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Volumn 95, Issue 4, 2005, Pages 1156-1166

Altered expression of neprilysin family members in the pituitary gland of sleep-disturbed rats, an animal model of severe fatigue

Author keywords

Damage induced neuronal endopeptidase; ECEL1; Endothelin converting enzyme 1; Fatigue; Galanin; Metallopeptidase

Indexed keywords

MEMBRANE METALLOENDOPEPTIDASE; MESSENGER RNA;

EID: 28244454638     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2005.03436.x     Document Type: Article
Times cited : (35)

References (46)
  • 1
    • 0027998531 scopus 로고
    • Hydrolysis of iodine labelled urodilatin and ANP by recombinant neutral endopeptidase EC 3.4.24.11
    • Abassi Z. A., Golomb E., Agbaria R., Roller P. P., Tate J. and Keiser H. R. (1994) Hydrolysis of iodine labelled urodilatin and ANP by recombinant neutral endopeptidase EC 3.4.24.11. Br. J. Pharmacol. 113, 204-208.
    • (1994) Br. J. Pharmacol. , vol.113 , pp. 204-208
    • Abassi, Z.A.1    Golomb, E.2    Agbaria, R.3    Roller, P.P.4    Tate, J.5    Keiser, H.R.6
  • 2
    • 0033828365 scopus 로고    scopus 로고
    • Neprilysin, a novel target for ultraviolet B regulation of melanogenesis via melanocortins
    • Aberdam E., Auberger P., Ortonne J. P. and Ballotti R. (2000) Neprilysin, a novel target for ultraviolet B regulation of melanogenesis via melanocortins. J. Invest. Dermatol. 115, 381-387.
    • (2000) J. Invest. Dermatol. , vol.115 , pp. 381-387
    • Aberdam, E.1    Auberger, P.2    Ortonne, J.P.3    Ballotti, R.4
  • 3
    • 0028952265 scopus 로고
    • Endopeptidase-24.11 is the integral membrane peptidase initiating degradation of somatostatin in the hippocampus
    • Bames K., Doherty S. and Turner A. J. (1995) Endopeptidase-24.11 is the integral membrane peptidase initiating degradation of somatostatin in the hippocampus. J. Neurochem. 64, 1826-1832.
    • (1995) J. Neurochem. , vol.64 , pp. 1826-1832
    • Bames, K.1    Doherty, S.2    Turner, A.J.3
  • 5
    • 0027933561 scopus 로고
    • Increase of prolactin mRNA in the rat hypothalamus after intracerebroventricular injection of VIP or PACAP
    • Bredow S., Kacsoh B., Obal F. Jr, Fang J. and Krueger J. M. (1994) Increase of prolactin mRNA in the rat hypothalamus after intracerebroventricular injection of VIP or PACAP. Brain Res. 660, 301-308.
    • (1994) Brain Res. , vol.660 , pp. 301-308
    • Bredow, S.1    Kacsoh, B.2    Obal Jr., F.3    Fang, J.4    Krueger, J.M.5
  • 6
    • 0037396496 scopus 로고    scopus 로고
    • The neuroendocrinology of chronic fatigue syndrome
    • Cleare A. J. (2003) The neuroendocrinology of chronic fatigue syndrome. Endocr. Rev. 24, 236-252.
    • (2003) Endocr. Rev. , vol.24 , pp. 236-252
    • Cleare, A.J.1
  • 7
    • 0025606527 scopus 로고
    • Degradation of α-melanocyte stimulating hormone (α-MSH) by CALLA/endopeptidase 24.11 expressed by human melanoma cells in culture
    • Deschodt-Lanckman M., Vanneste Y., Loir B., Michel A., Libert A., Ghanem G. and Lejeune F. (1990) Degradation of α-melanocyte stimulating hormone (α-MSH) by CALLA/endopeptidase 24.11 expressed by human melanoma cells in culture. Int. J. Cancer 46, 1124-1130.
