P. Y. (1984) An aminopeptidase activity in bovine pituitary secretory vesicles that cleaves the N-terminal arginine from beta-lipotropin 60-65. FEBS Lett. 175, 135-139.
15. Gainer H., Russell J. T., and Loh Y. P. (1985) The enzymology and intracellular organization of peptide precursor processing: the secretory vesicle hypothesis. Neuroendocrinology 40, 171-184.
16. Gomez S., Gluschankof P., Lepage A., and Cohen P. (1988) Relationship between endo- and exopeptidases in a processing enzyme system: activation of an endoprotease by the aminopeptidase B-like activity in somatostatin-28 convertase. Proc. Natl. Acad. Sci. USA 85, 5468-5472.
17. 125I-(Met)enkephalin in bovine adrenal medullary chromaffin granules. FEBS Lett. 172, 212-218.
18. Hook V. Y. H., Eiden L. E., and Brownstein M. J. (1982) A carboxypeptidase processing enzyme for enkephalin precursors. Nature 295, 341-342.
19. Hook V. Y., Azaryan A. V., Hwang S. R., and Tezapsidis N. (1994) Proteases and the emerging role of protease inhibitors in prohormone processing. FASEB J. 8, 1269-1278.
20. Hook V. Y. H., Schiller M. R., and Azaryan A. V. (1996a) The processing proteases "prohormone thiol protease," PC1/3 and PC2, and 70-kDa aspartic proteinase show preferences among proenkephalin, proneuropeptide Y, and proopiomelanocortin substrates. Arch. Biochem. Biophys. 328, 107-114.
21. Hook V. Y. H., Schiller M. R., Azaryan A. V., and Tezapsidis N. (1996b) Proenkephalin-processing enzymes in chromaffin granules: a model for neuropeptide biosynthesis. Ann. NY Acad. Sci. 780, 121-133.
22. Krieger T. J. and Hook V. Y. (1991) Purification and characterization of a novel thiol protease involved in processing the enkephalin precursor. J. Biol. Chem. 266, 8376-8383.
23. Krieger T. J., Mende-Mueller L., and Hook V. Y. H. (1992) Prohormone thiol protease and enkephalin precursor processing: cleavage at dibasic and monobasic sites. J. Neurochem. 59, 26-31.
24. Loh Y. P., Parish D. C., and Tuteja R. (1985) Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles. J. Biol. Chem. 260, 7194-7205.
25. Loh Y. P., Beinfeld M. C., and Birch N. P. (1993) Prohormone processing : the role of propeptides in intracellular sorting, precursor processing, and secretion, in Mechanisms of Intracellular Trafficking and Processing of Proproteins (Loh Y. P., ed), pp. 179-224. CRC Press, Boca Raton.
26. Lowry O. H., Rosebrough N. J., Farr A. L., and Randall R. J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 265-275.
27. Lundberg J. M., Hamberger B., Schultzberg M., Hokfelt T., Granberg P. O., Efendie S., Terenius L., Goldstein M., and Luft R. (1979) Enkephalin- and somatostatin-like immunoreactivities in human adrenal medulla and pheochromocytoma. Proc. Natl. Acad. Sci. USA 76, 4079-4083.
28. Mantle D. (1992) Comparison of soluble aminopeptidases in human cerebral cortex, skeletal muscle and kidney tissues. Clin. Chim. Acta 207, 107-118.
29. Mantle D., Lauffart B., McDermott J. R., Kidd A. M., and Pennington R. J. T. (1985) Purification and characterization of two Cl-activated aminopeptidases hydrolysing basic termini from human skeletal muscle. Eur. J. Biochem. 147, 307-312.
30. McDermott J. R., Mantle D., Lauffart B., Gibson A. M., and Biggins J. A. (1988) Purification and characterization of two soluble deactivated arginyl aminopeptidases from human brain and their endopeptidase action on neuropeptides. J. Neurochem. 50, 176-182.
31. 31P nuclear magnetic resonance spectroscopy. J. Biol. Chem. 254, 1170-1177.
32. Seidah N. G., Chretien M., and Day R. (1994) The family of subtilisin/kexin-like proprotein and pro-hormone convertases: divergent or shared functions. Biochimie 76, 197-209.
33. Steiner D. F., Smeekens S. P., Ohagi S., and Chan S. J. (1992) The new enzymology of precursor processing endoproteases. J. Biol. Chem. 267, 23435-23438.
34. Taylor A. (1993) Aminopeptidases: structure and function. FASEB J. 7, 290-298.
35. Tezapsidis N., Noctor S., Kannan R., Krieger T. J., Mende-Mueller L., and Hook V. Y. H. (1995) Stimulation of 'prohormone thiol protease' (PTP) and [Met]enkephalin by a cysteine protease inhibitor of PTP. J. Biol. Chem. 270, 13285-13290.
36. Ungar A. and Phillips J. H. (1983) Regulation of the adrenal medulla. Physiol. Rev. 63, 787-843.
37. Webb E. C. (1986) Nomenclature Committee of the International Union of Biochemistry (NC-IUB) enzyme nomenclature recommendations. Eur. J. Biochem. 157, 16.