메뉴 건너뛰기




Volumn 40, Issue 1, 2010, Pages 53-62

Prolyl endopeptidase mRNA expression in the central nervous system during rat development

Author keywords

In situ hybridization; Ontogeny; Peptidase; QRT PCR

Indexed keywords

MESSENGER RNA; PROLINE; PROLYL ENDOPEPTIDASE; SERINE PROTEINASE;

EID: 77952548639     PISSN: 08910618     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jchemneu.2010.03.002     Document Type: Article
Times cited : (9)

References (77)
  • 1
    • 0344395063 scopus 로고    scopus 로고
    • Ontogeny of soluble and particulate prolyl endopeptidase activity in several areas of the rat brain and in the pituitary gland
    • Agirregoitia N., Irazusta A., Ruiz F., Irazusta J., Gil J. Ontogeny of soluble and particulate prolyl endopeptidase activity in several areas of the rat brain and in the pituitary gland. Dev. Neurosci. 2003, 25:316-323.
    • (2003) Dev. Neurosci. , vol.25 , pp. 316-323
    • Agirregoitia, N.1    Irazusta, A.2    Ruiz, F.3    Irazusta, J.4    Gil, J.5
  • 3
    • 33846890219 scopus 로고    scopus 로고
    • Ontogeny of prolyl endopeptidase and pyroglutamyl peptidase I in rat tissues
    • Agirregoitia N., Casis L., Gil J., Ruiz F., Irazusta J. Ontogeny of prolyl endopeptidase and pyroglutamyl peptidase I in rat tissues. Regul. Pept. 2007, 139:52-58.
    • (2007) Regul. Pept. , vol.139 , pp. 52-58
    • Agirregoitia, N.1    Casis, L.2    Gil, J.3    Ruiz, F.4    Irazusta, J.5
  • 5
    • 0015383228 scopus 로고
    • Postnatal development of the cerebellar cortex in the rat. II. Phases in the maturation of Purkinje cells and of the molecular layer
    • Altman J. Postnatal development of the cerebellar cortex in the rat. II. Phases in the maturation of Purkinje cells and of the molecular layer. J. Comp. Neurol. 1972, 145:399-463.
    • (1972) J. Comp. Neurol. , vol.145 , pp. 399-463
    • Altman, J.1
  • 6
    • 40749138146 scopus 로고    scopus 로고
    • The stress system in depression and neurodegeneration: focus on the human hypothalamus
    • Bao A.M., Meynen G., Swaab D.F. The stress system in depression and neurodegeneration: focus on the human hypothalamus. Brain Res. Rev. 2008, 57:531-553.
    • (2008) Brain Res. Rev. , vol.57 , pp. 531-553
    • Bao, A.M.1    Meynen, G.2    Swaab, D.F.3
  • 7
    • 8544244410 scopus 로고    scopus 로고
    • Development of the telencephalon: neural stem cells, neurogenesis, and neuronal migration
    • Elsevier Academic Press, San Diego, CA, G. Paxinos (Ed.)
    • Bayer S.A., Altman J. Development of the telencephalon: neural stem cells, neurogenesis, and neuronal migration. The Rat Nervous System 2004, Elsevier Academic Press, San Diego, CA. G. Paxinos (Ed.).
    • (2004) The Rat Nervous System
    • Bayer, S.A.1    Altman, J.2
  • 8
    • 0037342917 scopus 로고    scopus 로고
    • Effect of S 17092, a novel prolyl endopeptidase inhibitor, on substance P and alpha-melanocyte-stimulating hormone breakdown in the rat brain
    • Bellemère G., Morain P., Vaudry H., Jegou S. Effect of S 17092, a novel prolyl endopeptidase inhibitor, on substance P and alpha-melanocyte-stimulating hormone breakdown in the rat brain. J. Neurochem. 2003, 84:919-929.
