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Volumn 10, Issue SUPPL. 1, 2010, Pages

Importance of research on peptidylarginine deiminase and citrullinated proteins in age-related disease

Author keywords

Aging; Alzheimer's disease; Citrullinated proteins; Epidermal differentiation; Peptidylarginine deiminase

Indexed keywords

ARGININE; BRAIN PROTEIN; CALCIUM ION; CITRULLINE; FILAGGRIN; GLIAL FIBRILLARY ACIDIC PROTEIN; KAINIC ACID; KERATIN; MONOMER; PROFILAGGRIN; PROTEIN; PROTEIN ARGININE DEIMINASE; HYDROLASE; PROTEIN-ARGININE DEIMINASE;

EID: 77954661595     PISSN: 14441586     EISSN: 14470594     Source Type: Journal    
DOI: 10.1111/j.1447-0594.2010.00593.x     Document Type: Review
Times cited : (43)

References (41)
  • 1
    • 0019161972 scopus 로고
    • Partial purification and specificity of an arginine-converting enzyme from bovine epidermis
    • Kubilus J, Waitkus RF, Baden HP. Partial purification and specificity of an arginine-converting enzyme from bovine epidermis. Biochim Biophys Acta 1980, 615:246-251.
    • (1980) Biochim Biophys Acta , vol.615 , pp. 246-251
    • Kubilus, J.1    Waitkus, R.F.2    Baden, H.P.3
  • 2
    • 0011137031 scopus 로고
    • Content of citrulline and other amino acids in a protein of hair follicles
    • Rogers GE, Simmonds DH. Content of citrulline and other amino acids in a protein of hair follicles. Nature 1958, 182:186-187.
    • (1958) Nature , vol.182 , pp. 186-187
    • Rogers, G.E.1    Simmonds, D.H.2
  • 3
    • 0021114827 scopus 로고
    • Purification and properties of a brain enzyme which deiminates proteins
    • Kubilus J, Baden HP. Purification and properties of a brain enzyme which deiminates proteins. Biochim Biophys Acta 1983, 745:285-291.
    • (1983) Biochim Biophys Acta , vol.745 , pp. 285-291
    • Kubilus, J.1    Baden, H.P.2
  • 4
    • 0030583124 scopus 로고    scopus 로고
    • All-trans retinoic acid increases peptidylarginine deiminases in a newborn rat keratinocyte cell line
    • Ishigami A, Ohsawa T, Watanabe K, Senshu T. All-trans retinoic acid increases peptidylarginine deiminases in a newborn rat keratinocyte cell line. Biochem Biophys Res Commun 1996, 223:299-303.
    • (1996) Biochem Biophys Res Commun , vol.223 , pp. 299-303
    • Ishigami, A.1    Ohsawa, T.2    Watanabe, K.3    Senshu, T.4
  • 5
    • 0028914527 scopus 로고
    • Studies of calcineurin-calmodulin interaction: probing the role of arginine residues using peptidylarginine deiminase
    • Imparl JM, Senshu T, Graves DJ. Studies of calcineurin-calmodulin interaction: probing the role of arginine residues using peptidylarginine deiminase. Arch Biochem Biophys 1995, 318:370-377.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 370-377
    • Imparl, J.M.1    Senshu, T.2    Graves, D.J.3
  • 6
    • 0027317616 scopus 로고
    • Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain
    • Lamensa JW, Moscarello MA. Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain. J Neurochem 1993, 61:987-996.
    • (1993) J Neurochem , vol.61 , pp. 987-996
    • Lamensa, J.W.1    Moscarello, M.A.2
  • 7
    • 0029824853 scopus 로고    scopus 로고
    • Protein Unfolding by Peptidylarginine Deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin
    • Tarcsa E, Marekov LN, Mei G, Melino G, Lee S-C, Steinert PM. Protein Unfolding by Peptidylarginine Deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J Biol Chem 1996, 271:30709-30716.
