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2007 | 12 | 4 |

Tytuł artykułu

Microglial expression of peptidylarginine deiminase 2 in the prenatal rat brain

Autorzy

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Peptidylarginine deiminases (PADs) are Ca2t+-dependant post-translational modification enzymes that catalyze the citrullination of protein arginyl residues. PAD type 2 (PAD2) is thought to be involved in some processes of neurodegeneration and myelination in the central nervous system. In this study, we found PAD2-positive cells in rat cerebra in 19-to 21-day old embryos, i.e. at a developmental stage well before myelination begins. Most of the cells were microglial marker-positive cells found mainly in the prospective medulla, and others were microglial marker-negative cells found mainly in the prospective dentate gyrus of the hippocampus. The former seemed to be in an activated state as judged by morphological criteria. The specificity of the enzyme activity, immunoblotting and reverse transcriptase-polymerase chain reaction analyses revealed that these cells expressed PAD2 and not PAD1, PAD3 or PAD4. Our data is indicative of microglial expression of PAD2 in the prenatal developing cerebrum.

Wydawca

-

Rocznik

Tom

12

Numer

4

Opis fizyczny

p.536-544,fig.,ref.

Twórcy

autor
  • Meiji University, Suginami-ku, Tokyo 168-8555, Japan
autor

Bibliografia

  • 1. Vossenaar, E.R., Zendman, A.J.W., van Venrooij, W.J. and Pruijn, G.J.M. PAD, a growing family of citrullinating enzymes: genes, features and involvement in disease. BioEssays 25 (2003) 1106-1118.
  • 2. György, B., Tóth, E., Tarcsa, E., Falus, A. and Buzás, E.I. Citrullination: a posttranslational modification in health and disease. Int. J. Biochem. Cell. Biol. 38 (2006) 1662-1677.
  • 3. Watanabe, K., Akiyama, K., Hikichi, K., Ohtsuka, R., Okuyama, A. and Senshu, T. Combined biochemical and immunochemical comparison of peptidylarginine deiminases present in various tissues. Biochim. Biophys. Acta 976 (1988) 375-383.
  • 4. Asaga, H. and Senshu, T. Combined biochemical and immunocytochemical analyses of postmortem protein deimination in the rat spinal cord. Cell Biol. Int. 17 (1993) 525-532.
  • 5. Asaga, H. and Ishigami, A. Protein deimination in the rat brain after kainate administration: citrulline-containing proteins as a novel marker of neurodegeneration. Neurosci. Lett. 299 (2001) 5-8.
  • 6. Ishigami, A., Asaga, H., Ohsawa, T., Akiyama, K. and Maruyama, N. Peptidylarginine deiminase type I, type II, type III and type IV are expressed in rat epidermis. Biomed. Res. 22 (2001) 63-65.
  • 7. Asaga, H. and Ishigami, A. Protein deimination in the rat brain: generation of citrulline-containing proteins in cerebrum perfused with oxygen-deprived media. Biomed. Res. 21 (2000) 197-205.
  • 8. Vincent, S.R., Leung, E., and Watanabe, K. Immunohistochemical localization of peptidylarginine deiminase in the rat brain. J. Chem. Neuroanat. 5 (1992) 159-168.
  • 9. Ishigami, A., Ohsawa, T., Hiratsuka, M., Taguchi H., Kobayashi, S., Saito, Y., Maruyama, S., Asaga, H., Toda, T., Kimura, N. and Mariyama, N. Abnormal accumulation of citrullinated proteins catalyzed by peptidylarginine deiminase in hippocampal extracts from patients with Alzheimer’s disease. J. Neurosci. Res. 80 (2005) 120-128.
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  • 11. Wood, D.D. and Moscarello, M.A. The isolation, characterization and lipidaggregating properties of a citrulline containing myelin basic protein. J. Biol. Chem. 264 (1989) 5121-5127.
  • 12. Akiyama, K., Sakurai, Y., Asou, H. and Senshu, T. Localization of peptidylarginine deiminase type II in a stage-specific immature oligodendrocyte from rat cerebral hemisphere. Neurosci. Lett. 274 (1999) 53-55.
  • 13. Pritzker, L.B., Nguyen, T.A. and Moscarello, M.A. The developmental expression and activity of peptidylarginine deiminase in the mouse. Neurosci. Lett. 266 (1999) 161-164.
  • 14. Pixley, S.K., Kobayashi, Y. and de Vellis, J. Monoclonal antibody to intermediate filament proteins in astrocytes. J. Neurosci. Res. 12 (1984) 525-541.
  • 15. Izant, J.G. and McIntosh, J.R. Microtubule-associated proteins: a monoclonal antibody to MAP2 binds to differentiated neurons. Proc. Natl. Acad. Sci. USA 77 (1980) 4741-4745.
  • 16. Streit, W.J. An improved staining method for rat microglial cells using the lectin from Griffonia simplicifolia (GSA I-B4). J. Histochem. Cytochem. 38 (1990) 1983-1686.
  • 17. Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 (1951) 265- 275.
  • 18. Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685.
  • 19. Ishigami, A., Kuramoto, M., Yamada, M., Watanabe, K. and 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. 433 (1998) 113-118.
  • 20. Watanabe, K. and Senshu, T. Isolation and characterization of cDNA clones encoding rat skeletal muscle peptidylarginine deiminase. J. Biol. Chem. 264 (1989) 15255-15260.
  • 21. Nishijyo, T., Kawada, A., Kanno, T., Shiraiwa, M. and Takahara, H. Isolation and molecular cloning of epidermal- and hair follicle-specific peptidylarginine deiminase (Type III) from rat. J. Biochem. 121 (1997) 868- 875.
  • 22. Tso, J.Y., Sun, X.H., Kao, T.H., Reece, K.S. and Wu, R. Isolation and characterization of rat and human glyceraldehyde-3-phosphate dehydrogenase cDNAs: genomic complexity and molecular evolution of the gene. Nucleic Acids Res. 13 (1985) 2485-2502.
  • 23. Asaga, H., Akiyama, K., Ohsawa, T. and Ishigami, A. Increased and type IIspecific expression of peptidylarginine deiminase in activated microglia but not hyperplastic astrocytes following kainic acid-evoked neurodegeneration in the rat brain. Neurosci. Lett. 326 (2002) 129-132.
  • 24. Joosten, E.A. and Gribnau, A.A. Astrocytes and guidance of outgrowing corticospinal tract axons in the rat. An immunocytochemical study using anti-vimentin and anti-glial fibrillary acidic protein. Neuroscience 31 (1989) 439-452.
  • 25. Wright, P.W., Bolling, L.C., Calvert, M.E., Sarmento, O.F., Berkeley, E.V., Shea, M.C., Hao, Z., Jayes, F.C., Bush, L.A., Shetty, J., Shore, A.N., Reddi, P.P., Tung, K.S., Samy, E., Allietta, M.M., Sherman, N.E., Herr, J.C. and Coonrod, S.A. ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets. Dev. Biol. 56 (2003) 73-88.
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Typ dokumentu

Bibliografia

Identyfikatory

Identyfikator YADDA

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