    • (2003) J. Neurochem. , vol.84 , pp. 919-929
    • Bellemère, G.1    Morain, P.2    Vaudry, H.3    Jegou, S.4
  • 9
    • 19044379994 scopus 로고    scopus 로고
    • Effect of prolyl endopeptidase inhibition on arginine-vasopressin and thyrotrophin-releasing hormone catabolism in the rat brain
    • Bellemère G., Vaudry H., Morain P., Jégou S. Effect of prolyl endopeptidase inhibition on arginine-vasopressin and thyrotrophin-releasing hormone catabolism in the rat brain. J. Neuroendocrinol. 2005, 17:306-313.
    • (2005) J. Neuroendocrinol. , vol.17 , pp. 306-313
    • Bellemère, G.1    Vaudry, H.2    Morain, P.3    Jégou, S.4
  • 10
    • 1542314779 scopus 로고    scopus 로고
    • Localization of the mRNA encoding prolyl endopeptidase in the rat brain and pituitary
    • Bellemère G., Vaudry H., Mounien L., Boutelet I., Jégou S. Localization of the mRNA encoding prolyl endopeptidase in the rat brain and pituitary. J. Comp. Neurol. 2004, 471:128-143.
    • (2004) J. Comp. Neurol. , vol.471 , pp. 128-143
    • Bellemère, G.1    Vaudry, H.2    Mounien, L.3    Boutelet, I.4    Jégou, S.5
  • 11
    • 0031027044 scopus 로고    scopus 로고
    • GAP-43: an intrinsic determinant of neuronal development and plasticity
    • Benowitz L., Routtenberg Q.A. GAP-43: an intrinsic determinant of neuronal development and plasticity. Trends Neurosci. 1997, 20:84-91.
    • (1997) Trends Neurosci. , vol.20 , pp. 84-91
    • Benowitz, L.1    Routtenberg, Q.A.2
  • 12
    • 0021258597 scopus 로고
    • Ontogeny of brain neurotensin in the rat: a radioimmunoassay study
    • Bissette G., Richardson C., Kizer J.S., Nemeroff C.B. Ontogeny of brain neurotensin in the rat: a radioimmunoassay study. J. Neurochem. 1984, 43:283-287.
    • (1984) J. Neurochem. , vol.43 , pp. 283-287
    • Bissette, G.1    Richardson, C.2    Kizer, J.S.3    Nemeroff, C.B.4
  • 13
    • 0027379382 scopus 로고
    • Control of pulsatile secretion of gonadotrophin releasing hormone from hypothalamic explants
    • Bourguignon J.P., Gerard A., Alvarez Gonzalez M.L., Franchimont P. Control of pulsatile secretion of gonadotrophin releasing hormone from hypothalamic explants. Hum. Reprod. 1993, 8(Suppl. 2):18-22.
    • (1993) Hum. Reprod. , vol.8 , Issue.SUPPL. 2 , pp. 18-22
    • Bourguignon, J.P.1    Gerard, A.2    Alvarez Gonzalez, M.L.3    Franchimont, P.4
  • 14
    • 33845477051 scopus 로고    scopus 로고
    • Suggested functions for prolyl oligopeptidase: a puzzling paradox
    • Brandt I., Scharpe S., Lambeir A.M. Suggested functions for prolyl oligopeptidase: a puzzling paradox. Clin. Chim. Acta 2007, 377:50-61.
    • (2007) Clin. Chim. Acta , vol.377 , pp. 50-61
    • Brandt, I.1    Scharpe, S.2    Lambeir, A.M.3
  • 17
    • 0019252656 scopus 로고
    • Ontogeny of vasopressin and oxytocin in the fetal rat: early vasopressinergic innervation of the fetal brain
    • Buijs R.M., Velis D.N., Swaab D.F. Ontogeny of vasopressin and oxytocin in the fetal rat: early vasopressinergic innervation of the fetal brain. Peptides 1980, 1:315-324.
    • (1980) Peptides , vol.1 , pp. 315-324
    • Buijs, R.M.1    Velis, D.N.2    Swaab, D.F.3
  • 18
    • 19444377984 scopus 로고    scopus 로고
    • How can the mood stabilizer VPA limit both mania and depression?
    • Cheng L., Lumb M., Polgar L., Mudge A.W. How can the mood stabilizer VPA limit both mania and depression?. Mol. Cell. Neurosci. 2005, 29:155-161.
