Nardilysin

Handbook of Proteolytic Enzymes

Volumn 1, Issue , 2013, Pages 1421-1426

  Nishi, Eiichiro ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84880825544     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-382219-2.00320-3     Document Type: Chapter

References (31)

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2. Gluschankof P., Gomez S., Morel A., Cohen P. Enzymes that process somatostatin precursors. A novel endoprotease that cleaves before the arginine-lysine doublet is involved in somatostatin-28 convertase activity of rat brain cortex. J. Biol. Chem. 1987, 262(20):9615-9620.
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5. Csuhai E., Safavi A., Hersh L.B. Purification and characterization of a secreted arginine-specific dibasic cleaving enzyme from EL-4 cells. Biochemistry 1995, 34(38):12411-12419.
6. Nishi E., Prat A., Hospital V., Elenius K., Klagsbrun M. N-arginine dibasic convertase is a specific receptor for heparin-binding EGF-like growth factor that mediates cell migration. EMBO J. 2001, 20(13):3342-3350.
7. Hospital V., Chesneau V., Balogh A., Joulie C., Seidah N.G., Cohen P., Prat A. N-arginine dibasic convertase (nardilysin) isoforms are soluble dibasic-specific metalloendopeptidases that localize in the cytoplasm and at the cell surface. Biochem. J. 2000, 349(Pt. 2):587-597.
8. Csuhai E., Chen G., Hersh L.B. Regulation of N-arginine dibasic convertase activity by amines: putative role of a novel acidic domain as an amine binding site. Biochemistry 1998, 37(11):3787-3794.
9. Csuhai E., Juliano M.A., Juliano L., Hersh L.B. Kinetic analysis of spermine binding to NRD convertase. Arch. Biochem. Biophys. 1999, 362(2):291-300.
10. Chow K.M., Csuhai E., Juliano M.A., St Pyrek J., Juliano L., Hersh L.B. Studies on the subsite specificity of rat nardilysin (N-arginine dibasic convertase). J. Biol. Chem. 2000, 275(26):19545-19551.
11. Chow K.M., Oakley O., Goodman J., Ma Z., Juliano M.A., Juliano L., Hersh L.B. Nardilysin cleaves peptides at monobasic sites. Biochemistry 2003, 42(7):2239-2244.
12. Fontes G., Lajoix A.D., Bergeron F., Cadel S., Prat A., Foulon T., Gross R., Dalle S., Le-Nguyen D., Tribillac F., Bataille D. Miniglucagon (MG)-generating endopeptidase, which processes glucagon into MG, is composed of N-arginine dibasic convertase and aminopeptidase B. Endocrinology 2005, 146(2):702-712.
13. Kessler J.H., Khan S., Seifert U., Le Gall S., Chow K.M., Paschen A., Bres-Vloemans S.A., de Ru A., van Montfoort N., Franken K.L., Benckhuijsen W.E., Brooks J.M., van Hall T., Ray K., Mulder A., Doxiadis II, van Swieten P.F., Overkleeft H.S., Prat A., Tomkinson B., Neefjes J., Kloetzel P.M., Rodgers D.W., Hersh L.B., Drijfhout J.W., van Veelen P.A., Ossendorp F., Melief C.J. Antigen processing by nardilysin and thimet oligopeptidase generates cytotoxic T cell epitopes. Nat. Immunol. 2011, 12(1):45-53.
14. Hospital V., Nishi E., Klagsbrun M., Cohen P., Seidah N.G., Prat A. The metalloendopeptidase nardilysin (NRDc) is potently inhibited by heparin-binding epidermal growth factor-like growth factor (HB-EGF). Biochem. J. 2002, 367(Pt. 1):229-238.
15. 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(7113):870-874.
16. Ma Z., Csuhai E., Chow K.M., Hersh L.B. Expression of the acidic stretch of nardilysin as a functional binding domain. Biochemistry 2001, 40(31):9447-9452.