    • (1996) J Biol Chem , vol.271 , pp. 30709-30716
    • Tarcsa, E.1    Marekov, L.N.2    Mei, G.3    Melino, G.4    Lee, S.-C.5    Steinert, P.M.6
  • 8
    • 0032789345 scopus 로고    scopus 로고
    • Studies on specificity of peptidylarginine deiminase reactions using an immunochemical probe that recognizes an enzymatically deiminated partial sequence of mouse keratin K1
    • Senshu T, Akiyama K, Ishigami A, Nomura K. Studies on specificity of peptidylarginine deiminase reactions using an immunochemical probe that recognizes an enzymatically deiminated partial sequence of mouse keratin K1. J Dermatol Sci 1999, 21:113-126.
    • (1999) J Dermatol Sci , vol.21 , pp. 113-126
    • Senshu, T.1    Akiyama, K.2    Ishigami, A.3    Nomura, K.4
  • 9
    • 0029103435 scopus 로고
    • Detection of deiminated proteins in rat skin: probing with a monospecific antibody after modification of citrulline residues
    • Senshu T, Akiyama K, Kan S, Asaga H, Ishigami A, Manabe M. Detection of deiminated proteins in rat skin: probing with a monospecific antibody after modification of citrulline residues. J Invest Dermatol 1995, 105:163-169.
    • (1995) J Invest Dermatol , vol.105 , pp. 163-169
    • Senshu, T.1    Akiyama, K.2    Kan, S.3    Asaga, H.4    Ishigami, A.5    Manabe, M.6
  • 10
    • 20244368810 scopus 로고    scopus 로고
    • Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease
    • Ishigami A, Ohsawa T, Hiratsuka M. Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease. J Neurosci Res 2005, 80:120-128.
    • (2005) J Neurosci Res , vol.80 , pp. 120-128
    • Ishigami, A.1    Ohsawa, T.2    Hiratsuka, M.3
  • 11
    • 0024281847 scopus 로고
    • Combined biochemical and immunochemical comparison of peptidylarginine deiminases present in various tissues
    • Watanabe K, Akiyama K, Hikichi K, Ohtsuka R, Okuyama A, Senshu T. Combined biochemical and immunochemical comparison of peptidylarginine deiminases present in various tissues. Biochim Biophys Acta 1988, 966:375-383.
    • (1988) Biochim Biophys Acta , vol.966 , pp. 375-383
    • Watanabe, K.1    Akiyama, K.2    Hikichi, K.3    Ohtsuka, R.4    Okuyama, A.5    Senshu, T.6
  • 12
    • 0025955772 scopus 로고
    • Three types of mouse peptidylarginine deiminase: characterization and tissue distribution
    • Terakawa H, Takahara H, Sugawara K. Three types of mouse peptidylarginine deiminase: characterization and tissue distribution. J Biochem (Tokyo) 1991, 110:661-666.
    • (1991) J Biochem (Tokyo) , vol.110 , pp. 661-666
    • Terakawa, H.1    Takahara, H.2    Sugawara, K.3
  • 13
    • 0031812033 scopus 로고    scopus 로고
    • Molecular cloning of two novel types of peptidylarginine deiminase cDNAs from retinoic acid-treated culture of a newborn rat keratinocyte cell line
    • Ishigami A, Kuramoto M, Yamada M, Watanabe K, Senshu T. Molecular cloning of two novel types of peptidylarginine deiminase cDNAs from retinoic acid-treated culture of a newborn rat keratinocyte cell line. FEBS Lett 1998, 433:113-118.
    • (1998) FEBS Lett , vol.433 , pp. 113-118
    • Ishigami, A.1    Kuramoto, M.2    Yamada, M.3    Watanabe, K.4    Senshu, T.5
  • 14
    • 0027292204 scopus 로고
    • CDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase. Detection of a 3′-untranslated nucleotide sequence common to the mRNA of transiently expressed genes and rapid turnover of this enzyme's mRNA in the estrous cycle
    • Tsuchida M, Takahara H, Minami N. cDNA nucleotide sequence and primary structure of mouse uterine peptidylarginine deiminase. Detection of a 3′-untranslated nucleotide sequence common to the mRNA of transiently expressed genes and rapid turnover of this enzyme's mRNA in the estrous cycle. Eur J Biochem 1993, 215:677-685.
    • (1993) Eur J Biochem , vol.215 , pp. 677-685
    • Tsuchida, M.1    Takahara, H.2    Minami, N.3
  • 15
    • 0024430819 scopus 로고
    • Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase
    • Watanabe K, Senshu T. Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase. J Biol Chem 1989, 264:15255-15260.