    • (2005) Mol. Cell. Neurosci. , vol.29 , pp. 155-161
    • Cheng, L.1    Lumb, M.2    Polgar, L.3    Mudge, A.W.4
  • 19
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 1987, 162:156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 21
    • 0027238835 scopus 로고
    • A survey of the cerebral regionalization and ontogeny of eight exo- and endopeptidases in murines
    • Dauch P., Masuo Y., Vincent J.P., Checler F. A survey of the cerebral regionalization and ontogeny of eight exo- and endopeptidases in murines. Peptides 1993, 14:593-599.
    • (1993) Peptides , vol.14 , pp. 593-599
    • Dauch, P.1    Masuo, Y.2    Vincent, J.P.3    Checler, F.4
  • 23
    • 0020057301 scopus 로고
    • Subcellular distribution of prolyl endopeptidase and cation-sensitive neutral endopeptidase in rabbit brain
    • Dresdner K., Barker L.A., Orlowski M., Wilk S. Subcellular distribution of prolyl endopeptidase and cation-sensitive neutral endopeptidase in rabbit brain. J. Neurochem. 1982, 38:1151-1154.
    • (1982) J. Neurochem. , vol.38 , pp. 1151-1154
    • Dresdner, K.1    Barker, L.A.2    Orlowski, M.3    Wilk, S.4
  • 26
    • 84940123948 scopus 로고
    • Ontogeny of arginine vasopressin-immunoreactive neurons in the hypothalamus of fetal and newborn sheep
    • Faucher D.J., Evans P.J., Khurana R., Miller M.M. Ontogeny of arginine vasopressin-immunoreactive neurons in the hypothalamus of fetal and newborn sheep. Acta Anat. (Basel) 1994, 149:279-290.
    • (1994) Acta Anat. (Basel) , vol.149 , pp. 279-290
    • Faucher, D.J.1    Evans, P.J.2    Khurana, R.3    Miller, M.M.4
  • 27
    • 0025648967 scopus 로고
    • Distribution and ontogeny of thyrotropin-releasing hormone degrading enzymes in rats
    • Fuse Y., Polk D.H., Lam R.W., Reviczky A.L., Fisher D.A. Distribution and ontogeny of thyrotropin-releasing hormone degrading enzymes in rats. Am. J. Physiol. 1990, 259:E787-E791.
    • (1990) Am. J. Physiol. , vol.259
    • Fuse, Y.1    Polk, D.H.2    Lam, R.W.3    Reviczky, A.L.4    Fisher, D.A.5
  • 29
    • 0028873829 scopus 로고
    • The role of neuropeptides in learning: focus on the neurokinin substance P
    • Huston J.P., Hasenohrl R.U. The role of neuropeptides in learning: focus on the neurokinin substance P. Behav. Brain Res. 1995, 66:117-127.
    • (1995) Behav. Brain Res. , vol.66 , pp. 117-127
    • Huston, J.P.1    Hasenohrl, R.U.2
  • 31
    • 0031913776 scopus 로고    scopus 로고
    • CDNA cloning of mouse prolyl endopeptidase and its involvement in DNA synthesis by Swiss 3T3 cells
    • Ishino T., Ohtsuki S., Homma K., Natori S. cDNA cloning of mouse prolyl endopeptidase and its involvement in DNA synthesis by Swiss 3T3 cells. J. Biochem. (Tokyo) 1998, 123:540-545.
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 540-545
    • Ishino, T.1    Ohtsuki, S.2    Homma, K.3    Natori, S.4
  • 33
    • 0035852759 scopus 로고    scopus 로고
    • The effects of aging on gene expression in the hypothalamus and cortex of mice
    • Jiang C.H., Tsien J.Z., Schultz P.G., Hu Y. The effects of aging on gene expression in the hypothalamus and cortex of mice. Proc. Natl. Acad. Sci. U.S.A. 2001, 98:1930-1934.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 1930-1934
    • Jiang, C.H.1    Tsien, J.Z.2    Schultz, P.G.3    Hu, Y.4
  • 34
    • 0032188925 scopus 로고    scopus 로고
    • Prolyl endopeptidase from Sphingomonas capsulata: isolation and characterization of the enzyme and nucleotide sequence of the gene
    • Kabashima T., Fujii M., Meng Y., Ito K., Yoshimoto T. Prolyl endopeptidase from Sphingomonas capsulata: isolation and characterization of the enzyme and nucleotide sequence of the gene. Arch. Biochem. Biophys. 1998, 358:141-148.
