脳科学辞典

「ネプリライシン」の版間の差分

ページ

ネプリライシン (ソースを閲覧)

2013年3月27日 (水) 09:06時点における版

9,675 バイト除去 、 2013年3月27日 (水)
細
編集の要約なし
細編集の要約なし
細編集の要約なし
19行目: 19行目:


'''1.ネプリライシンとは'''
'''1.ネプリライシンとは'''
ネプリライシンは活性部位が存在するカルボキシル末端側は管腔側/細胞外に配向するⅡ型の膜貫通型ペプチダーゼである。活性中心にZn結合モチ−フ(HEXXH配列)を有することから、メタロペプチダ−ゼに分類される[1][2]。別名として、エンケファリナーゼ、中性エンドペプチダーゼ24.11、CD10、membrane metallo-endopeptidase、common acute lymphoblastic leukemia antigen (CALLA)とも呼ばれている。プロテアーゼのM13ファミリーのMA(E)クランに分類される。脊椎動物に広く分類し、バクテリア由来のサーモライシンと高い相同性を示す[1][2]。
ネプリライシンは活性部位が存在するカルボキシル末端側は管腔側/細胞外に配向するⅡ型の膜貫通型ペプチダーゼである。活性中心にZn結合モチ−フ(HEXXH配列)を有することから、メタロペプチダ−ゼに分類される<ref><pubmed> 8475170 </pubmed></ref>[1][2]。別名として、エンケファリナーゼ、中性エンドペプチダーゼ24.11、CD10、membrane metallo-endopeptidase、common acute lymphoblastic leukemia antigen (CALLA)とも呼ばれている。プロテアーゼのM13ファミリーのMA(E)クランに分類される。脊椎動物に広く分類し、バクテリア由来のサーモライシンと高い相同性を示す[1][2]。