    • (1990) Int. J. Cancer , vol.46 , pp. 1124-1130
    • Deschodt-Lanckman, M.1    Vanneste, Y.2    Loir, B.3    Michel, A.4    Libert, A.5    Ghanem, G.6    Lejeune, F.7
  • 8
    • 0036298089 scopus 로고    scopus 로고
    • Hypothalamic thyrotropin-releasing hormone mRNA responses to hypothyroxinemia induced by sleep deprivation
    • Everson C. A. and Nowak T. S. Jr (2002) Hypothalamic thyrotropin- releasing hormone mRNA responses to hypothyroxinemia induced by sleep deprivation. Am. J. Physiol. Endocrinol. Metab. 283, E85-E93.
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.283
    • Everson, C.A.1    Nowak Jr., T.S.2
  • 9
    • 0037466757 scopus 로고    scopus 로고
    • Ontogeny, regional and cellular distribution of the novel metalloprotease neprilysin 2 in the rat: A comparison with neprilysin and endothelin-converting enzyme-1
    • Facchinetti P., Rose C., Schwartz J. C. and Ouimet T. (2003) Ontogeny, regional and cellular distribution of the novel metalloprotease neprilysin 2 in the rat: a comparison with neprilysin and endothelin-converting enzyme-1. Neuroscience 118, 627-639.
    • (2003) Neuroscience , vol.118 , pp. 627-639
    • Facchinetti, P.1    Rose, C.2    Schwartz, J.C.3    Ouimet, T.4
  • 10
    • 0027973857 scopus 로고
    • The chronic fatigue syndrome: A comprehensive approach to its definition and study
    • International Chronic Fatigue Syndrome Study Group
    • Fukuda K., Straus S. E., Hickie I., Sharpe M. C., Dobbins J. G. and Komaroff A. (1994) The chronic fatigue syndrome: a comprehensive approach to its definition and study. International Chronic Fatigue Syndrome Study Group. Ann. Intern. Med. 121, 953-959.
    • (1994) Ann. Intern. Med. , vol.121 , pp. 953-959
    • Fukuda, K.1    Straus, S.E.2    Hickie, I.3    Sharpe, M.C.4    Dobbins, J.G.5    Komaroff, A.6
  • 11
    • 18344362983 scopus 로고    scopus 로고
    • Neuropeptide Y inhibits spontaneous α-melanocyte-stimulating hormone (α-MSH) release via a Y(5) receptor and suppresses thyrotropin-releasing hormone-induced α-MSH secretion via a Y(1) receptor in frog melanotrope cells
    • Galas L., Tonon M. C., Beaujean D. et al. (2002) Neuropeptide Y inhibits spontaneous α-melanocyte-stimulating hormone (α-MSH) release via a Y(5) receptor and suppresses thyrotropin-releasing hormone-induced α-MSH secretion via a Y(1) receptor in frog melanotrope cells. Endocrinology 143, 1686-1694.
    • (2002) Endocrinology , vol.143 , pp. 1686-1694
    • Galas, L.1    Tonon, M.C.2    Beaujean, D.3
  • 12
    • 0021853198 scopus 로고
    • An immunoradiometric assay for endopeptidase-24.11 shows it to be a widely distributed enzyme in pig tissues
    • Gee N. S., Bowes M. A., Buck P. and Kenny A. J. (1985) An immunoradiometric assay for endopeptidase-24.11 shows it to be a widely distributed enzyme in pig tissues. Biochem. J. 228, 119-126.
