Carboxypeptidase E is a sorting receptor for prohormones: Binding and kinetic studies

Molecular and Cellular Endocrinology

Volumn 139, Issue 1-2, 1998, Pages 7-13

  Cool, David R ^a   Loh, Y Peng ^a  

^a EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH AND HUMAN DEVELOPMENT   (United States)

Author keywords

Carboxypeptidase H; Chromogranin A; Proenkephalin; Prohormone sorting; Proinsulin

Indexed keywords

BICARBONATE; CARBOXYPEPTIDASE H; CHROMOGRANIN A; HORMONE PRECURSOR; HORMONE RECEPTOR; MEMBRANE ENZYME; PROENKEPHALIN; PROINSULIN; PROOPIOMELANOCORTIN; SIGNAL PEPTIDE;

ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; BINDING KINETICS; CONTROLLED STUDY; HORMONE RECEPTOR INTERACTION; HYPOPHYSIS; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING; SECRETORY GRANULE;

EID: 0032580247     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0303-7207(98)00081-1     Document Type: Article

References (28)

1. Carnell L., Moore H-P.H. Transport via the regulated secretory pathway in semi-intact PC12 cells: Role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II. J. Cell Biol. 127:1994;693-705.
2. Chanat E., Weiss U., Huttner W.B., Tooze S.A. Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its mis-sorting to the constitutive secretory pathway. EMBO J. 12:1993;2159-2168.
3. Chanat E., Weiss U., Huttner W.B. The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans-Golgi network. FEBS Lett. 351:1994;225-230.
4. Chandra S., Kable E.P.W., Morrison G.H., Webb W.W. Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy. J. Cell Sci. 10:1991;747-752.
5. Colomer V., Kicska G.A., Rindler M.J. Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH. J. Biol. Chem. 271:1996;48-55.
6. Cool D.R., Fenger M., Snell C.R., Loh Y.P. Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway. J. Biol. Chem. 270:1995;8723-8729.
7. Cool D.R., Loh Y.P. Identification of a sorting signal for the regulated secretory pathway at the N-terminus of pro-opiomelanocortin. Biochimie. 76:1994;265-270.
8. Cool D.R., Louie D.Y., Loh Y.P. Yeast aspartic protease 3 (YAP3p) is sorted to secretory granules and activated to process pro-opiomelanocortin in PC12 cells. Endocrinology. 137:1996;5441-5446.
9. fat mice. Cell. 88:1997;73-83.
10. Estivariz F.E., Birch N.P., Loh Y.P. Generation of lys-γ3melanotropin from pro-opiomelanocortin by a bovine intermediate lobe secretory vesicle membrane-associated aspartic protease and purified proopiomelanocortin converting enzyme. J. Biol. Chem. 264:1989;17796-17801.
11. Fricker L.D. Carboxypeptidase E. Annu. Rev. Physiol. 50:1988;309-321.
12. Fricker L., Das B., Angeletti R. Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10). J. Biol. Chem. 265:1990;2476-2482.
13. Hook V.Y.H. Differential distribution of carboxypeptidase processing enzyme activity and immunoreactivity in membrane and soluble components of chromaffin granules. J. Neurochem. 45:1985;987-989.
14. Jung L.J., Kreiner T., Scheller R.H. Expression of mutant ELH prohormones in AtT-20 cells: The relationship between prohormone processing and sorting. J. Cell Biol. 121:1993;11-21.
15. Kuliawat R., Arvan P. Protein targeting via the 'constitutive-like' secretory pathway in isolated pancreatic islets: Passive sorting in the immature granule compartment. J. Cell Biol. 118:1992;521-529.
16. Loh Y.P., Tam W.W.H., Russell J.T. Measurement of Δ-pH and membrane potential in secretory vesicles isolated from bovine pituitary intermediate lobe. J. Biol. Chem. 259:1984;8238-8245.
17. Mitra A., Song L., Fricker L.D. The C-terminal region of carboxypeptidase E is involved in membrane binding and intracellular routing in AtT-20 cells. J. Biol. Chem. 269:1994;19876-19881.
18. Moore H-P.H., Walker M.L., Lee F., Kelly R.B. Expressing a human proinsulin cDNA in a mouse ACTH-secreting cell. Intracellular storage, proteolytic processing, and secretion on stimulation. Cell. 35:1983;531-538.
19. Normant, E., Loh, Y.P., 1998. Depletion of carboxypeptidase E, a regulated secretory pathway receptor, causes misrouting and constitutive secretion of proinsulin, proenkephalin but not chromogranin A. Endocrinology (in press).
20. Orci L., Ravazzola M., Amherdt M., Perrelet A., Powell S.K., Quinn D.L., Moore H-P.H. The trans-most cisternae of the Golgi complex: A compartment for sorting of secretory and plasma membrane proteins. Cell. 51:1987;1039-1051.
21. 2-terminal sequences. J. Biol. Chem. 265:1990;17101-17105.
22. Pekar A.H., Frank B.H. Conformation of proinsulin. A comparison of insulin and proinsulin self-association at neutral pH. Biochemistry. 11:1972;4013-4016.
23. Schnabel E., Mains R.E., Farquhar M.G. Proteolytic processing of pro-ACTH/Endorphin begins in the Golgi complex of pituitary corticotropes and AtT20 cells. Mol. Endocrinol. 3:1989;1223-1235.
24. fat mice associated with a carboxypeptidase E mutation. Proc. Natl. Acad. Sci. USA. 94:1997;5314-5319.
25. Tam W.H.H., Andreasson K.A., Loh Y.P. The amino-terminal sequence of pro-opiomelanocortin directs intracellular targeting to the regulated secretory pathway. Eur. J. Cell Biol. 62:1993;294-306.
26. Thomas G., Thorne B.A., Thomas L., Allen R.G., Hruby D.E., Fuller R., Thorner J. Yeast KEX2 endopeptidase correctly cleaves a neuroendocrine prohormone in mammalian cells. Science. 241:1988;226-228.
27. Varlamov O., Fricker L.D. The C-terminal region of carboxypeptidase E involved in membrane binding is distinct from the region involved with intracellular routing. J. Biol. Chem. 271:1996;6077-6083.
28. Yoo S.H., Lewis M.S. Thermodynamic study of the pH-dependent interaction of chromogranin A with an intraluminal loop peptide of the inositol 1,4,5-trisphosphate receptor. Biochemistry. 34:1995;632-638.