메뉴 건너뛰기




Volumn 80, Issue 1, 2005, Pages 120-128

Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer's disease

Author keywords

Alzheimer's disease; Astrocyte; Citrulline; Glial fibrillary acidic protein; PAD; Vimentin

Indexed keywords

ANTIBODY; BRAIN EXTRACT; BRAIN PROTEIN; CALCIUM ION; CITRULLINATED PROTEIN; CITRULLINE; GLIAL FIBRILLARY ACIDIC PROTEIN; PEPTIDYLARGININE DEIMINASE 2; PROTEIN ARGININE DEIMINASE; UNCLASSIFIED DRUG; VIMENTIN;

EID: 20244368810     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/jnr.20431     Document Type: Article
Times cited : (216)

References (47)
  • 1
    • 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. 1999. Localization of peptidylarginine deiminase type II in a stage-specific immature oligodendrocyte from rat cerebral hemisphere. Neurosci Lett 274:53-55.
    • (1999) Neurosci Lett , vol.274 , pp. 53-55
    • Akiyama, K.1    Sakurai, Y.2    Asou, H.3    Senshu, T.4
  • 2
    • 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. 2000. Protein deimination in the rat brain: generation of citrulline-containing proteins in cerebrum perfused with oxygen-deprived media. Biomed Res 21:197-205.
    • (2000) Biomed Res , vol.21 , pp. 197-205
    • Asaga, H.1    Ishigami, A.2
  • 3
    • 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. 2001. Protein deimination in the rat brain after kainate administration: citrulline-containing proteins as a novel marker of neurodegeneration. Neurosci Lett 299:5-8.
    • (2001) Neurosci Lett , vol.299 , pp. 5-8
    • Asaga, H.1    Ishigami, A.2
  • 4
    • 0027316375 scopus 로고
    • Combined biochemical and immunocytochemical analyses of postmortem protein deimination in the rat spinal cord
    • Asaga H, Senshu T. 1993. Combined biochemical and immunocytochemical analyses of postmortem protein deimination in the rat spinal cord. Cell Biol Int 17:525-532.
    • (1993) Cell Biol Int , vol.17 , pp. 525-532
    • Asaga, H.1    Senshu, T.2
  • 5
    • 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. 2002. 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 326:129-132.
    • (2002) Neurosci Lett , vol.326 , pp. 129-132
    • Asaga, H.1    Akiyama, K.2    Ohsawa, T.3    Ishigami, A.4
  • 6
    • 0346770038 scopus 로고    scopus 로고
    • Age-related myelin breakdown: A developmental model of cognitive decline and Alzheimer's disease
    • Bartzokis G. 2004. Age-related myelin breakdown: a developmental model of cognitive decline and Alzheimer's disease. Neurobiol Aging 25: 5-18.
    • (2004) Neurobiol Aging , vol.25 , pp. 5-18
    • Bartzokis, G.1
  • 7
    • 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, Kawada A, Nachat R, Serre G, Simon M. 2004. Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6. Gene 330:19-27.
    • (2004) Gene , vol.330 , pp. 19-27
    • Chavanas, S.1    Mechin, M.C.2    Takahara, H.3    Kawada, A.4    Nachat, R.5    Serre, G.6    Simon, M.7
  • 8
    • 0023753142 scopus 로고
    • Calcium-mediated neurotoxicity: Relationship to specific channel types and role in ischemic damage
    • Choi DW. 1988. Calcium-mediated neurotoxicity: relationship to specific channel types and role in ischemic damage. Trends Neurosci 11:465-469.
    • (1988) Trends Neurosci , vol.11 , pp. 465-469
    • Choi, D.W.1
  • 10
    • 0026646278 scopus 로고
    • Extracellular calcium is a mediator of astroglial injury during combined glucose-oxygen deprivation
    • Haun SE, Murphy EJ, Bates CM, Horrocks LA. 1992. Extracellular calcium is a mediator of astroglial injury during combined glucose-oxygen deprivation. Brain Res 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
  • 11
    • 0034465081 scopus 로고    scopus 로고
    • The hypoxic brain. Insights from ischemia research