    • (1998) Arch. Biochem. Biophys. , vol.358 , pp. 141-148
    • Kabashima, T.1    Fujii, M.2    Meng, Y.3    Ito, K.4    Yoshimoto, T.5
  • 35
    • 0018946189 scopus 로고
    • Changes in prolyl endopeptidase during maturation of rat brain and hydrolysis of substance P by the purified enzyme
    • Kato T., Nakano T., Kojima K., Nagatsu T., Sakakibara S. Changes in prolyl endopeptidase during maturation of rat brain and hydrolysis of substance P by the purified enzyme. J. Neurochem. 1980, 35:527-535.
    • (1980) J. Neurochem. , vol.35 , pp. 527-535
    • Kato, T.1    Nakano, T.2    Kojima, K.3    Nagatsu, T.4    Sakakibara, S.5
  • 36
    • 0028446574 scopus 로고
    • A prolyl endoproteinase that acts specifically on the extrinsic 18-kDa protein of photosystem II: purification and further characterization
    • Kuwabara T., Suzuki K. A prolyl endoproteinase that acts specifically on the extrinsic 18-kDa protein of photosystem II: purification and further characterization. Plant. Cell. Physiol. 1994, 35:665-675.
    • (1994) Plant. Cell. Physiol. , vol.35 , pp. 665-675
    • Kuwabara, T.1    Suzuki, K.2
  • 37
    • 0028272080 scopus 로고
    • Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts
    • Lew R.A., Tetaz T.J., Glucksman M.J., Roberts J.L., Smith A.I. Evidence for a two-step mechanism of gonadotropin-releasing hormone metabolism by prolyl endopeptidase and metalloendopeptidase EC 3.4.24.15 in ovine hypothalamic extracts. J. Biol. Chem. 1994, 269:12626-12632.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12626-12632
    • Lew, R.A.1    Tetaz, T.J.2    Glucksman, M.J.3    Roberts, J.L.4    Smith, A.I.5
  • 38
    • 0028217535 scopus 로고
    • Lower serum prolyl endopeptidase enzyme activity in major depression: further evidence that peptidases play a role in the pathophysiology of depression
    • Maes M., Goossens F., Scharpe S., Meltzer H.Y., D'Hondt P., Cosyns P. Lower serum prolyl endopeptidase enzyme activity in major depression: further evidence that peptidases play a role in the pathophysiology of depression. Biol. Psychiatr. 1994, 35:545-552.
    • (1994) Biol. Psychiatr. , vol.35 , pp. 545-552
    • Maes, M.1    Goossens, F.2    Scharpe, S.3    Meltzer, H.Y.4    D'Hondt, P.5    Cosyns, P.6
  • 39
    • 0028802506 scopus 로고
    • Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: effects of antidepressants, mood stabilizers, and antipsychotic drugs
    • Maes M., Goossens F., Scharpe S., Calabrese J., Desnyder R., Meltzer H.Y. Alterations in plasma prolyl endopeptidase activity in depression, mania, and schizophrenia: effects of antidepressants, mood stabilizers, and antipsychotic drugs. Psychiatr. Res. 1995, 58:217-225.
    • (1995) Psychiatr. Res. , vol.58 , pp. 217-225
    • Maes, M.1    Goossens, F.2    Scharpe, S.3    Calabrese, J.4    Desnyder, R.5    Meltzer, H.Y.6
  • 41
    • 0029922761 scopus 로고    scopus 로고
    • Comparison of proline endopeptidase activity in brain tissue from normal cases and cases with Alzheimer's disease, Lewy body dementia, Parkinson's disease and Huntington's disease
    • Mantle D., Falkous G., Ishiura S., Blanchard P.J., Perry E.K. Comparison of proline endopeptidase activity in brain tissue from normal cases and cases with Alzheimer's disease, Lewy body dementia, Parkinson's disease and Huntington's disease. Clin. Chim. Acta 1996, 249:129-139.