'''2.構造とサブファミリー'''
'''2.構造とサブファミリー'''
55行目: 55行目:
'''8. 参考文献'''
'''8. 参考文献'''
<references />
<references />
[1] Roques BP, Noble F, Daugé V, Fournié-Zaluski MC, Beaumont A: Neutral endopeptidase 24.11: structure, inhibition, and experimental and clinical pharmacology. Pharmacol Rev: 1993, 45(1);87-146 [PubMed:8475170]
[2] Turner AJ: Neprilysin, In Handbook of Proteolytic Enzyzmes, Second edition, Barrett AJ, Rawlings ND, Woessner JF, Eds. (Academic Press, London, 2004), vol. 1, chap.108.
[3] Iwata N, Higuchi M, Saido TC: Metabolism of amyloid-β peptide and Alzheimer's disease. Pharmacol Ther: 2005, 108(2);129-48 [PubMed:16112736]
[4] Saido TC, Iwata N: Metabolism of amyloid β peptide and pathogenesis of Alzheimer's disease-Towards presymptomatic diagnosis, prevention and therapy. Neurosci Res: 2006, 54(4);235-53 [PubMed:16457902]
[5] http://www.uniprot.org/uniprot/P08473
[6] D'Adamio L, Shipp MA, Masteller EL, Reinherz EL: Organization of the gene encoding common acute lymphoblastic leukemia antigen (neutral endopeptidase 24.11): multiple miniexons and separate 5’untranslated regions. Proc Natl Acad Sci USA: 1989, 86(18);7103–7 [PubMed:2528730]
[7] Li C, Booze RM, Hersh LB: Tissue-specific expression of rat neutral endopeptidase (neprilysin) mRNAs. J Biol Chem: 1995, 270(11);5723–8 [PubMed:7890699]
[8] Li C, Hersh LB: Characterization of the promoter region of the rat neprilysin gene. Arch Biochem Biophys: 1998, 358(1);189–95 [PubMed:9750180]
[9] http://www.uniprot.org/uniprot/Q495T
[10] Shirotani K, Tsubuki S, Iwata N, Takaki Y, Harigaya W, Maruyama K, Kiryu-Seo S, Kiyama H, Iwata H, Tomita T, Iwatsubo T, Saido TC: Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases. J Biol Chem: 2001, 276(24);21895-901 [PubMed:11278416]
[11] Fukami S, Watanabe K, Iwata N, Haraoka J, Lu B, Gerard NP, Gerard C, Fraser P, Westaway D, St George-Hyslop P, Saido TC: Aβ-degrading endopeptidase, neprilysin, in mouse brain: Synaptic and axonal localization inversely correlating with Aβ pathology. Neurosci Res: 2002, 43(1);39-56 [PubMed:12074840]
[12] Johnson GD, Stevenson T, Ahn K: Hydrolysis of peptide hormones by endothelin-converting enzyme-1. A comparison with neprilysin. J Biol Chem: 1999, 274;4053-58 [PubMed:9750180]
[13] Iwata N, Tsubuki S, Takaki Y, Watanabe K, Sekiguchi M, Hosoki E, Kawashima-Morishima M, Lee HJ, Hama E, Sekine-Aizawa Y, Saido TC: Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat Med: 2000, 6(2);143-50 [PubMed:10655101]
[14] Iwata N, Tsubuki S, Takaki Y, Shirotani K, Lu B, Gerard NP, Gerard C, Hama E, Lee HJ, Saido TC: Metabolic regulation of brain Aβ by neprilysin. Science: 2001, 292(5521);1550-2 [PubMed:11375493]
[15] Kanemitsu H, Tomiyama T, Mori H: Human neprilysin is capable of degrading amyloid β peptide not only in the monomeric form but also the pathological oligomeric form. Neurosci Lett: 2003, 350(2);113–6 [PubMed:12972166]
[16] Lu B, Gerard NP, Kolakowski LF Jr, Bozza M, Zurakowski D, Finco O, Carroll MC, Gerard C: Neutral endopeptidase modulation of septic shock. J Exp Med: 1995, 181(6);2271-5 [PubMed:7760013]
[17] Grasemann H, Lu B, Jiao A, Boudreau J, Gerard NP, De Sanctis GT: Targeted deletion of the neutral endopeptidase gene alters ventilatory responses to acute hypoxia in mice. J Appl Physiol: 1999, 87(4);1266-71 [PubMed:10517751]
[18] Lu B, Figini M, Emanueli C, Geppetti P, Grady EF, Gerard NP, Ansell J, Payan DG, Gerard C, Bunnett N: The control of microvascular permeability and blood pressure by neutral endopeptidase. Nat Med: 1997, 3(8);904-7 [PubMed: 9256283]
[19] Dempsey EC, Wick MJ, Karoor V, Barr EJ, Tallman DW, Wehling CA, Walchak SJ, Laudi S, Le M, Oka M, Majka S, Cool CD, Fagan KA, Klemm DJ, Hersh LB, Gerard NP, Gerard C, Miller YE: Neprilysin null mice develop exaggerated pulmonary vascular remodeling in response to chronic hypoxia. Am J Pathol: 2009, 174(3);782-96 [PubMed: 19234135][DOI:10.2353/ajpath.2009.080345.]
[20] Scholzen TE, Steinhoff M, Bonaccorsi P, Klein R, Amadesi S, Geppetti P, Lu B, Gerard NP, Olerud JE, Luger TA, Bunnett NW, Grady EF, Armstrong CA, Ansel JC: Neutral endopeptidase terminates substance P-induced inflammation in allergic contact dermatitis. J Immunol: 2001, 166(2);1285-91 [PubMed:11145711]
[21] Fischer HS, Zernig G, Hauser KF, Gerard C, Hersh LB, Saria A.: Neutral endopeptidase knockout induces hyperalgesia in a model of visceral pain, an effect related to bradykinin and nitric oxide. J Mol Neurosci: 2002, 18(1-2);129-34 [PubMed:11931342]
[22] Saria A, Hauser KF, Traurig HH, Turbek CS, Hersh L, Gerard C.: Opioid-related changes in nociceptive threshold and in tissue levels of enkephalins after target disruption of the gene for neutral endopeptidase (EC 3.4.24.11) in mice. Neurosci Lett: 1997, 234(1);27-30 [PubMed:9347938]