    • Hossmann KA. 1999. The hypoxic brain. Insights from ischemia research. Adv Exp Med Biol 474:155-169.
    • (1999) Adv Exp Med Biol , vol.474 , pp. 155-169
    • Hossmann, K.A.1
  • 12
    • 0028914527 scopus 로고
    • Studies of calcineurin-calmodulin interaction: Probing the role of arginine residues using peptidylarginine deiminase
    • Imparl JM, Senshu T, Graves DJ. 1995. Studies of calcineurin-calmodulin interaction: probing the role of arginine residues using peptidylarginine deiminase. Arch Biochem Biophys 318:370-377.
    • (1995) Arch Biochem Biophys , vol.318 , pp. 370-377
    • Imparl, J.M.1    Senshu, T.2    Graves, D.J.3
  • 13
    • 0024473081 scopus 로고
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain
    • 2+-dependent deimination-induced disassembly of intermediate filaments involves specific modification of the amino-terminal head domain. J Biol Chem 264:18119-18127.
    • (1989) J Biol Chem , vol.264 , pp. 18119-18127
    • Inagaki, M.1    Takahara, H.2    Nishi, Y.3    Sugawara, K.4    Sato, C.5
  • 14
    • 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. 1996. All-trans retinoic acid increases peptidylarginine deiminases in a newborn rat keratinocyte cell line. Biochem Biophys Res Commun 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
  • 15
    • 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. 1998. Molecular cloning of two novel types of peptidylarginine deiminase cDNAs from retinoic acid-treated culture of a newborn rat keratinocyte cell line. FEBS Lett 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
  • 16
    • 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. 2001. Peptidylarginine deiminase type I, type II, type III and type IV are expressed in rat epidermis. Biomed Res 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
  • 17
    • 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. 2002a. Protein deimination and peptidylarginine deiminase expression during cornification of rat epidermal keratinocytes. Biomed Res 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
  • 18
    • 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. 2002b. Human peptidylarginine deiminase type II: molecular cloning, gene organization, and expression in human skin. Arch Biochem Biophys 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
  • 19
    • 0022616654 scopus 로고
    • Alzheimer's disease
    • Katzman R. 1986. Alzheimer's disease. N Engl J Med 314:964-973.
    • (1986) N Engl J Med , vol.314 , pp. 964-973
    • Katzman, R.1
  • 20
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller JN, Hanni KB, Markesbery WR. 2000. Impaired proteasome function in Alzheimer's disease. J Neurochem 75:436-439.
    • (2000) J Neurochem , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 21
    • 0021114827 scopus 로고
    • Purification and properties of a brain enzyme which deiminates proteins
    • Kubilus J, Baden HP. 1983. Purification and properties of a brain enzyme which deiminates proteins. Biochim Biophys Acta 745:285-291.
    • (1983) Biochim Biophys Acta , vol.745 , pp. 285-291
    • Kubilus, J.1    Baden, H.P.2
  • 22
    • 0019161972 scopus 로고
    • Partial purification and specificity of an arginine-converting enzyme from bovine epidermis
    • Kubilus J, Waitkus RF, Baden HP. 1980. Partial purification and specificity of an arginine-converting enzyme from bovine epidermis. Biochim Biophys Acta 615:246-251.
    • (1980) Biochim Biophys Acta , vol.615 , pp. 246-251
    • Kubilus, J.1    Waitkus, R.F.2    Baden, H.P.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0027317616 scopus 로고
    • Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain
    • Lamensa JW, Moscarello MA. 1993. Deimination of human myelin basic protein by a peptidylarginine deiminase from bovine brain. J Neurochem 61:987-996.
    • (1993) J Neurochem , vol.61 , pp. 987-996
    • Lamensa, J.W.1    Moscarello, M.A.2
  • 26
    • 0034829801 scopus 로고    scopus 로고
    • The molecular bases of Alzheimer's disease and other neurodegenerative disorders
    • Maccioni RB, Munoz JP, Barbeito L. 2001. The molecular bases of Alzheimer's disease and other neurodegenerative disorders. Arch Med Res 32:367-381.
    • (2001) Arch Med Res , vol.32 , pp. 367-381
    • Maccioni, R.B.1    Munoz, J.P.2    Barbeito, L.3
  • 27
    • 0028342830 scopus 로고
    • Myelin in multiple sclerosis is developmentally immature
    • Moscarello MA, Wood DD, Ackerley C, Boulias C. 1994. Myelin in multiple sclerosis is developmentally immature. J Clin Invest 94:146-154.
    • (1994) J Clin Invest , vol.94 , pp. 146-154
    • Ma, M.1    Wood, D.D.2    Ackerley, C.3    Boulias, C.4
  • 28
    • 0036316687 scopus 로고    scopus 로고
    • Peptidylarginine deiminase: A candidate factor in demyelinating disease
    • Moscarello MA, Pritzker L, Mastronardi FG, Wood DD. 2002. Peptidylarginine deiminase: a candidate factor in demyelinating disease. J Neurochem 81:335-343.
    • (2002) J Neurochem , vol.81 , pp. 335-343
    • Moscarello, M.A.1    Pritzker, L.2    Mastronardi, F.G.3    Wood, D.D.4
  • 30
    • 0030681215 scopus 로고    scopus 로고
    • Consensus recommendations for the postmortem diagnosis of Alzheimer's disease
    • National Institute on Aging, and Reagan Institute Working Group on Diagnostic Criteria for the Neuropathological Assessment of Alzheimer's Disease. 1997. Consensus recommendations for the postmortem diagnosis of Alzheimer's disease. Neurobiol Aging 18:S1-S2.
    • (1997) Neurobiol Aging , vol.18
  • 31
    • 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. 1997. Isolation and molecular cloning of epidermal- and hair follicle-specific peptidylarginine deiminase (type III) from rat. J Biochem (Tokyo) 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
  • 32
    • 0346523446 scopus 로고    scopus 로고
    • Immunocytochemical localization of peptidylarginine deiminase type III, trichohyalin and deiminated trichohyalin in infant rat dorsal skin hair follicle
    • Ohsawa T, Ishigami A, Akiyama K, Asaga H. 2001. Immunocytochemical localization of peptidylarginine deiminase type III, trichohyalin and deiminated trichohyalin in infant rat dorsal skin hair follicle. Biomed Res 22:91-97.
    • (2001) Biomed Res , vol.22 , pp. 91-97
    • Ohsawa, T.1    Ishigami, A.2    Akiyama, K.3    Asaga, H.4
  • 33
    • 0011137031 scopus 로고
    • Content of citrulline and other amino acids in a protein of hair follicles
    • Rogers GE, Simmonds DH. 1958. Content of citrulline and other amino acids in a protein of hair follicles. Nature 182:186-187.
    • (1958) Nature , vol.182 , pp. 186-187
    • Rogers, G.E.1    Simmonds, D.H.2
  • 34
    • 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, Yonekawa T, Shiraiwa M, Kawada A, Takahara H. 1999. 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 259:660-669.
    • (1999) Eur J Biochem , vol.259 , pp. 660-669
    • Rus'D, A.A.1    Ikejiri, Y.2    Ono, H.3    Yonekawa, T.4    Shiraiwa, M.5    Kawada, A.6    Takahara, H.7
  • 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. 1992. Detection of citrulline residues in deiminated proteins on polyvinylidene difluoride membrane. Anal Biochem 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
    • 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. 1995. Detection of deiminated proteins in rat skin: probing with a monospecific antibody after modification of citrulline residues. J Invest Dermatol 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