    • (1996) Clin. Chim. Acta , vol.249 , pp. 129-139
    • Mantle, D.1    Falkous, G.2    Ishiura, S.3    Blanchard, P.J.4    Perry, E.K.5
  • 43
    • 0025042324 scopus 로고
    • Proline-specific proteases in cultivated neuronal and glial cells
    • Mentlein R., von Kolszynski M., Sprang R., Lucius R. Proline-specific proteases in cultivated neuronal and glial cells. Brain Res. 1990, 527:159-162.
    • (1990) Brain Res. , vol.527 , pp. 159-162
    • Mentlein, R.1    von Kolszynski, M.2    Sprang, R.3    Lucius, R.4
  • 44
    • 0142125365 scopus 로고    scopus 로고
    • Factors influencing analysis of prolyl endopeptidase in human blood and cerebrospinal fluid: increase in assay sensitivity
    • Momeni N., Yoshimoto T., Ryberg B., Sandberg-Wollheim M., Grubb A. Factors influencing analysis of prolyl endopeptidase in human blood and cerebrospinal fluid: increase in assay sensitivity. Scand. J. Clin. Lab. Invest. 2003, 63:387-395.
    • (2003) Scand. J. Clin. Lab. Invest. , vol.63 , pp. 387-395
    • Momeni, N.1    Yoshimoto, T.2    Ryberg, B.3    Sandberg-Wollheim, M.4    Grubb, A.5
  • 45
    • 0022707224 scopus 로고
    • In vivo and in vitro development of alpha-MSH and ACTH in the embryonic and postnatal rat brain
    • Monnet-Tschudi F., Eberle A.N., Honegger P. In vivo and in vitro development of alpha-MSH and ACTH in the embryonic and postnatal rat brain. Brain Res. 1986, 391:125-132.
    • (1986) Brain Res. , vol.391 , pp. 125-132
    • Monnet-Tschudi, F.1    Eberle, A.N.2    Honegger, P.3
  • 46
    • 53249090063 scopus 로고    scopus 로고
    • Expression and traffic of cellular prolyl oligopeptidase are regulated during cerebellar granule cell differentiation, maturation, and aging
    • Moreno-Baylach M.J., Felipo V., Mannisto P.T., Garcia-Horsman J.A. Expression and traffic of cellular prolyl oligopeptidase are regulated during cerebellar granule cell differentiation, maturation, and aging. Neuroscience 2008, 156:580-585.
    • (2008) Neuroscience , vol.156 , pp. 580-585
    • Moreno-Baylach, M.J.1    Felipo, V.2    Mannisto, P.T.3    Garcia-Horsman, J.A.4
  • 47
    • 70249089694 scopus 로고    scopus 로고
    • Issues about the physiological functions of prolyl oligopeptidase based on its discordant spatial association with substrates and inconsistencies among mRNA, protein levels, and enzymatic activity
    • Myöhänen T.T., García-Horsman J.A., Tenorio-Laranga J., Männistö P.T. Issues about the physiological functions of prolyl oligopeptidase based on its discordant spatial association with substrates and inconsistencies among mRNA, protein levels, and enzymatic activity. J. Histochem. Cytochem. 2009, 57:831-848.
    • (2009) J. Histochem. Cytochem. , vol.57 , pp. 831-848
    • Myöhänen, T.T.1    García-Horsman, J.A.2    Tenorio-Laranga, J.3    Männistö, P.T.4
  • 48
    • 58149336803 scopus 로고    scopus 로고
    • Localization of prolyl oligopeptidase in the thalamic and cortical projection neurons: a retrograde neurotracing study in the rat brain
    • Myöhänen T.T., Kääriäinen T.M., Jalkanen A.J., Piltonen M., Männistö P.T. Localization of prolyl oligopeptidase in the thalamic and cortical projection neurons: a retrograde neurotracing study in the rat brain. Neurosci. Lett. 2009, 450:201.
