Molecular cloning demonstrates structural features of homologous bovine prohormone convertases 1 and 2

DNA and Cell Biology

Volumn 19, Issue 7, 2000, Pages 409-419

  Hwang, Shin Rong ^a   Ng, Siu Ming ^a   Steineckert, Brent ^a   Seidah, Nabil G ^b   Hook, Vivian Y H ^a,c  

^a UNIVERSITY OF CALIFORNIA SAN DIEGO   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c CLIN RESEARCH INSTITUTE OF MONTREAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; FURIN; HISTAMINE; SERINE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; GENE EXPRESSION; GENE ISOLATION; GENETIC CONSERVATION; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN;

ADRENAL MEDULLA; AMINO ACID SEQUENCE; ANIMALS; ASPARTIC ENDOPEPTIDASES; BASE SEQUENCE; CATTLE; CLONING, MOLECULAR; DNA, COMPLEMENTARY; GENE EXPRESSION REGULATION, ENZYMOLOGIC; MOLECULAR SEQUENCE DATA; PROPROTEIN CONVERTASE 2; PROPROTEIN CONVERTASES; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID; SUBTILISINS;

ANIMALIA; BOVINAE; EUKARYOTA; MAMMALIA;

EID: 0033865381     PISSN: 10445498     EISSN: None     Source Type: Journal    
DOI: 10.1089/10445490050085906     Document Type: Article

References (45)

