Peptide Degradation (Neprilysin and Other Regulatory Peptidases)

Handbook of Biologically Active Peptides

Volumn , Issue , 2013, Pages 1757-1764

  Turner, Anthony J ^a   Nalivaeva, Natalia N ^b  

^a UNIVERSITY OF LEEDS   (United Kingdom)

^b SECHENOV INSTITUTE OF EVOLUTIONARY PHYSIOLOGY AND BIOCHEMISTRY   (Russian Federation)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84884938005     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-385095-9.00241-4     Document Type: Chapter

References (35)

1. Anthony C.S., Corradi H.R., Schwager S.L., Redelinghuys P., Georgiadis D., Dive V., et al. The N domain of human angiotensin-I-converting enzyme: the role of N-glycosylation and the crystal structure in complex with an N domain-specific phosphinic inhibitor, RXP407. J Biol Chem 2010, 285:35685-35693.
2. Belyaev N.D., Kellett K.A., Beckett C., Makova N.Z., et al. The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a β-secretase-dependent pathway. J Biol Chem 2010, 285:41443-41454.
3. Belyaev N.D., Nalivaeva N.N., Makova N.Z., Turner A.J. Neprilysin gene expression requires binding of the amyloid precursor protein intracellular domain to its promoter: implications for Alzheimer disease. EMBO Rep 2009, 10:94-100.
4. Bland N.D., Pinney J.W., Thomas J.E., Turner A.J., et al. Bioinformatic analysis of the neprilysin (M13) family of peptidases reveals complex evolutionary and functional relationships. BMC Evol Biol 2008, 8:16.
5. Ciaccio C., Tundo G.R., Grasso G., Spoto G., et al. Somatostatin: a novel substrate and a modulator of insulin-degrading enzyme activity. J Mol Biol 2009, 385:1556-1567.
6. Demuth H.-U., McIntosh C.H., Pederson R.A., et al. Type 2 diabetes-therapy with dipeptidyl peptidase IV inhibitors. Biochim Biophys Acta 2005, 1751:33-44.
7. Eckman E.A., Watson M., Marlow L., Sambamurti K., et al. Alzheimer's disease β-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. J Biol Chem 2003, 278:2081-2084.
8. Garcia-Horsman J.A., Männistö P.T., Venäläinen J.I. On the role of prolyl oligopeptidase in health and disease. Neuropeptides 2007, 41:1-24.
9. Hafez D., Huang J.Y., Huynh A.M., Valtierra S., et al. Neprilysin-2 is an important β-amyloid degrading enzyme. Am J Pathol 2011, 178:306-312.
10. Hu J., Igarashi A., Kamata M., Nakagawa H. Angiotensin-converting enzyme degrades Alzheimer amyloid β-peptide (Aβ); retards Aβ aggregation, deposition, fibril formation; and inhibits cytotoxicity. J Biol Chem 2001, 276:47863-47868.
11. Ikeda K., Emoto N., Raharjo S.B., Nurhantari Y., et al. Molecular identification and characterisation of a novel membrane-bound metalloprotease, the soluble form of which hydrolyzes a variety of vasoactive peptides. J Biol Chem 1999, 274:32469-32477.
12. Iwata N., Tsubuki S., Takaki Y., Watanabe K., et al. Identification of the major Aβ1-42 degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition. Nature Med 2000, 6:143-150.
13. Lambert D.W., Clarke N.E., Turner A.J. Not just angiotensinases: new roles for the angiotensin-converting enzymes. Cell Mol Life Sci 2010, 67:89-98.
14. Lambert L.A., Whyteside A.R., Turner A.J., Usmani B.A. Isoforms of endothelin-converting enzyme-1 (ECE-1) have opposing effects on prostate cancer cell invasion. Br J Cancer 2008, 99:1114-1120.
15. Leissring M.A., Malito E., Hedouin S., Reinstatler L., et al. Designed inhibitors of insulin-degrading enzyme regulate the catabolism and activity of insulin. PLoS One 2010, 5. e10504.