    • (1985) Biochem. J. , vol.228 , pp. 119-126
    • Gee, N.S.1    Bowes, M.A.2    Buck, P.3    Kenny, A.J.4
  • 13
    • 0030884084 scopus 로고    scopus 로고
    • Vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating peptide (PACAP-27, but not PACAP-38) degradation by the neutral endopeptidase EC 3.4.24.11
    • Gourlet P., Vandermeers A., Robberecht P. and Deschodt-Lanckman M. (1997). Vasoactive intestinal peptide (VIP) and pituitary adenylate cyclase-activating peptide (PACAP-27, but not PACAP-38) degradation by the neutral endopeptidase EC 3.4.24.11. Biochem. Pharmacol. 54, 509-515.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 509-515
    • Gourlet, P.1    Vandermeers, A.2    Robberecht, P.3    Deschodt-Lanckman, M.4
  • 14
    • 0032722991 scopus 로고    scopus 로고
    • Transforming growth factor-β activated during exercise in brain depresses spontaneous motor activity of animals: Relevance to central fatigue
    • Inoue K., Yamazaki H., Manabe Y., Fukuda C., Hanai K. and Fushiki T. (1999) Transforming growth factor-β activated during exercise in brain depresses spontaneous motor activity of animals: relevance to central fatigue. Brain Res. 846, 145-153.
    • (1999) Brain Res. , vol.846 , pp. 145-153
    • Inoue, K.1    Yamazaki, H.2    Manabe, Y.3    Fukuda, C.4    Hanai, K.5    Fushiki, T.6
  • 15
    • 0033621739 scopus 로고    scopus 로고
    • Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
    • Iwata N., Tsubuki S., Takaki Y et al. (2000) Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat. Med. 6, 143-150.
    • (2000) Nat. Med. , vol.6 , pp. 143-150
    • Iwata, N.1    Tsubuki, S.2    Takaki, Y.3
  • 16
    • 0035947207 scopus 로고    scopus 로고
    • Metabolic regulation of brain A by neprilysin
    • Iwata N., Tsubuki S., Takaki Y et al. (2001) Metabolic regulation of brain A by neprilysin. Science 292, 1550-1552.
    • (2001) Science , vol.292 , pp. 1550-1552
    • Iwata, N.1    Tsubuki, S.2    Takaki, Y.3
  • 17
    • 0037010286 scopus 로고    scopus 로고
    • Region-specific reduction of Aβeta-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging
    • Iwata N., Takaki Y., Fukami S., Tsubuki S. and Saido T. C. (2002) Region-specific reduction of Aβeta-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging. J. Neurosci. Res. 70, 493-500.
    • (2002) J. Neurosci. Res. , vol.70 , pp. 493-500
    • Iwata, N.1    Takaki, Y.2    Fukami, S.3    Tsubuki, S.4    Saido, T.C.5
  • 18
    • 0036849640 scopus 로고    scopus 로고
    • Damage-induced neuronal endopeptidase (DINE/ECEL) expression is regulated by leukemia inhibitory factor and deprivation of nerve growth factor in rat sensory ganglia after nerve injury
    • Kato R., Kiryu-Seo S. and Kiyama H. (2002) Damage-induced neuronal endopeptidase (DINE/ECEL) expression is regulated by leukemia inhibitory factor and deprivation of nerve growth factor in rat sensory ganglia after nerve injury. J. Neurosci. 22, 9410-9418.
    • (2002) J. Neurosci. , vol.22 , pp. 9410-9418
    • Kato, R.1    Kiryu-Seo, S.2    Kiyama, H.3
  • 19
    • 13344275855 scopus 로고
    • Nerve injury enhances rat neuronal glutamate transporter expression: Identification by differential display PCR
    • Kiryu S., Yao G. L., Monta N., Kato H. and Kiyama H. (1995) Nerve injury enhances rat neuronal glutamate transporter expression: identification by differential display PCR. J. Neurosci. 15, 7872-7878.
    • (1995) J. Neurosci. , vol.15 , pp. 7872-7878
    • Kiryu, S.1    Yao, G.L.2    Monta, N.3    Kato, H.4    Kiyama, H.5
  • 20
    • 4444311284 scopus 로고    scopus 로고
    • DINE (damage-induced neuronal endopeptidase)
    • Kiryu-Seo S. and Kiyama H. (2004) DINE (damage-induced neuronal endopeptidase). Protein Pept. Lett. 11, 451-460.