    • (1989) J Biol Chem , vol.264 , pp. 15255-15260
    • Watanabe, K.1    Senshu, T.2
  • 16
    • 0030913713 scopus 로고    scopus 로고
    • Isolation and molecular cloning of epidermal- and hair follicle-specific peptidylarginine deiminase (type III) from rat
    • Nishijyo T, Kawada A, Kanno T, Shiraiwa M, Takahara H. Isolation and molecular cloning of epidermal- and hair follicle-specific peptidylarginine deiminase (type III) from rat. J Biochem (Tokyo) 1997, 121:868-875.
    • (1997) J Biochem (Tokyo) , vol.121 , pp. 868-875
    • Nishijyo, T.1    Kawada, A.2    Kanno, T.3    Shiraiwa, M.4    Takahara, H.5
  • 17
    • 0000668159 scopus 로고    scopus 로고
    • Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse
    • Rus'd AA, Ikejiri Y, Ono H. Molecular cloning of cDNAs of mouse peptidylarginine deiminase type I, type III and type IV, and the expression pattern of type I in mouse. Eur J Biochem 1999, 259:660-669.
    • (1999) Eur J Biochem , vol.259 , pp. 660-669
    • Rus'd, A.A.1    Ikejiri, Y.2    Ono, H.3
  • 18
    • 0001940734 scopus 로고    scopus 로고
    • Peptidylarginine deiminase type I, type II, type III and type IV are expressed in rat epidermis
    • Ishigami A, Asaga H, Ohsawa T, Akiyama K, Maruyama N. Peptidylarginine deiminase type I, type II, type III and type IV are expressed in rat epidermis. Biomed Res 2001, 22:63-65.
    • (2001) Biomed Res , vol.22 , pp. 63-65
    • Ishigami, A.1    Asaga, H.2    Ohsawa, T.3    Akiyama, K.4    Maruyama, N.5
  • 19
    • 0037442843 scopus 로고    scopus 로고
    • CDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I
    • Guerrin M, Ishigami A, Mechin MC. cDNA cloning, gene organization and expression analysis of human peptidylarginine deiminase type I. Biochem J 2003, 370:167-174.
    • (2003) Biochem J , vol.370 , pp. 167-174
    • Guerrin, M.1    Ishigami, A.2    Mechin, M.C.3
  • 20
    • 0036406870 scopus 로고    scopus 로고
    • Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin
    • Ishigami A, Ohsawa T, Asaga H, Akiyama K, Kuramoto M, Maruyama N. Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin. Arch Biochem Biophys 2002, 407:25-31.
    • (2002) Arch Biochem Biophys , vol.407 , pp. 25-31
    • Ishigami, A.1    Ohsawa, T.2    Asaga, H.3    Akiyama, K.4    Kuramoto, M.5    Maruyama, N.6
  • 21
    • 0033749775 scopus 로고    scopus 로고
    • Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin
    • Kanno T, Kawada A, Yamanouchi J. Human peptidylarginine deiminase type III: molecular cloning and nucleotide sequence of the cDNA, properties of the recombinant enzyme, and immunohistochemical localization in human skin. J Invest Dermatol 2000, 115:813-823.
    • (2000) J Invest Dermatol , vol.115 , pp. 813-823
    • Kanno, T.1    Kawada, A.2    Yamanouchi, J.3
  • 22
    • 0033600723 scopus 로고    scopus 로고
    • Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3)
    • Nakashima K, Hagiwara T, Ishigami A. Molecular characterization of peptidylarginine deiminase in HL-60 cells induced by retinoic acid and 1alpha,25-dihydroxyvitamin D(3). J Biol Chem 1999, 274:27786-27792.
    • (1999) J Biol Chem , vol.274 , pp. 27786-27792
    • Nakashima, K.1    Hagiwara, T.2    Ishigami, A.3
  • 23
    • 1842829046 scopus 로고    scopus 로고
    • Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6
    • Chavanas S, Mechin MC, Takahara H. Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene 2004, 330:19-27.