  • 37
    • 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, Noniura K. 1999. 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 21:113-126.
    • (1999) J Dermatol Sci , vol.21 , pp. 113-126
    • Senshu, T.1    Akiyama, K.2    Ishigami, A.3    Noniura, K.4
  • 38
    • 0031614624 scopus 로고    scopus 로고
    • Alzheimer disease
    • Smith MA. 1998. Alzheimer disease. Int Rev Neurobiol 42:1-54.
    • (1998) Int Rev Neurobiol , vol.42 , pp. 1-54
    • Ma, S.1
  • 39
    • 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. 1996. Protein unfolding by peptidylarginine deiminase. Substrate specificity and structural relationships of the natural substrates trichohyalin and filaggrin. J Biol Chem 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
  • 40
    • 0025955772 scopus 로고
    • Three types of mouse peptidylarginine deiminase: Characterization and tissue distribution
    • Terakawa H, Takahara H, Sugawara K. 1991. Three types of mouse peptidylarginine deiminase: characterization and tissue distribution. J Biochem (Tokyo) 110:661-666.
    • (1991) J Biochem (Tokyo) , vol.110 , pp. 661-666
    • Terakawa, H.1    Takahara, H.2    Sugawara, K.3
  • 41
    • 0842287157 scopus 로고    scopus 로고
    • Relationships between arteriosclerosis, cerebral amyloid angiopathy and myelin loss from cerebral cortical white matter in Alzheimer's disease
    • Tian J, Shi J, Bailey K, Mann DM. 2004. Relationships between arteriosclerosis, cerebral amyloid angiopathy and myelin loss from cerebral cortical white matter in Alzheimer's disease. Neuropathol Appl Neurobiol 30:46-56.
    • (2004) Neuropathol Appl Neurobiol , vol.30 , pp. 46-56
    • Tian, J.1    Shi, J.2    Bailey, K.3    Mann, D.M.4
  • 42
    • 0031888451 scopus 로고    scopus 로고
    • TMIG-2DPAGE: A new concept of two-dimensional gel protein database for research on aging
    • Toda T, Kaji K, Kimura N 1998. TMIG-2DPAGE: a new concept of two-dimensional gel protein database for research on aging. Electrophoresis 19:344-348.
    • (1998) Electrophoresis , vol.19 , pp. 344-348
    • Toda, T.1    Kaji, K.2    Kimura, N.3
  • 43
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A 76:4350-4354.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 44
    • 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 enzymes mRNA in the estrous cycle
    • Tsuchida M, Takahara H, Minami N, Arai T, Kobayashi Y, Tsujimoto H, Fukazawa C, Sugawara K. 1993. 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 enzymes mRNA in the estrous cycle. Eur J Biochem 215:677-685.
    • (1993) Eur J Biochem , vol.215 , pp. 677-685
    • Tsuchida, M.1    Takahara, H.2    Minami, N.3    Arai, T.4    Kobayashi, Y.5    Tsujimoto, H.6    Fukazawa, C.7    Sugawara, K.8
  • 45
    • 0026544923 scopus 로고
    • Immunohistochemical localization of peptidylarginine deiminase in the rat brain
    • Vincent SR, Leung E, Watanabe K. 1992. Immunohistochemical localization of peptidylarginine deiminase in the rat brain. J Chem Neuroanat 5:159-168.
    • (1992) J Chem Neuroanat , vol.5 , pp. 159-168
    • Vincent, S.R.1    Leung, E.2    Watanabe, K.3
  • 46
    • 0024430819 scopus 로고
    • Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase
    • Watanabe K, Senshu T. 1989. Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase. J Biol Chem 264:15255-15260.
    • (1989) J Biol Chem , vol.264 , pp. 15255-15260
    • Watanabe, K.1    Senshu, T.2
  • 47
    • 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. 1988. Combined biochemical and immunochemical comparison of peptidylarginine deiminases present in various tissues. Biochim Biophys Acta 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.