    • (2004) Protein Pept. Lett. , vol.11 , pp. 451-460
    • Kiryu-Seo, S.1    Kiyama, H.2
  • 21
    • 0034636109 scopus 로고    scopus 로고
    • Damage-induced neuronal endopeptidase (DINE) is a unique metallopeptidase expressed in response to neuronal damage and activates superoxide scavengers
    • Kiryu-Seo S., Sasaki M., Yokohama H., Nakagomi S., Hirayama T., Aoki S., Wada K. and Kiyama H. (2000) Damage-induced neuronal endopeptidase (DINE) is a unique metallopeptidase expressed in response to neuronal damage and activates superoxide scavengers. Proc. Natl Acad. Sci. USA 97, 4345-4350.
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4345-4350
    • Kiryu-Seo, S.1    Sasaki, M.2    Yokohama, H.3    Nakagomi, S.4    Hirayama, T.5    Aoki, S.6    Wada, K.7    Kiyama, H.8
  • 22
    • 0036429750 scopus 로고    scopus 로고
    • Brain regions involved in fatigue sensation: Reduced acetylcamitine uptake into the brain
    • Kuratsune H., Yamaguti K., Lindh G. et al. (2002) Brain regions involved in fatigue sensation: reduced acetylcamitine uptake into the brain. Neuroimage 17, 1256-1265.
    • (2002) Neuroimage , vol.17 , pp. 1256-1265
    • Kuratsune, H.1    Yamaguti, K.2    Lindh, G.3
  • 23
    • 4444253053 scopus 로고    scopus 로고
    • The zinc metallopeptidase family: New faces, new functions
    • Lew R. A. (2004) The zinc metallopeptidase family: new faces, new functions. Protein Pept. Lett. 11, 407-414.
    • (2004) Protein Pept. Lett. , vol.11 , pp. 407-414
    • Lew, R.A.1
  • 24
    • 0026776797 scopus 로고
    • Identification and characterization of neutral endopeptidase in endothelial cells from venous or arterial origins
    • Llorens-Cortes C., Huang H., Vicart P., Gasc J. M., Paulin D. and Corvol P. (1992) Identification and characterization of neutral endopeptidase in endothelial cells from venous or arterial origins. J. Biol. Chem. 267, 14 012-14 018.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14012-14018
    • Llorens-Cortes, C.1    Huang, H.2    Vicart, P.3    Gasc, J.M.4    Paulin, D.5    Corvol, P.6
  • 25
    • 0021211465 scopus 로고
    • The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11
    • Matsas R., Kenny A. J. and Turner A. J. (1984) The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.11. Biochem. J. 223, 433-440.
    • (1984) Biochem. J. , vol.223 , pp. 433-440
    • Matsas, R.1    Kenny, A.J.2    Turner, A.J.3
  • 26
    • 0029800662 scopus 로고    scopus 로고
    • Metabolism and functions of neuropeptide Y
    • Medeiros Mdos S. and Turner A. J. (1996) Metabolism and functions of neuropeptide Y. Neurochem. Res. 21, 1125-1132.
    • (1996) Neurochem. Res. , vol.21 , pp. 1125-1132
    • Medeiros Mdos, S.1    Turner, A.J.2
  • 27
    • 0019822497 scopus 로고
    • Purification of a membrane-bound metalloendopeptidase from porcine kidney that degrades peptide hormones
    • Mumford R. A., Pierzchala P. A., Strauss A. W. and Zimmerman M. (1981) Purification of a membrane-bound metalloendopeptidase from porcine kidney that degrades peptide hormones. Proc. Natl Acad. Sci. USA 78, 6623-6627.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 6623-6627
    • Mumford, R.A.1    Pierzchala, P.A.2    Strauss, A.W.3    Zimmerman, M.4
  • 28
    • 0034619582 scopus 로고    scopus 로고
    • Endothelin-converting enzymes and endothelin receptor B messenger RNAs are expressed in different neural cell species and these messenger RNAs are coordinately induced in neurons and astrocytes respectively following nerve injury
    • Nakagomi S., Kiryu-Seo S. and Kiyama H. (2000) Endothelin-converting enzymes and endothelin receptor B messenger RNAs are expressed in different neural cell species and these messenger RNAs are coordinately induced in neurons and astrocytes respectively following nerve injury. Neuroscience 101, 441-449.