[23] Rose JB, Crews L, Rockenstein E, Adame A, Mante M, Hersh LB, Gage FH, Spencer B, Potkar R, Marr RA, Masliah E: Neuropeptide Y fragments derived from neprilysin processing are neuroprotective in a transgenic model of Alzheimer's disease. J Neurosci: 2009, 29(4);1115-25[PubMed:19176820][DOI:10.1523/JNEUROSCI.4220-08.2009]
[24] Iwata N, Takaki Y, Fukami S, Tsubuki S, Saido TC: Region-specific reduction of Aβ-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging. J Neurosci Res: 2002, 70(3):493-500 [PubMed:12391610]
[25] Hellström-Lindahl E, Ravid R, Nordberg A: Age-dependent decline of neprilysin in Alzheimer's disease and normal brain: inverse correlation with Aβ levels. Neurobiol Aging: 2008, 29(2);210-221 [PubMed:17098332]
[26] Russo R, Borghi R, Markesbery W, Tabaton M, Piccini A: Neprylisin decreases uniformly in Alzheimer's disease and in normal aging. FEBS Lett: 2005, 579(27);6027-6030 [PubMed: 16226260]
[27] Yasojima K, Akiyama H, McGeer EG, McGeer PL: Reduced neprilysin in high plaque areas of Alzheimer brain: a possible relationship to deficient degradation of β-amyloid peptide. Neurosci Lett: 2001, 297(2);97–100 [PubMed:11121879]
[28] Yasojima K, McGeer E, McGeer PL: Relationship between β amyloid peptide generating molecules and neprilysin in Alzheimer disease and normal brain. Brain Res: 2001, 919(1);115–21 [PubMed:11689168]
[29] Wang DS, Iwata N, Hama E, Saido TC, Dickson DW: Oxidized neprilysin in aging and Alzheimer’s disease brains. Biochem Biophys Res Commun: 2003, 310(1);236-241 [PubMed:14511676]
[30] Miners JS, Van Helmond Z, Chalmers K, Wilcock G, Love S, Kehoe PG: Decreased expression and activity of neprilysin in Alzheimer disease are associated with cerebral amyloid angiopathy. J Neuropathol Exp Neurol: 2006, 65(10);1012-21 [PubMed:17021406]
[31] 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 Neuropathol Exp Neurol: 2002, 61(10);849-56 [PubMed:12387451]
[32] Wang TL, Chang H, Hung CR, Tseng YZ: Attenuation of neutrophil and endothelial activation by intravenous morphine in patients with acute myocardial infarction. Am J Cardiol: 1997, 80(12);1532–5 [PubMed:9416930]
[33] Howell S, Caswell AM, Kenny AJ, Turner AJ: Membrane peptidases on human osteoblast-like cells in culture: hydrolysis of calcitonin and hormonal regulation of endopeptidase-24.11. Biochem J: 1993, 290(Pt 1);159–64 [PubMed:8439284]
[34] Bae SJ, Matsunaga Y, Takenaka M, Tanaka Y, Hamazaki Y, Shimizu K, Katayama I.: Substance P induced preprotachykinin A mRNA, neutral endopeptidase mRNA and substance P in cultured normal fibroblasts. Int Arch Allergy Immunol: 2002, 127(4);316–21 [PubMed:12021551]
[35] Joshi DD, Dang A, Yadav P, Qian J, Bandari PS, Chen K, Donnelly R, Castro T, Gascon P, Haider A, Rameshwar P: Negative feedback on the effect of stem cell factor on hematopoiesis is partly mediated through neutral endopeptidase activity on substance P: a combined functional and proteomic study. Blood: 2001, 98(9);2697–706 [PubMed:11675340]
[36] Saito T, Takaki Y, Iwata N, Trojanowski J, Saido TC: Alzheimer's disease, neuropeptides, neuropeptidase, and amyloid-β peptide metabolism. Sci Aging Knowl Environ: 2003, 2003(3);PE1 [PubMed:12844556]
[37] Saito T, Iwata N, Tsubuki S, Takaki Y, Takano J, Huang SM, Suemoto T, Higuchi M, Saido TC: Somatostatin regulates brain amyloid β peptide, Aβ42, via modulation of proteolytic degradation. Nature Med: 2005, 11(4);434-39 [PubMed:15778722]
[38] Davies P, Katzman R, Terry RD: Reduced somatostatin-like immunoreactivity in cerebral cortex from cases of Alzheimer diseas and Alzheimer senile dementa. Nature: 1980, 288(5788);279–80 [PubMed:6107862]
[39] Lu T, Pan Y, Kao SY, Li C, Kohane I, Chan J, Yankner BA: Gene regulation and DNA damage in the ageing human brain. Nature: 2004, 429(6994),883-91 [PubMed:15190254]
[40] Iwata N, Mizukami H, Shirotani K, Takaki Y, Muramatsu S, Lu B, Gerard NP, Gerard C, Ozawa K, Saido TC: Presynaptic localization of neprilysin contributes to efficient clearance of amyloid-β peptide in mouse brain. J Neurosci: 2004, 24(4);991–8 [PubMed:14749444]
[41] Nilsson P, Iwata N, Muramatsu S, Tjernberg LO, Winblad B, Saido TC. Gene therapy in Alzheimer's disease -Potential for disease modification. J Cell Mol Med: 2010, 14(4);741-57 [PubMed:20158567][DOI: 10.1111/j.1582-4934.2010.01038.x]
[42] Iwata N, Sekiguchi M, Hattori Y, Takahashi A, Asai M, Ji B, Higuchi M, Staufenbiel M, Muramatsu S, Saido TC. Global and effective gene delivery of neprilysin to the brain via intravascular administration of AAV vector in Alzheimer's disease mice. Sci Rep: 2013, 3 Article number 1472 [PubMed:23503602][DOI: 10.1038/srep01472.]


脚注1エンドトキシ（内毒素）：グラム陰性菌の外膜に存在する耐熱性の毒素．糖脂質と糖鎖からなるリポ多糖で,免疫系などに作用してマクロファージや好中球を活性化してサイトカインなどの炎症性因子の放出を促す．
脚注1エンドトキシ（内毒素）：グラム陰性菌の外膜に存在する耐熱性の毒素．糖脂質と糖鎖からなるリポ多糖で,免疫系などに作用してマクロファージや好中球を活性化してサイトカインなどの炎症性因子の放出を促す．
Nobuhisaiwata
19

回編集

「https://bsd.neuroinf.jp/wiki/特別:携帯機器差分/19184」から取得