16. Marr R.A., Rockenstein E., Mukherjee A., Kindy M.S., et al. Neprilysin gene transfer reduces human amyloid pathology in transgenic mice. J Neurosci 2003, 23:1992-1996.
17. Miller L., Hou X., Gagnidze K., Sweedler J.V., et al. Mice deficient in endothelin-converting enzyme-2 exhibit abnormal responses to morphine and altered peptide levels in the spinal cord. J Neurochem 2011, 119:1074-19985.
18. Nalivaeva N.N., Fisk L.R., Belyaev N.D., Turner A.J. Amyloid-degrading enzymes as therapeutic targets in Alzheimer's disease. Curr Alzheimer Res 2008, 5:212-224.
19. Natesh R., Schwager S.L., Sturrock E.D., Acharya K.R. Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 2003, 421:551-554.
20. Oefner C., D'Arcy A., Hennig M., Winkler F.K., et al. Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon. J Mol Biol 2000, 296:341-349.
21. Pardossi-Piquard R., Petit A., Kawarai T., Sunyach C., et al. Presenilin-dependent transcriptional control of the Aβ-degrading enzyme neprilysin by intracellular domains of βAPP and APLP. Neuron 2005, 46:541-554.
22. Petit A., Barelli H., Morain P., Checler F. Novel proline endopeptidase inhibitors do not modify Aβ40/42 formation and degradation by human cells expressing wild-type and Swedish mutated β-amyloid precursor protein. Br J Pharmacol 2000, 130:1613-1617.
23. Rasmussen H.B., Branner S., Wiberg F.C., Wagtmann N. Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog. Nat Struct Biol 2003, 10:19-25.
24. Rawlings N.D., Barrett A.J., Bateman A. Asparagine peptide lyases: a seventh catalytic type of proteolytic enzymes. J Biol Chem 2011, 286:38321-38328.
25. Roosterman D., Cottrell G.S., Padilla B.E., Muller L., et al. Endothelin-converting enzyme 1 degrades neuropeptides in endosomes to control receptor recycling. Proc Natl Acad Sci U S A 2007, 104:11838-11843.
26. Rougeot C., Messaoudi M., Hermitte V., Rigault A.G., et al. Sialorphin, a natural inhibitor of rat membrane-bound neutral endopeptidase that displays analgesic activity. Proc Natl Acad Sci U S A 2003, 100:8549-8554.
27. Shen Y., Joachimiak A., Rosner M.R., Tang W.J. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature 2006, 443:870-874.
28. Standeven K.F., Hess K., Carter A.M., Rice G.I., et al. Neprilysin, obesity and the metabolic syndrome. Int J Obes (Lond) 2011, 8:1031-1040.
29. Tipnis S.R., Hooper N.M., Hyde R., Karran E., et al. A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase. J Biol Chem 2000, 275:33238-33243.
30. Turner A.J., Murphy L.J. Molecular pharmacology of endothelin converting enzymes. Biochem Pharmacol 1996, 51:91-102.
31. Vanhoof G., Goossens F., De Meester I., Hendriks D., et al. Proline motifs in peptides and their biological processing. FASEB J 1995, 9:736-744.
32. Vickers C., Hales P., Kaushik V., Dick L., et al. Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase. J Biol Chem 2002, 277:14838-14843.
33. Whyteside A.R., Turner A.J. Human neprilysin-2 (NEP2) and NEP display distinct subcellular localisations and substrate preferences. FEBS Lett 2008, 582:2382-2386.
34. Zhao J., Li L., Leissring M.A. Insulin-degrading enzyme is exported via an unconventional protein secretion pathway. Mol Neurodegener 2009, 4:4.
35. Zou K., Yamaguchi H., Akatsu H., Sakamoto T., et al. Angiotensin-converting enzyme converts amyloid β-protein 1-42 (Aβ1-42) to (Aβ1-40), and its inhibition enhances brain Aβ deposition. J Neurosci 2007, 27:8628-8635.