    • (2009) Neurosci. Lett. , vol.450 , pp. 201
    • Myöhänen, T.T.1    Kääriäinen, T.M.2    Jalkanen, A.J.3    Piltonen, M.4    Männistö, P.T.5
  • 49
    • 43949142408 scopus 로고    scopus 로고
    • Spatial association of prolyl oligopeptidase, inositol 1,4,5-triphosphate type 1 receptor, substance P and its neurokinin-1 receptor in the rat brain: an immunohistochemical colocalization study
    • Myöhänen T.T., Venalainen J.I., Garcia-Horsman J.A., Mannisto P.T. Spatial association of prolyl oligopeptidase, inositol 1,4,5-triphosphate type 1 receptor, substance P and its neurokinin-1 receptor in the rat brain: an immunohistochemical colocalization study. Neuroscience 2008, 153:1177-1189.
    • (2008) Neuroscience , vol.153 , pp. 1177-1189
    • Myöhänen, T.T.1    Venalainen, J.I.2    Garcia-Horsman, J.A.3    Mannisto, P.T.4
  • 53
    • 0028268660 scopus 로고
    • A prolyl endopeptidase of Sarcophaga peregrina (flesh fly): its purification and suggestion for its participation in the differentiation of the imaginal discs
    • Ohtsuki S., Homma K., Kurata S., Komano H., Natori S. A prolyl endopeptidase of Sarcophaga peregrina (flesh fly): its purification and suggestion for its participation in the differentiation of the imaginal discs. J. Biochem. (Tokyo) 1994, 115:449-453.
    • (1994) J. Biochem. (Tokyo) , vol.115 , pp. 449-453
    • Ohtsuki, S.1    Homma, K.2    Kurata, S.3    Komano, H.4    Natori, S.5
  • 54
    • 0018290958 scopus 로고
    • Purification and properties of a prolyl endopeptidase from rabbit brain
    • Orlowski M., Wilk E., Pearce S., Wilk S. Purification and properties of a prolyl endopeptidase from rabbit brain. J. Neurochem. 1979, 33:461-469.
    • (1979) J. Neurochem. , vol.33 , pp. 461-469
    • Orlowski, M.1    Wilk, E.2    Pearce, S.3    Wilk, S.4
  • 57
    • 0022900108 scopus 로고
    • Ontogeny of substance P receptor binding sites in rat brain
    • Quirion R., Dam T.V. Ontogeny of substance P receptor binding sites in rat brain. J. Neurosci. 1986, 6:2187-2199.
    • (1986) J. Neurosci. , vol.6 , pp. 2187-2199
    • Quirion, R.1    Dam, T.V.2
  • 58
    • 35648968089 scopus 로고    scopus 로고
    • Substance P at the nexus of mind and body in chronic inflammation and affective disorders
    • Rosenkranz M.A. Substance P at the nexus of mind and body in chronic inflammation and affective disorders. Psychol. Bull. 2007, 133:1007-1037.
    • (2007) Psychol. Bull. , vol.133 , pp. 1007-1037
    • Rosenkranz, M.A.1
  • 59
    • 23844502162 scopus 로고    scopus 로고
    • Brain prolyl endopeptidase expression in aging, APP transgenic mice and Alzheimer's disease
    • Rossner S., Schulz I., Zeitschel U., Schliebs R., Bigl V., Demuth H.U. Brain prolyl endopeptidase expression in aging, APP transgenic mice and Alzheimer's disease. Neurochem. Res. 2005, 30:695-702.
    • (2005) Neurochem. Res. , vol.30 , pp. 695-702
    • Rossner, S.1    Schulz, I.2    Zeitschel, U.3    Schliebs, R.4    Bigl, V.5    Demuth, H.U.6
  • 60
    • 0030771506 scopus 로고    scopus 로고
    • Postnatal ontogeny of the thyrotropin-releasing hormone receptor messenger ribonucleic acids in the rat forebrain
    • Satoh T., Yamada M., Feng P., Hashimoto K., Wilber J.F., Mori M. Postnatal ontogeny of the thyrotropin-releasing hormone receptor messenger ribonucleic acids in the rat forebrain. Neuropeptides 1997, 31:351-355.