    • (2000) Neuroscience , vol.101 , pp. 441-449
    • Nakagomi, S.1    Kiryu-Seo, S.2    Kiyama, H.3
  • 29
    • 2642593603 scopus 로고
    • Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts
    • O'Donnell-Tormey J. and Quigley J. P. (1983) Detection and partial characterization of a chymostatin-sensitive endopeptidase in transformed fibroblasts. Proc. Natl Acad. Sci. USA 80, 344-348.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 344-348
    • O'Donnell-Tormey, J.1    Quigley, J.P.2
  • 30
    • 0035832117 scopus 로고    scopus 로고
    • Brevican in the developing hippocampal fimbria: Differential expression in myelinating oligodendrocytes and adult astrocytes suggests a dual role for brevican in central nervous system fiber tract development
    • Ogawa T., Hagihara K., Suzuki M. and Yamaguchi Y. (2001) Brevican in the developing hippocampal fimbria: differential expression in myelinating oligodendrocytes and adult astrocytes suggests a dual role for brevican in central nervous system fiber tract development. J. Comp. Neurol. 432, 285-295.
    • (2001) J. Comp. Neurol. , vol.432 , pp. 285-295
    • Ogawa, T.1    Hagihara, K.2    Suzuki, M.3    Yamaguchi, Y.4
  • 31
    • 8644234198 scopus 로고    scopus 로고
    • Expression of damage-induced neuronal endopeptidase (DINE) mRNA in peri-infarct cortical and thalamic neurons following middle cerebral artery occlusion
    • Ohba N., Kiryu-Seo S., Maeda M., Muraoka M., Ishii M. and Kiyama H. (2004) Expression of damage-induced neuronal endopeptidase (DINE) mRNA in peri-infarct cortical and thalamic neurons following middle cerebral artery occlusion. J. Neurochem. 91, 956-964.
    • (2004) J. Neurochem. , vol.91 , pp. 956-964
    • Ohba, N.1    Kiryu-Seo, S.2    Maeda, M.3    Muraoka, M.4    Ishii, M.5    Kiyama, H.6
  • 32
    • 0024244762 scopus 로고
    • Effects of α-MSH on sleep, behavior, and brain temperature: Interactions with IL-1
    • Opp M. R., Obal F. Jr, and Krueger J. M. (1988) Effects of α-MSH on sleep, behavior, and brain temperature: interactions with IL-1. Am. J. Physiol. 255, R914-R922.
    • (1988) Am. J. Physiol. , vol.255
    • Opp, M.R.1    Obal Jr., F.2    Krueger, J.M.3
  • 34
    • 0034755665 scopus 로고    scopus 로고
    • The neuroendocrinology of chronic fatigue syndrome and fibromyalgia
    • Parker A. J., Wessely S. and Cleare A. J. (2001) The neuroendocrinology of chronic fatigue syndrome and fibromyalgia. Psychol. Med. 31, 1331-1345.
    • (2001) Psychol. Med. , vol.31 , pp. 1331-1345
    • Parker, A.J.1    Wessely, S.2    Cleare, A.J.3
  • 36
    • 0034704345 scopus 로고    scopus 로고
    • Identification and characterization of two androgen response regions in the human neutral endopeptidase gene
    • Shen R., Sumitomo M., Dai J. et al. (2000) Identification and characterization of two androgen response regions in the human neutral endopeptidase gene. Mol. Cell Endocrinol. 170, 131-142.
