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Volumn 19, Issue 2, 2009, Pages 259-267

Functional characterization of the human-specific (type II) form of kallikrein 8, a gene involved in learning and memory

Author keywords

Alternative splicing; Cognition; Human evolution; Type II KLK8

Indexed keywords

ISOPROTEIN; KALLIKREIN; KLK8 PROTEIN, HUMAN;

EID: 59449107828     PISSN: 10010602     EISSN: 17487838     Source Type: Journal    
DOI: 10.1038/cr.2009.4     Document Type: Article
Times cited : (12)

References (39)
  • 1
    • 0013394889 scopus 로고    scopus 로고
    • Mechanisms of alternative pre-messenger RNA splicing
    • Black DL. Mechanisms of alternative pre-messenger RNA splicing. Annu Rev Biochem 2003;72:291-336.
    • (2003) Annu Rev Biochem , vol.72 , pp. 291-336
    • Black, D.L.1
  • 2
    • 33745899048 scopus 로고    scopus 로고
    • Alternative splicing: New insights from global analyses
    • Blencowe BJ. Alternative splicing: new insights from global analyses. Cell 2006;126:37-47.
    • (2006) Cell , vol.126 , pp. 37-47
    • Blencowe, B.J.1
  • 3
    • 26444593981 scopus 로고    scopus 로고
    • Evidence of functional selection pressure for alternative splicing events that accelerate evolution of protein subsequences
    • Xing Y, Lee C. Evidence of functional selection pressure for alternative splicing events that accelerate evolution of protein subsequences. Proc Natl Acad Sci USA 2005;102:13526-13531.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 13526-13531
    • Xing, Y.1    Lee, C.2
  • 4
    • 0032549748 scopus 로고    scopus 로고
    • Splicing regulation in neurons: Tinkering with cell-specific control
    • Grabowski PJ. Splicing regulation in neurons: tinkering with cell-specific control. Cell 1998;92:709-712.
    • (1998) Cell , vol.92 , pp. 709-712
    • Grabowski, P.J.1
  • 5
    • 10944272640 scopus 로고    scopus 로고
    • Tau gene alternative splicing: Expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases
    • Andreadis A. Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases. Biochim Biophys Acta 2005;1739:91-103.
    • (2005) Biochim Biophys Acta , vol.1739 , pp. 91-103
    • Andreadis, A.1
  • 6
    • 0032435862 scopus 로고    scopus 로고
    • Alternative splicing of pre-mRNA: Developmental consequences and mechanisms of regulation
    • Lopez AJ. Alternative splicing of pre-mRNA: developmental consequences and mechanisms of regulation. Amu Rev Genet 1998;32:279-305.
    • (1998) Amu Rev Genet , vol.32 , pp. 279-305
    • Lopez, A.J.1
  • 7
    • 0029050958 scopus 로고
    • Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus
    • Chen ZL, Yoshida S, Kato K, et al. Expression and activity-dependent changes of a novel limbic-serine protease gene in the hippocampus. J Neurosci 1995;15:5088-5097.
    • (1995) J Neurosci , vol.15 , pp. 5088-5097
    • Chen, Z.L.1    Yoshida, S.2    Kato, K.3
  • 8
    • 0031842366 scopus 로고    scopus 로고
    • Blockade of neuropsin, a serine protease, ameliorates kindling epilepsy
    • Momota Y, Yoshida S, Ito J, et al. Blockade of neuropsin, a serine protease, ameliorates kindling epilepsy. Eur J Neurosci 1998;10:760-764.
    • (1998) Eur J Neurosci , vol.10 , pp. 760-764
    • Momota, Y.1    Yoshida, S.2    Ito, J.3
  • 9
    • 0030682129 scopus 로고    scopus 로고
    • Effects of oxidative stress on the expression of limbic-specific protease neuropsin and avoidance learning in mice
    • Akita H, Matsuyama T, Iso H, Sugita M, Yoshida S. Effects of oxidative stress on the expression of limbic-specific protease neuropsin and avoidance learning in mice. Brain Res 1997;769:86-96.
    • (1997) Brain Res , vol.769 , pp. 86-96
    • Akita, H.1    Matsuyama, T.2    Iso, H.3    Sugita, M.4    Yoshida, S.5
  • 10
    • 33645864350 scopus 로고    scopus 로고
    • Neuropsin is essential for early processes of memory acquisition and Schaffer collateral long-term potentiation in adult mouse hippocampus in vivo
