The neuropeptide-degrading enzyme NL1 is expressed in specific neurons of mouse brain

Peptides

Volumn 24, Issue 7, 2003, Pages 1083-1091

  Carpentier, Mélanie ^a   Marcinkiewicz, Mieczyslaw ^b   Boileau, Guy ^a   DesGroseillers, Luc ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

^b CLIN RESEARCH INSTITUTE OF MONTREAL   (Canada)

Author keywords

Bradykinin; In situ hybridization; Neprilysin; Pituitary gland; Substance P

Indexed keywords

GLYCOPROTEIN; GLYCOPROTEIN NL 1; MESSENGER RNA; NEUROPEPTIDE; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; BRAIN FUNCTION; BRAIN NERVE CELL; BRAIN REGION; CELL LEVEL; CELL SUBPOPULATION; CELLULAR DISTRIBUTION; CENTRAL NERVOUS SYSTEM; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME DEGRADATION; ENZYME SUBSTRATE; GENE EXPRESSION; GENE IDENTIFICATION; GENE LOCATION; GENE MAPPING; GRAY MATTER; HYPOPHYSIS; IN SITU HYBRIDIZATION; MOUSE; NERVOUS TISSUE; NONHUMAN; PERINATAL PERIOD; PRIORITY JOURNAL; PROTEIN EXPRESSION; RNA ANALYSIS; SPINAL CORD;

ANIMALIA;

EID: 0141629602     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0196-9781(03)00177-3     Document Type: Article

References (25)

1. Carpentier M., Robitaille Y., DesGroseillers L., Boileau G., Marcinkiewicz M. Declining expression of Neprilysin in Alzheimer disease vasculature: possible involvement in cerebral amyloid angiopathy. J. Neurochem. Exp. Neurol. 61:2002;849-856.
2. Carson J., Turner A.J. Beta-amyloid catabolism: roles for Neprilysin (NEP) and other metallopeptidases? J. Neurochem. 81:2002;1-8.
3. Crine P, Dion N, Boileau G. Endopeptidase 24.11. In: Kenny AJ, Boustead CM, editors. Cell-surface peptidases in health and disease. Oxford, UK: BIOS Scientific Publishers Ltd.; 1997. p. 79-98.
4. Drezner M.K. PHEX gene and hypophosphatemia. Kidney Int. 57:2000;9-18.
5. Fisher H.S., Zernig G., Hauser K.F., Hersh L.B., Saria A. Neutral endopeptidase knock out induces hyperalgesia in a model of visceral pain, an effect related to Bradykinin and nitric oxide. J. Mol. Neurosci. 18:2002;129-134.
6. Gaudoux F., Boileau G., Crine P. Localization of Neprilysin (E.C. 3.4.24.11) mRNA in rat brain by in situ hybridization. J. Neurosci. Res. 34:1993;426-433.
7. Ghaddar G., Frota-Rochon A., Carpentier M., Marcinkiewicz M., Seidah N., Crine P.et al. Molecular cloning and biochemical characterization of a new mouse testis soluble-zinc-metallopeptidase of the neprilysin family. Biochem. J. 347:2000;419-429.
8. Ikeda K., Emonto N., Raharjo S.B., Nurhantari Y., Saiki K., Yokoyama M. et al. Molecular identification and characterization of a novel membrane-bound metalloprotease, the soluble secreted form of which hydrolyzes a variety of vasoactive peptides. J. Biol. Chem. 274:1999;32469-32477.
9. Iwata N., Tsubuki S., Takaki Y., Watanabe K., Sekiguchi M., Hosoki E.et al. Identification of the major Abeta1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat. Med. 6:2000;143-150.
10. Kiryu-Seo S., Sasaki M., Yokohama H., Nakagomi S., Hirayama T., Aoki S. et al. Damage-induced neuronal endopeptidase (DINE) is a unique metallopeptidase expressed in response to neural damage and activates superoxide scavengers. Proc. Natl. Acad. Sci. U.S.A. 97:2000;4345-4350.
11. Marsh W.L. Molecular biology of blood groups: cloning the Kell gene. Transfusion. 32:1992;98-101.
12. Ouimet T., Facchinetti P., Rose C., Bonhomme M.-C., Gros C., Schwartz J.-C. Neprilysin II: a putative novel metalloprotease and its isoforms in CNS and testis. Biochem. Biophys. Res. Commun. 271:2000;565-570.
13. Renolleau S., Dauger S., Vardon G., Levacher B., Simonneau M., Yanagisawa M.et al. Impaired ventilatory response to hypoxia in mice deficient in Endothelin-Converting-Enzyme-1. Pediat. Res. 49:2001;705-712.
14. Roques B.P., Fournié-Zaluski M.C., Soroca E., Lecomte J.M., Malfroy B., Llorens C.et al. The enkephlinase inhibitor thiorphan shows antinociceptive activity in mice. Nature. 288:1980;286-288.
15. Roques B.P., Noble F., Dauge V., Fournie-Zaluski M.C., Beaumont A. Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology. Pharmacol. Rev. 45:1993;87-146.
16. Rose C., Voisin S., Gros C., Schwartz J.-C., Ouimet T. Cell-specific activity of neprilysin 2 isoforms and enzymatic specificity compared with neprilysin. Biochem. J. 363:2002;697-705.
17. Ruchon A.F., Marcinkiewicz M., Siegfried G., Tenenhouse H.S., DesGroseillers L., Crine P.et al. Pex mRNA is localized in developing mouse osteoblasts and odontoblasts. J. Histochem. Cytochem. 46:1998;459-468.
18. Schweizer A., Valdenaire O., Koster A., Lang Y., Schmitt G., Lenz B.et al. Neonatal lethality in mice deficient in XCE, a novel member of the endothelin-converting enzyme and neutral endopeptidase family. J. Biol. Chem. 274:1999;20450-20456.
19. Sencer-Dene B., Thorogood P., Nair S., Kenny A.J., Harris M. Distribution of, and a putative role for, the cell-surface metallo-endopeptidases during mammalian craniofacial development. Development. 120:1994;3213-3226.
20. Tennenhouse H.S. X-linked hypophosphatemia: a homologous disorder in humans and mice. Nephrol. Dial. Transplant. 14:1999;333-341.
21. Turner AJ. Endothelin-converting enzymes. In: Kenny AJ, Boustead CM, editors. Cell-surface peptidases in health and disease. Oxford, UK: BIOS Scientific Publishers Ltd.; 1997. p. 137-53.
22. Turner A.J., Brown C.D., Carson J.A., Barnes K. The neprilysin family in health and disease. Adv. Exp. Med. Biol. 477:2000;229-240.
23. Valdenaire O., Richards J.G., Faull R.M., Schweizer A. XCE, a new member of the endothelin-converting enzyme and neutral endopeptidase family, is preferentially expressed in the CNS. Mol. Brain Res. 64:1999;211-221.
24. Valdenaire O., Schweiser A. Endothelin-converting enzyme-like 1 (ECEL1; XCE): a putative metallopeptidase crucially involved in the nervous control of respiration. Biochem. Soc. Trans. 28:2000;430-460.
25. Yanagisawa H., Hammer R.E., Richardson J.A., Emoto N., Williams C., Takeda S.et al. Disruption of ECE-1 and ECE-2 reveals a role for endothelin converting enzyme-2 in murine cardiac development. J. Clin. Invest. 105:2000;1372-1382.