    • (2004) Gene , vol.330 , pp. 19-27
    • Chavanas, S.1    Mechin, M.C.2    Takahara, H.3
  • 24
    • 0034968874 scopus 로고    scopus 로고
    • Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils
    • Asaga H, Nakashima K, Senshu T, Ishigami A, Yamada M. Immunocytochemical localization of peptidylarginine deiminase in human eosinophils and neutrophils. J Leukocyte Biol 2001, 70:46-51.
    • (2001) J Leukocyte Biol , vol.70 , pp. 46-51
    • Asaga, H.1    Nakashima, K.2    Senshu, T.3    Ishigami, A.4    Yamada, M.5
  • 25
    • 0020670580 scopus 로고
    • The growth and differentiation of cultured newborn rat keratinocytes
    • Baden HP, Kubilus J. The growth and differentiation of cultured newborn rat keratinocytes. J Invest Dermatol 1983, 80:124-130.
    • (1983) J Invest Dermatol , vol.80 , pp. 124-130
    • Baden, H.P.1    Kubilus, J.2
  • 26
    • 17744387366 scopus 로고    scopus 로고
    • Protein deimination and peptidylarginine deiminase expression during cornification of rat epidermal keratinocytes
    • Ishigami A, Asaga H, Ohsawa T, Akiyama K, Maruyama N. Protein deimination and peptidylarginine deiminase expression during cornification of rat epidermal keratinocytes. Biomed Res 2002, 23:145-151.
    • (2002) Biomed Res , vol.23 , pp. 145-151
    • Ishigami, A.1    Asaga, H.2    Ohsawa, T.3    Akiyama, K.4    Maruyama, N.5
  • 27
    • 0027443508 scopus 로고
    • Independent regulation of two cytoplasmic processing stages of the intermediate filament-associated protein filaggrin and role of Ca2+ in the second stage
    • Resing KA, al-Alawi N, Blomquist C, Fleckman P, Dale BA. Independent regulation of two cytoplasmic processing stages of the intermediate filament-associated protein filaggrin and role of Ca2+ in the second stage. J Biol Chem 1993, 268:25139-25145.
    • (1993) J Biol Chem , vol.268 , pp. 25139-25145
    • Resing, K.A.1    al-Alawi, N.2    Blomquist, C.3    Fleckman, P.4    Dale, B.A.5
  • 28
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller JN, Hanni KB, Markesbery WR. Impaired proteasome function in Alzheimer's disease. J Neurochem 2000, 75:436-439.
    • (2000) J Neurochem , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 29
    • 0034829801 scopus 로고    scopus 로고
    • The molecular bases of Alzheimer's disease and other neurodegenerative disorders
    • Maccioni RB, Munoz JP, Barbeito L. The molecular bases of Alzheimer's disease and other neurodegenerative disorders. Arch Med Res 2001, 32:367-381.
    • (2001) Arch Med Res , vol.32 , pp. 367-381
    • Maccioni, R.B.1    Munoz, J.P.2    Barbeito, L.3
  • 30
    • 0034480414 scopus 로고    scopus 로고
    • Protein deimination in the rat brain: generation of citrulline-containing proteins in cerebrum perfused with oxygen-deprived media
    • Asaga H, Ishigami A. Protein deimination in the rat brain: generation of citrulline-containing proteins in cerebrum perfused with oxygen-deprived media. Biomed Res 2000, 21:197-205.
    • (2000) Biomed Res , vol.21 , pp. 197-205
    • Asaga, H.1    Ishigami, A.2
  • 31
    • 0026544923 scopus 로고
    • Immunohistochemical localization of peptidylarginine deiminase in the rat brain
    • Vincent SR, Leung E, Watanabe K. Immunohistochemical localization of peptidylarginine deiminase in the rat brain. J Chem Neuroanat 1992, 5:159-168.
    • (1992) J Chem Neuroanat , vol.5 , pp. 159-168
    • Vincent, S.R.1    Leung, E.2    Watanabe, K.3
  • 32
    • 0035895702 scopus 로고    scopus 로고
    • Protein deimination in the rat brain after kainate administration: citrulline-containing proteins as a novel marker of neurodegeneration
    • Asaga H, Ishigami A. Protein deimination in the rat brain after kainate administration: citrulline-containing proteins as a novel marker of neurodegeneration. Neurosci Lett 2001, 299:5-8.