1. Azaryan, A.V., Krieger, T.J., and Hook, V.Y.H. (1995). 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.
2. Benjannet, S., Rondeau, N., Day, R., Chrétien, M., and Seidah, N.G. (1991). PC1 and PC2 are pro-protein convertases capable of cleaving POMC at distinct pairs of basic residues. Proc. Natl. Acad. Sci. USA 88, 3564-3568.
3. Benjannet, S., Mamarbachi, A.M., Hamelin, J., Savaria, D., Munzer, J.S., Chrétien, M., and Seidah, N.G. (1998). Residues unique to the prohormone convertase PC2 modulate its autoactivation, binding to 7B2 and enzymatic activity. FEBS Lett. 428, 37-42.
4. Bloomquist, B.T., Eipper, B.A., and Mains, R.E. (1991). Prohormone-converting enzymes: Regulation and evaluation of function using antisense RNA. Mol. Endocrinol. 5, 2014-2024.
5. Braks, J.A., and Martens, G.J. (1994). 7B2 is a neuroendocrine chaperone that transiently interacts with prohormone convertase PC2 in the secretory pathway. Cell 78, 263-273.
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. Cawley, N.X., Cool, D.R., Normant, E., Shen, F.S., Olsen, V., and Loh Y.P. (1998). The mechanism of sorting propiomelanocortin to secretory granules and its processing by aspartic and PC enzymes. In Proteolytic and Cellular Mechanisms in Prohormone and Proprotine Processing. V.Y.H. Hook, ed. (Landes Bioscience Publishers, Austin, TX) pp. 29-48.
8. Creemers, J.W., Roebroek, A.J., and Van De Ven, W.J. (1992). Expression in human lung tumor cells of the proprotein processing enzyme PC1/PC2, cloning and primary sequence of a 5 kb cDNA. FEBS Lett. 300, 82-88.
9. Dhanvantari, S., Seidah, N.G., and Brubaker, P.L. (1996). Role of prohormone convertases in the tissue-specific processing of proglucagon. Mol. Endocrinol. 10, 342-355.
10. Duguay, S.J., Milewski, W.M., Young, D., Nakayama, K., and Steiner, D.F. (1997). Processing of wild-type and mutant proinsulin-like growth factor-IA by subtilisin-related proprotein convertases. J. Biol. Chem. 272, 6663-6670.
11. Estivariz, F.E., Friedman, T.C., Chikuma, T., and Loh Y.P. (1992). Processing of adrenocorticotropin by two proteases in bovine intermediate lobe secretory vesicle membranes: A distinct acidic, tetrabasic residue-specific calcium-activated serine protease and a PC2-like enzyme. J. Biol. Chem. 267, 7456-7463.
12. Ftouhi, N., Day, R., Mbikay, M., Chrétien, M., and Seidah, N.G. (1994). Gene organization of the mouse pro-hormone and pro-protein convertase PC1. DNA Cell Biol. 13, 395-407.
13. Furuta, M., Carroll, R., Martin, S., Swift, H.H., Ravazzola, M., Orci, L., and Steiner, D.F. (1998). Incomplete processing of proinsulin to insulin accompanied by elevation of Des31,32 proinsulin intermediates in islets of mice lacking active PC2. J. Biol. Chem. 273, 3431-3437.
14. Gierasch, L.M. (1989). Signal sequences. Biochemistry 28, 923-930.
15. Hill, R.M., Ledgerwood, E.C., Brennan, S.O., Pu, L.P., Loh, Y.P., Christie, D.L., and Birch, N. (1995). Comparison of the molecular forms of the kex2/subtilisin-like serine proteases SPC2, SPC3, and furin in neuroendocrine secretory vesicles reveals differences in carboxyl-terminus truncation and membrane association. J. Neurochem. 65, 2318-2326.
16. Holzward, M.A. (1984). The distribution of vasoactive intestinal peptide in the rat adrenal cortex and medulla. J. Auton. Nerv. Syst. 11, 269-283.
17. Hook, V.Y.H., Azaryan, A.V., and Hwang, S.R. (1994). Proteases and the emerging role of protease inhibitors in prohormone processing. FASEB J. 8, 1269-1278.
18. Hook, V.Y.H., Kang, Y.H., Schiller, M., Tezapsidis, N., Johnston, J.M., and Azaryan, A. (1998). Prohormone thiol protease (PTP), a novel cysteine protease for proenkephalin and prohormone processing. In Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing. V.Y.H. Hook, ed. (Landes Bioscience Publishers, Austin, TX) pp. 89-104.
19. Hook, V.Y.H., and Yasothornsrikul, S. (1998). Carboxypeptidase and aminopeptidase proteases in proneuropeptide processing. In Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing. V.Y.H. Hook, ed. (Landes Bioscience Publishers, Austin, TX) pp. 121-140.
20. 1-antichymotrypsin. Proc. Natl. Acad. Sci. USA 91, 9579-9583.
21. 1-antichymotrypsin from bovine adrenal medulla and pituitary revealed by molecular cloning. FEBS Lett. 368, 471-476.
22. 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.
23. Kirchmair, R., Egger, C., Gee, P., Hogue-Angelletti, R., Fischer-Colbrie, R., Laslop, A., and Wikler, H. (1992a). Differential subcellular distribution of PC1, PC2 and furin in bovine adrenal medulla and secretion of PC1 and PC2 from this tissue. Neurosci. Lett. 143, 143-145.