    • Tamura H, Ishikawa Y, Hino N, et al. Neuropsin is essential for early processes of memory acquisition and Schaffer collateral long-term potentiation in adult mouse hippocampus in vivo. J Physiol 2006;570:541-551.
    • (2006) J Physiol , vol.570 , pp. 541-551
    • Tamura, H.1    Ishikawa, Y.2    Hino, N.3
  • 11
    • 0032525843 scopus 로고    scopus 로고
    • Sequence analysis and expression of human neuropsin cDNA and gene
    • Yoshida S, Taniguchi M, Hirata A, Shiosaka S. Sequence analysis and expression of human neuropsin cDNA and gene. Gene 1998;213:9-16.
    • (1998) Gene , vol.213 , pp. 9-16
    • Yoshida, S.1    Taniguchi, M.2    Hirata, A.3    Shiosaka, S.4
  • 12
    • 0034896563 scopus 로고    scopus 로고
    • The human KLK8 (neuropsin/ovasin) gene: Identification of two novel splice variants and its prognostic value in ovarian cancer
    • Magklara A, Scorilas A, Katsaros D, et al. The human KLK8 (neuropsin/ovasin) gene: identification of two novel splice variants and its prognostic value in ovarian cancer. Clin Cancer Res 2001;7:806- 811.
    • (2001) Clin Cancer Res , vol.7 , pp. 806-811
    • Magklara, A.1    Scorilas, A.2    Katsaros, D.3
  • 13
    • 8144222388 scopus 로고    scopus 로고
    • The emerging roles of human tissue kallikreins in cancer
    • Borgono CA, Diamandis EP. The emerging roles of human tissue kallikreins in cancer. Nat Rev Cancer 2004;4:876-890.
    • (2004) Nat Rev Cancer , vol.4 , pp. 876-890
    • Borgono, C.A.1    Diamandis, E.P.2
  • 15
    • 23244459692 scopus 로고    scopus 로고
    • Human tissue kallikreins: From gene structure to function and clinical applications
    • Yousef GM, Obiezu CV, Luo LY, et al. Human tissue kallikreins: from gene structure to function and clinical applications. Adv Clin Chem 2005;39:11-79.
    • (2005) Adv Clin Chem , vol.39 , pp. 11-79
    • Yousef, G.M.1    Obiezu, C.V.2    Luo, L.Y.3
  • 16
    • 33846241278 scopus 로고    scopus 로고
    • Human kallikrein 8 protease confers a favorable clinical outcome in non-small cell lung cancer by suppressing tumor cell invasiveness
    • Sher YP, Chou CC, Chou RH, et al. Human kallikrein 8 protease confers a favorable clinical outcome in non-small cell lung cancer by suppressing tumor cell invasiveness. Cancer Res 2006;66:11763- 11770.
    • (2006) Cancer Res , vol.66 , pp. 11763-11770
    • Sher, Y.P.1    Chou, C.C.2    Chou, R.H.3
  • 17
    • 0033559559 scopus 로고    scopus 로고
    • A novel form of human neuropsin, a brain-related serine protease, is generated by alternative splicing and is expressed preferentially in human adult brain
    • Mitsui S, Tsuruoka N, Yamashiro K, Nakazato H, Yamaguchi N. A novel form of human neuropsin, a brain-related serine protease, is generated by alternative splicing and is expressed preferentially in human adult brain. Eur J Biochem 1999;260:627-634.
    • (1999) Eur J Biochem , vol.260 , pp. 627-634
    • Mitsui, S.1    Tsuruoka, N.2    Yamashiro, K.3    Nakazato, H.4    Yamaguchi, N.5
  • 18
    • 34948887671 scopus 로고    scopus 로고
    • A human-specific mutation leads to the origin of a novel splice form of neuropsin (KLK8), a gene involved in learning and memory
    • Lu ZX, Peng J, Su B. A human-specific mutation leads to the origin of a novel splice form of neuropsin (KLK8), a gene involved in learning and memory. Hum Mutat 2007;28:978-984.
    • (2007) Hum Mutat , vol.28 , pp. 978-984
    • Lu, Z.X.1    Peng, J.2    Su, B.3
  • 19
    • 28844506112 scopus 로고    scopus 로고
    • Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins
    • Rajapakse S, Ogiwara K, Takano N, Moriyama A, Takahashi T. Biochemical characterization of human kallikrein 8 and its possible involvement in the degradation of extracellular matrix proteins. FEBS Lett 2005;579:6879-6884.
    • (2005) FEBS Lett , vol.579 , pp. 6879-6884
    • Rajapakse, S.1    Ogiwara, K.2    Takano, N.3    Moriyama, A.4    Takahashi, T.5
  • 20