    • (1997) Neuropeptides , vol.31 , pp. 351-355
    • Satoh, T.1    Yamada, M.2    Feng, P.3    Hashimoto, K.4    Wilber, J.F.5    Mori, M.6
  • 63
    • 0034464737 scopus 로고    scopus 로고
    • Requirement of thyrotropin-releasing hormone for the postnatal functions of pituitary thyrotrophs: ontogeny study of congenital tertiary hypothyroidism in mice
    • Shibusawa N., Yamada M., Hirato J., Monden T., Satoh T., Mori M. Requirement of thyrotropin-releasing hormone for the postnatal functions of pituitary thyrotrophs: ontogeny study of congenital tertiary hypothyroidism in mice. Mol. Endocrinol. 2000, 14:137-146.
    • (2000) Mol. Endocrinol. , vol.14 , pp. 137-146
    • Shibusawa, N.1    Yamada, M.2    Hirato, J.3    Monden, T.4    Satoh, T.5    Mori, M.6
  • 64
    • 0027967899 scopus 로고
    • Pronounced increase in prolyl endopeptidase activity in primary cultures of rat cerebral cortex during neuronal differentiation
    • Szappanos A.E., Lakics V., Erdo S.L. Pronounced increase in prolyl endopeptidase activity in primary cultures of rat cerebral cortex during neuronal differentiation. Neurobiology (Bp) 1994, 2:211-221.
    • (1994) Neurobiology (Bp) , vol.2 , pp. 211-221
    • Szappanos, A.E.1    Lakics, V.2    Erdo, S.L.3
  • 65
    • 0018901958 scopus 로고
    • Catabolism of neuropeptides by a brain proline endopeptidase
    • Taylor W.L., Dixon J.E. Catabolism of neuropeptides by a brain proline endopeptidase. Biochem. Biophys. Res. Commun. 1980, 94:9-15.
    • (1980) Biochem. Biophys. Res. Commun. , vol.94 , pp. 9-15
    • Taylor, W.L.1    Dixon, J.E.2
  • 66
  • 67
    • 0026056946 scopus 로고
    • Early appearance and transient expression of vasopressin receptors in the brain of rat fetus and infant. An autoradiographical and electrophysiological study
    • Tribollet E., Goumaz M., Raggenbass M., Dubois-Dauphin M., Dreifuss J.J. Early appearance and transient expression of vasopressin receptors in the brain of rat fetus and infant. An autoradiographical and electrophysiological study. Dev. Brain Res. 1991, 58:13-24.
    • (1991) Dev. Brain Res. , vol.58 , pp. 13-24
    • Tribollet, E.1    Goumaz, M.2    Raggenbass, M.3    Dubois-Dauphin, M.4    Dreifuss, J.J.5
  • 68
    • 4544329007 scopus 로고    scopus 로고
    • Pyroglutamyl peptidase I and prolyl endopeptidase in human semen: increased activity in necrozoospermia
    • Valdivia A., Irazusta J., Fernandez D., Mugica J., Ochoa C., Casis L. Pyroglutamyl peptidase I and prolyl endopeptidase in human semen: increased activity in necrozoospermia. Regul. Pept. 2004, 122:79-84.
    • (2004) Regul. Pept. , vol.122 , pp. 79-84
    • Valdivia, A.1    Irazusta, J.2    Fernandez, D.3    Mugica, J.4    Ochoa, C.5    Casis, L.6
  • 69
    • 0021084784 scopus 로고
    • Prolyl endopeptidase
    • Wilk S. Prolyl endopeptidase. Life Sci. 1983, 33:2149-2157.