    • (2001) Neurosci Lett , vol.299 , pp. 5-8
    • Asaga, H.1    Ishigami, A.2
  • 33
    • 0037189068 scopus 로고    scopus 로고
    • Increased and type II-specific expression of peptidylarginine deiminase in activated microglia but not hyperplastic astrocytes following kainic acid-evoked neurodegeneration in the rat brain
    • Asaga H, Akiyama K, Ohsawa T, Ishigami A. Increased and type II-specific expression of peptidylarginine deiminase in activated microglia but not hyperplastic astrocytes following kainic acid-evoked neurodegeneration in the rat brain. Neurosci Lett 2002, 326:129-132.
    • (2002) Neurosci Lett , vol.326 , pp. 129-132
    • Asaga, H.1    Akiyama, K.2    Ohsawa, T.3    Ishigami, A.4
  • 34
    • 0032885575 scopus 로고    scopus 로고
    • Localization of peptidylarginine deiminase type II in a stage-specific immature oligodendrocyte from rat cerebral hemisphere
    • Akiyama K, Sakurai Y, Asou H, Senshu T. Localization of peptidylarginine deiminase type II in a stage-specific immature oligodendrocyte from rat cerebral hemisphere. Neurosci Lett 1999, 274:53-55.
    • (1999) Neurosci Lett , vol.274 , pp. 53-55
    • Akiyama, K.1    Sakurai, Y.2    Asou, H.3    Senshu, T.4
  • 35
    • 0026764429 scopus 로고
    • Detection of citrulline residues in deiminated proteins on polyvinylidene difluoride membrane
    • Senshu T, Sato T, Inoue T, Akiyama K, Asaga H. Detection of citrulline residues in deiminated proteins on polyvinylidene difluoride membrane. Anal Biochem 1992, 203:94-100.
    • (1992) Anal Biochem , vol.203 , pp. 94-100
    • Senshu, T.1    Sato, T.2    Inoue, T.3    Akiyama, K.4    Asaga, H.5
  • 36
    • 0027316375 scopus 로고
    • Combined biochemical and immunocytochemical analyses of postmortem protein deimination in the rat spinal cord
    • Asaga H, Senshu T. Combined biochemical and immunocytochemical analyses of postmortem protein deimination in the rat spinal cord. Cell Biol Int 1993, 17:525-532.
    • (1993) Cell Biol Int , vol.17 , pp. 525-532
    • Asaga, H.1    Senshu, T.2
  • 37
    • 0022616654 scopus 로고
    • Alzheimer's disease
    • Katzman R. Alzheimer's disease. N Engl J Med 1986, 314:964-973.
    • (1986) N Engl J Med , vol.314 , pp. 964-973
    • Katzman, R.1
  • 38
    • 0031614624 scopus 로고    scopus 로고
    • Alzheimer disease
    • Smith MA. Alzheimer disease. Int Rev Neurobiol 1998, 42:1-54.
    • (1998) Int Rev Neurobiol , vol.42 , pp. 1-54
    • Smith, M.A.1
  • 39
    • 0034465081 scopus 로고    scopus 로고
    • The hypoxic brain. Insights from ischemia research
    • Hossmann KA. The hypoxic brain. Insights from ischemia research. Adv Exp Med Biol 1999, 474:155-169.
    • (1999) Adv Exp Med Biol , vol.474 , pp. 155-169
    • Hossmann, K.A.1
  • 40
    • 0023753142 scopus 로고
    • Calcium-mediated neurotoxicity: relationship to specific channel types and role in ischemic damage
    • Choi DW. Calcium-mediated neurotoxicity: relationship to specific channel types and role in ischemic damage. Trends Neurosci 1988, 11:465-469.
    • (1988) Trends Neurosci , vol.11 , pp. 465-469
    • Choi, D.W.1
  • 41
    • 0026646278 scopus 로고
    • Extracellular calcium is a mediator of astroglial injury during combined glucose-oxygen deprivation
    • Haun SE, Murphy EJ, Bates CM, Horrocks LA. Extracellular calcium is a mediator of astroglial injury during combined glucose-oxygen deprivation. Brain Res 1992, 593:45-50.
    • (1992) Brain Res , vol.593 , pp. 45-50
    • Haun, S.E.1    Murphy, E.J.2    Bates, C.M.3    Horrocks, L.A.4


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