    • 33745679371 scopus 로고    scopus 로고
    • Activation and enzymatic characterization of recombinant human kallikrein 8
    • Kishi T, Cloutier SM, Kundig C, Deperthes D, Diamandis EP. Activation and enzymatic characterization of recombinant human kallikrein 8. Biol Chem 2006;387:723-731.
    • (2006) Biol Chem , vol.387 , pp. 723-731
    • Kishi, T.1    Cloutier, S.M.2    Kundig, C.3    Deperthes, D.4    Diamandis, E.P.5
  • 21
    • 0030598059 scopus 로고    scopus 로고
    • Kindling induces neuropsin mRNA in the mouse brain
    • Okabe A, Momota Y, Yoshida S, et al. Kindling induces neuropsin mRNA in the mouse brain. Brain Res 1996;728:116-120.
    • (1996) Brain Res , vol.728 , pp. 116-120
    • Okabe, A.1    Momota, Y.2    Yoshida, S.3
  • 22
    • 0035099709 scopus 로고    scopus 로고
    • Expression of neuropsin in oligodendrocytes after injury to the CNS
    • He XP, Shiosaka S, Yoshida S. Expression of neuropsin in oligodendrocytes after injury to the CNS. Neurosci Res 2001;39:455-462.
    • (2001) Neurosci Res , vol.39 , pp. 455-462
    • He, X.P.1    Shiosaka, S.2    Yoshida, S.3
  • 23
    • 0028875106 scopus 로고
    • Ontogeny of neuropsin mRNA expression in the mouse brain
    • Suzuki J, Yoshida S, Chen ZL, et al. Ontogeny of neuropsin mRNA expression in the mouse brain. Neurosci Res 1995;23:345-351.
    • (1995) Neurosci Res , vol.23 , pp. 345-351
    • Suzuki, J.1    Yoshida, S.2    Chen, Z.L.3
  • 24
    • 34248368920 scopus 로고    scopus 로고
    • The implications of alternative splicing in the ENCODE protein complement
    • Tress ML, Martelli PL, Frankish A, et al. The implications of alternative splicing in the ENCODE protein complement. Proc Natl Acad Sci USA 2007;104:5495-5500.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5495-5500
    • Tress, M.L.1    Martelli, P.L.2    Frankish, A.3
  • 25
    • 22544482100 scopus 로고    scopus 로고
    • Schmuck EM, Board Whitbread AK, et al. Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-atonset of Alzheimer's and Parkinson's diseases. Pharmacogenet Genomics 2005;15:493-501.
    • Schmuck EM, Board PG, Whitbread AK, et al. Characterization of the monomethylarsonate reductase and dehydroascorbate reductase activities of Omega class glutathione transferase variants: implications for arsenic metabolism and the age-atonset of Alzheimer's and Parkinson's diseases. Pharmacogenet Genomics 2005;15:493-501.
  • 26
    • 33344471142 scopus 로고    scopus 로고
    • Regulation of gene expression by alternative untranslated regions
    • Hughes TA. Regulation of gene expression by alternative untranslated regions. Trends Genet 2006;22:119-122.
    • (2006) Trends Genet , vol.22 , pp. 119-122
    • Hughes, T.A.1
  • 27
    • 0035802386 scopus 로고    scopus 로고
    • Structural and functional features of eukaryotic mRNA untranslated regions
    • Pesole G, Mignone F, Gissi C, Grillo G, Licciulli F, Liuni S. Structural and functional features of eukaryotic mRNA untranslated regions. Gene 2001;276:73-81.
    • (2001) Gene , vol.276 , pp. 73-81
    • Pesole, G.1    Mignone, F.2    Gissi, C.3    Grillo, G.4    Licciulli, F.5    Liuni, S.6
  • 28
    • 0141888375 scopus 로고    scopus 로고
    • A slow RNA polymerase II affects alternative splicing in vivo
    • de la Mata M, Alonso CR, Kadener S, et al. A slow RNA polymerase II affects alternative splicing in vivo. Mol Cell 2003;12:525-532.
    • (2003) Mol Cell , vol.12 , pp. 525-532
    • de la Mata, M.1    Alonso, C.R.2    Kadener, S.3
  • 29
    • 19344363974 scopus 로고    scopus 로고
    • Promoter usage and alternative splicing
    • Kornblihtt AR. Promoter usage and alternative splicing. Curr Opin Cell Biol 2005;17:262-268.
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 262-268
    • Kornblihtt, A.R.1
  • 30
    • 0033638283 scopus 로고    scopus 로고
    • Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1
    • Monsalve M, Wu Z, Adelmant G, Puigserver P, Fan M, Spiegelman BM. Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1. Mol Cell 2000;6:307-316.