24. Kirchmair, R., Gee, P., Hogue-Angeletti, R., Laslop, A., Rischer-Colbrie, R., and Winkler, H. (1992b). Immunological characterization of the endoproteases PC1 and PC2 in adrenal chromaffin granules and in the pituitary gland. FEBS Lett. 297, 302-305.
25. Kornfeld, R., and Kornfeld, S. (1985). Assembly of asparagine-linked oligosaccharides. Annu. Rev. Biochem. 54, 631-664.
26. Lipkind, G.M., Zhou, A., and Steiner, D.F. (1998). A model for the structure of the P domains in the subtilisin-like prohormone convertases. Proc. Natl. Acad. Sci. USA 95, 7310-7315.
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. 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.
29. Malide, D., Seidah, N.G., Chrétien, M., and Bendayan, M. (1995). Electron microscopy immunocytochemical evidence for the involvement of the convertases PC1 and PC2 in the processing of proinsulin in pancreatic beta-cells. J. Histochem. Cytochem. 43, 11-19.
30. Muller, L., Zhu, X., and Lindberg, I. (1997). Mechanism of the facilitation of PC2 maturation by 7B2: Involvement in ProPC2 transport and activation but not folding. J. Cell Biol. 139, 625-638.
31. Parish, D.C., Tuteja, R., Altstein, M., Gainer, H., and Loh, Y.P. (1986). Purification and characterization of a paired basic residue-specific prohormone-converting enzyme from bovine pituitary neural lobe secretory vesicles. J. Biol. Chem. 261, 14392-14397.
32. Rothenberg, M.E., Eilertson, C.D., Klein, K., Mackin, R.B., and Noe, B.D. (1996). Evidence for redundancy in propeptide/prohormone convertase activities in processing proglucagon: An antisense study. Endocrinology 10, 331-341.
33. Rovère, C., Luis, J., Lissitzky, J.-C., Basak, A., Marvaldi, J., Chrétien, M., and Seidah, N.G. (1999). The RGD motif and the C-terminal segment of proprotein convertase 1 are critical for its cellular trafficking but not for its intracellular binding to integrin a5/b1. J. Biol. Chem. 274, 12461-12467.
34. Schultzberg, M., Hokfelt, T., Lundberg, J.M., Terenius, L., Elfvin, L.G., and Elde, R. (1978). Enkephalin-like immunoreactivity in nerve terminals in sympathetic ganglia and adrenal medullary gland cells. Acta Physiol. Scand. 103, 475-477.
35. Seidah, N.G., Marcinkiewicz, M., Benjannet, S., Gaspar, L., Beaubien, G., Mattei M.G., Lazure, C., Mbikay, M., and Chrétien, M. (1991). Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, furin, and Kex2: Distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2. Mol. Endocrinol. 5, 111-122.
36. Seidah, N.G., Hamelin, J., Gaspar, A.M., Day, R., and Chrétien, M. (1992). The cDNA sequence of the human pro-hormone and pro-protein convertase PC1. DNA Cell Biol. 11, 283-289.
37. Seidah, N.G., and Chretien, M. (1997). Eukaryotic protein processing: Endoproteolysis of precursor proteins. Curr. Opin. Biotechnol. 8, 602-607.
38. Seidah, N.G., Mbikay, M., Marcinkiewicz, M., and Chretien, M. (1998). The mammalian precursor convertases: Paralogs of the subtilisin/kexin family of calcium-dependent serine proteinases. In Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing. V.Y.H. Hook, ed. (Landes Bioscience Publishers, Austin, TX) pp. 49-76.
39. Seidah, N.G., Mowla, S.J., Hamelin, J., Mamarbachi, A.M., Benjannet, S., Toure, B.B., Basak, A., Munzer, J.S., Marcinkiewicz, J., Zhong, M., Barale, J.C., Lazure, C., Murphy, R.A., Chretien, M., and Marcin-Kiewicz, M. (1999). Mammalian subtilisin/kexin isozyme SKI-1: A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization. Proc. Natl. Acad. Sci. USA 96, 1321-1326.
40. Smeekens, S.P., and Steiner, D.F. (1990). Identification of a human insulinoma cDNA encoding a novel mammalian protein structurally related to the yeast dibasic processing protease Kex2. J. Biol. Chem. 265, 2997-3000.
41. 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.
42. Thomas, L., Leduc, R., Thorne, B.A., Smeekens, S.P., Steiner, D.F., and Thomas, G. (1991). Kex2-like endoproteases PC2 and PC3 accurately cleave a model prohormone in mammalian cells: Evidence for a common core of neuroendocrine processing enzymes. Proc. Natl. Acad. Sci. USA 88, 5297-5301.
43. Udenfriend, S., and Kilpatrick, D.L. (1983). Biochemistry of enkephalins and enkephalin-containing peptides. Arch. Biochem. Biophys. 221, 309-323.
44. Yasothornsrikul, S., Aaron, W., Toneff, T., and Hook, V.Y.H. (1999). Evidence for the proenkephalin processing enzyme prohormone thiol protease (PTP) as a multicatalytic cysteine protease complex: Activation by glutathione localized to secretory vesicles. Biochemistry 38, 7421-7430.
45. Zhou, A., Martin, S., Lipkind, G., Lamendola, J., and Steiner, D.F. (1998). Regulatory roles of the P domain of the subtilisin-like prohormone convertases. J. Biol. Chem. 273, 11107-11114.