    • (1983) Life Sci. , vol.33 , pp. 2149-2157
    • Wilk, S.1
  • 70
    • 0018903105 scopus 로고
    • Levels of alpha-melanotrophin in the plasma and pituitary glands of fetal and juvenile rats, and in the plasma of adult female rats during pregnancy and lactation
    • Wilson J.F., Morgan M.A. Levels of alpha-melanotrophin in the plasma and pituitary glands of fetal and juvenile rats, and in the plasma of adult female rats during pregnancy and lactation. J. Endocrinol. 1980, 84:363-370.
    • (1980) J. Endocrinol. , vol.84 , pp. 363-370
    • Wilson, J.F.1    Morgan, M.A.2
  • 71
    • 0037118050 scopus 로고    scopus 로고
    • A common mechanism of action for three mood-stabilizing drugs
    • Williams R.S., Cheng L., Mudge A.W., Harwood A.J. A common mechanism of action for three mood-stabilizing drugs. Nature 2002, 417:292-295.
    • (2002) Nature , vol.417 , pp. 292-295
    • Williams, R.S.1    Cheng, L.2    Mudge, A.W.3    Harwood, A.J.4
  • 72
    • 0033305610 scopus 로고    scopus 로고
    • Early prepubertal ontogeny of pulsatile gonadotropin-releasing hormone (GnRH) secretion. I. Inhibitory autofeedback control through prolyl endopeptidase degradation of GnRH
    • Yamanaka C., Lebrethon M.C., Vandersmissen E., Gerard A., Purnelle G., Lemaitre M., Wilk S., Bourguignon J.P. Early prepubertal ontogeny of pulsatile gonadotropin-releasing hormone (GnRH) secretion. I. Inhibitory autofeedback control through prolyl endopeptidase degradation of GnRH. Endocrinology 1999, 140:4609-4615.
    • (1999) Endocrinology , vol.140 , pp. 4609-4615
    • Yamanaka, C.1    Lebrethon, M.C.2    Vandersmissen, E.3    Gerard, A.4    Purnelle, G.5    Lemaitre, M.6    Wilk, S.7    Bourguignon, J.P.8
  • 73
    • 0018893161 scopus 로고
    • Proline-specific endopeptidase from Flavobacterium. Purification and properties
    • Yoshimoto T., Walter R., Tsuru D. Proline-specific endopeptidase from Flavobacterium. Purification and properties. J. Biol. Chem. 1980, 255:4786-4792.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4786-4792
    • Yoshimoto, T.1    Walter, R.2    Tsuru, D.3
  • 74
    • 0018750650 scopus 로고
    • Post-proline cleaving enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man
    • Yoshimoto T., Ogita K., Walter R., Koida M., Tsuru D. Post-proline cleaving enzyme. Synthesis of a new fluorogenic substrate and distribution of the endopeptidase in rat tissues and body fluids of man. Biochim. Biophys. Acta 1979, 569:184-192.
    • (1979) Biochim. Biophys. Acta , vol.569 , pp. 184-192
    • Yoshimoto, T.1    Ogita, K.2    Walter, R.3    Koida, M.4    Tsuru, D.5
  • 76
    • 0026315205 scopus 로고
    • Prolyl endopeptidase from Flavobacterium meningosepticum: cloning and sequencing of the enzyme gene
    • Yoshimoto T., Kanatani A., Shimoda T., Inaoka T., Kokubo T., Tsuru D. Prolyl endopeptidase from Flavobacterium meningosepticum: cloning and sequencing of the enzyme gene. J. Biochem. (Tokyo) 1991, 110:873-878.
    • (1991) J. Biochem. (Tokyo) , vol.110 , pp. 873-878
    • Yoshimoto, T.1    Kanatani, A.2    Shimoda, T.3    Inaoka, T.4    Kokubo, T.5    Tsuru, D.6
  • 77
    • 0026713975 scopus 로고
    • Ontogenesis and binding properties of high-affinity neurotensin receptors in human brain
    • Zsurger N., Chabry J., Coquerel A., Vincent J.P. Ontogenesis and binding properties of high-affinity neurotensin receptors in human brain. Brain Res. 1992, 586:303-310.
    • (1992) Brain Res. , vol.586 , pp. 303-310
    • Zsurger, N.1    Chabry, J.2    Coquerel, A.3    Vincent, J.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.