    • (2000) Mol Cell , vol.6 , pp. 307-316
    • Monsalve, M.1    Wu, Z.2    Adelmant, G.3    Puigserver, P.4    Fan, M.5    Spiegelman, B.M.6
  • 31
    • 0037230511 scopus 로고    scopus 로고
    • Human kallikrein 8: Immunoassay development and identification in tissue extracts and biological fluids
    • Kishi T, Grass L, Soosaipillai A, Shimizu-Okabe C, Diamandis EP. Human kallikrein 8: immunoassay development and identification in tissue extracts and biological fluids. Clin Chem 2003;49:87-96.
    • (2003) Clin Chem , vol.49 , pp. 87-96
    • Kishi, T.1    Grass, L.2    Soosaipillai, A.3    Shimizu-Okabe, C.4    Diamandis, E.P.5
  • 32
    • 0032079713 scopus 로고    scopus 로고
    • Characterization of recombinant and brain neuropsin, a plasticity-related serine protease
    • Shimizu C, Yoshida S, Shibata M, et al. Characterization of recombinant and brain neuropsin, a plasticity-related serine protease. J Biol Chem 1998;273:11189-11196.
    • (1998) J Biol Chem , vol.273 , pp. 11189-11196
    • Shimizu, C.1    Yoshida, S.2    Shibata, M.3
  • 33
  • 34
    • 0036838367 scopus 로고    scopus 로고
    • Decidualization induces the expression and activation of an extracellular protease neuropsin in mouse uterus
    • Matsumoto-Miyai K, Kitagawa R, Ninomiya A, Momota Y, Yoshida S, Shiosaka S. Decidualization induces the expression and activation of an extracellular protease neuropsin in mouse uterus. Biol Reprod 2002;67:1414-1418.
    • (2002) Biol Reprod , vol.67 , pp. 1414-1418
    • Matsumoto-Miyai, K.1    Kitagawa, R.2    Ninomiya, A.3    Momota, Y.4    Yoshida, S.5    Shiosaka, S.6
  • 35
    • 0031905989 scopus 로고    scopus 로고
    • Expression of neuropsin mRNA in the mouse embryo and the pregnant uterus
    • Chen ZL, Momota Y, Kato K et al. Expression of neuropsin mRNA in the mouse embryo and the pregnant uterus. J Histochem Cytochem 1998;46:313-320.
    • (1998) J Histochem Cytochem , vol.46 , pp. 313-320
    • Chen, Z.L.1    Momota, Y.2    Kato, K.3
  • 36
    • 0037155560 scopus 로고    scopus 로고
    • Extracellular serine protease neuropsin (KLK8) modulates neurite outgrowth and fasciculation of mouse hippocampal neurons in culture
    • Oka T, Akisada M, Okabe A, Sakurai K, Shiosaka S, Kato K. Extracellular serine protease neuropsin (KLK8) modulates neurite outgrowth and fasciculation of mouse hippocampal neurons in culture. Neurosci Lett 2002;321:141-144.
    • (2002) Neurosci Lett , vol.321 , pp. 141-144
    • Oka, T.1    Akisada, M.2    Okabe, A.3    Sakurai, K.4    Shiosaka, S.5    Kato, K.6
  • 37
    • 0035066198 scopus 로고    scopus 로고
    • Abnormalities of synapses and neurons in the hippocampus of neuropsin-deficient mice
    • Hirata A, Yoshida S, Inoue N, et al. Abnormalities of synapses and neurons in the hippocampus of neuropsin-deficient mice. Mol Cell Neurosci 2001;17:600-610.
    • (2001) Mol Cell Neurosci , vol.17 , pp. 600-610
    • Hirata, A.1    Yoshida, S.2    Inoue, N.3
  • 38
    • 0037177876 scopus 로고    scopus 로고
    • Role of loop structures of neuropsin in the activity of serine protease and regulated secretion
    • Oka T, Hakoshima T, Itakura M, et al. Role of loop structures of neuropsin in the activity of serine protease and regulated secretion. J Biol Chem 2002;277:14724-14730.
    • (2002) J Biol Chem , vol.277 , pp. 14724-14730
    • Oka, T.1    Hakoshima, T.2    Itakura, M.3
  • 39
    • 0008297599 scopus 로고    scopus 로고
    • Neuropsin regulates an early phase of schaffer-collateral long-term potentiation in the murine hippocampus
    • Komai S, Matsuyama T, Matsumoto K, et al. Neuropsin regulates an early phase of schaffer-collateral long-term potentiation in the murine hippocampus. Eur J Neurosci 2000;12:1479-1486.
    • (2000) Eur J Neurosci , vol.12 , pp. 1479-1486
    • Komai, S.1    Matsuyama, T.2    Matsumoto, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.