17. Nishi E., Hiraoka Y., Yoshida K., Okawa K., Kita T. Nardilysin enhances ectodomain shedding of heparin-binding epidermal growth factor-like growth factor through activation of tumor necrosis factor-alpha-converting enzyme. J. Biol. Chem. 2006, 281(41):31164-31172.
18. Winter A.G., Pierotti A.R. Gene expression of the dibasic-pair cleaving enzyme NRD convertase (N-arginine dibasic convertase) is differentially regulated in the GH3 pituitary and Mat-Lu prostate cell lines. Biochem. J. 2000, 351(Pt. 3):755-764.
19. Chesneau V., Prat A., Segretain D., Hospital V., Dupaix A., Foulon T., Jegou B., Cohen P. NRD convertase: a putative processing endoprotease associated with the axoneme and the manchette in late spermatids. J. Cell Sci. 1996, 109(Pt. 11):2737-2745.
20. Ma Z., Chow K.M., Yao J., Hersh L.B. Nuclear shuttling of the peptidase nardilysin. Arch. Biochem. Biophys. 2004, 422(2):153-160.
21. Ma Z., Wang X., Hockman S., Snow E.C., Hersh L.B. Subcellular localization of nardilysin during mouse oocyte maturation. Arch. Biochem. Biophys. 2005, 434(1):187-194.
22. Hospital V., Prat A., Joulie C., Cherif D., Day R., Cohen P. Human and rat testis express two mRNA species encoding variants of NRD convertase, a metalloendopeptidase of the insulinase family. Biochem. J. 1997, 327(Pt. 3):773-779.
23. Fumagalli P., Accarino M., Egeo A., Scartezzini P., Rappazzo G., Pizzuti A., Avvantaggiato V., Simeone A., Arrigo G., Zuffardi O., Ottolenghi S., Taramelli R. Human NRD convertase: a highly conserved metalloendopeptidase expressed at specific sites during development and in adult tissues. Genomics 1998, 47(2):238-245.
24. Ohno M., Hiraoka Y., Matsuoka T., Tomimoto H., Takao K., Miyakawa T., Oshima N., Kiyonari H., Kimura T., Kita T., Nishi E. Nardilysin regulates axonal maturation and myelination in the central and peripheral nervous system. Nat. Neurosci. 2009, 12(12):1506-1513.
25. Bernstein H.G., Stricker R., Dobrowolny H., Trubner K., Bogerts B., Reiser G. Histochemical evidence for wide expression of the metalloendopeptidase nardilysin in human brain neurons. Neuroscience 2007, 146(4):1513-1523.
26. Hiraoka Y., Ohno M., Yoshida K., Okawa K., Tomimoto H., Kita T., Nishi E. Enhancement of alpha-secretase cleavage of amyloid precursor protein by a metalloendopeptidase nardilysin. J. Neurochem. 2007, 102(5):1595-1605.
27. Hiraoka Y., Yoshida K., Ohno M., Matsuoka T., Kita T., Nishi E. Ectodomain shedding of TNF-alpha is enhanced by nardilysin via activation of ADAM proteases. Biochem. Biophys. Res. Commun. 2008, 370(1):154-158.
28. Bernstein, H.G., Stricker, R., Lendeckel, U., Bertram, I., Dobrowolny, H., Steiner, J., Bogerts, B., Reiser, G. Reduced neuronal co-localisation of nardilysin and the putative alpha-secretases ADAM10 and ADAM17 in Alzheimer's disease and Down syndrome brains. Age (Dordr.) 31(1), 11-25.
29. Chow K.M., Ma Z., Cai J., Pierce W.M., Hersh L.B. Nardilysin facilitates complex formation between mitochondrial malate dehydrogenase and citrate synthase. Biochim. Biophys. Acta 2005, 1723(1-3):292-301.
30. Stricker R., Chow K.M., Walther D., Hanck T., Hersh L.B., Reiser G. Interaction of the brain-specific protein p42IP4/centaurin-alpha1 with the peptidase nardilysin is regulated by the cognate ligands of p42IP4, PtdIns(3,4,5)P3 and Ins(1,3,4,5)P4, with stereospecificity. J. Neurochem. 2006, 98(2):343-354.
31. Korovkina V.P., Stamnes S.J., Brainard A.M., England S.K. Nardilysin convertase regulates the function of the maxi-K channel isoform mK44 in human myometrium. Am. J. Physiol. Cell Physiol. 2009, 296(3):C433-440.