    • (2000) Mol. Cell Endocrinol. , vol.170 , pp. 131-142
    • Shen, R.1    Sumitomo, M.2    Dai, J.3
  • 37
    • 0028261084 scopus 로고
    • Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells
    • Shimada K., Takahashi M. and Tanzawa K. (1994) Cloning and functional expression of endothelin-converting enzyme from rat endothelial cells. J. Biol Chem. 269, 18 275-18 278.
    • (1994) J. Biol Chem. , vol.269 , pp. 18275-18278
    • Shimada, K.1    Takahashi, M.2    Tanzawa, K.3
  • 38
    • 0036526050 scopus 로고    scopus 로고
    • Sleep and the hypothalamo-pituitary-adrenocortical system
    • Steiger A. (2002) Sleep and the hypothalamo-pituitary-adrenocortical system. Sleep Med. Rev. 6, 125-138.
    • (2002) Sleep Med. Rev. , vol.6 , pp. 125-138
    • Steiger, A.1
  • 39
    • 0347279895 scopus 로고    scopus 로고
    • Sleep and endocrine regulation
    • Steiger A. (2003) Sleep and endocrine regulation. Front Biosci. 8, s358-s376.
    • (2003) Front Biosci. , vol.8
    • Steiger, A.1
  • 42
    • 0030899822 scopus 로고    scopus 로고
    • Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX
    • Turner A. J. and Tanzawa K. (1997) Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX. FASEB J. 11, 355-364.
    • (1997) FASEB J. , vol.11 , pp. 355-364
    • Turner, A.J.1    Tanzawa, K.2
  • 43
    • 0035112440 scopus 로고    scopus 로고
    • The neprilysin (NEP) family of zinc metalloendopeptidases: Genomics and function
    • Turner A. J., Isaac R. E. and Coates D. (2001) The neprilysin (NEP) family of zinc metalloendopeptidases: genomics and function. Bioessays 23, 261-269.
    • (2001) Bioessays , vol.23 , pp. 261-269
    • Turner, A.J.1    Isaac, R.E.2    Coates, D.3
  • 44
    • 0033524706 scopus 로고    scopus 로고
    • XCE, a new member of the endothelin-converting enzyme and neutral endopeptidase family, is preferentially expressed in the CNS
    • Valdenaire O., Richards J. G., Faull R. L. and Schweizer A. (1999) XCE, a new member of the endothelin-converting enzyme and neutral endopeptidase family, is preferentially expressed in the CNS. Mol. Brain Res. 64, 211-221.
    • (1999) Mol. Brain Res. , vol.64 , pp. 211-221
    • Valdenaire, O.1    Richards, J.G.2    Faull, R.L.3    Schweizer, A.4
  • 45
    • 0024438636 scopus 로고
    • Localization of enkephalinase mRNA in rat brain by in situ hybridization: Comparison with immunohistochemical localization of the protein
    • Wilcox J. N., Pollard H., Moreau J., Schwartz J. C. and Malfroy B. (1989) Localization of enkephalinase mRNA in rat brain by in situ hybridization: comparison with immunohistochemical localization of the protein. Neuropeptides 14, 77-83.
    • (1989) Neuropeptides , vol.14 , pp. 77-83
    • Wilcox, J.N.1    Pollard, H.2    Moreau, J.3    Schwartz, J.C.4    Malfroy, B.5
  • 46
    • 0026605307 scopus 로고
    • In vivo metabolism of angiotensin I by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats
    • Yamamoto K., Chappell M. C., Brosnihan K. B. and Ferrario C. M. (1992) In vivo metabolism of angiotensin I by neutral endopeptidase (EC 3.4.24.11) in spontaneously hypertensive rats. Hypertension 19, 692-696.
    • (1992) Hypertension , vol.19 , pp. 692-696
    • Yamamoto, K.1    Chappell, M.C.2    Brosnihan, K.B.3    Ferrario, C.M.4


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