New approach to study of T cellular immunity development: Parallel investigation of lymphoid organ formation and changes in immune proteasome amount in rat early ontogenesis

Cellular Immunology

Volumn 256, Issue 1-2, 2009, Pages 47-55

  Sharova, Natalia P ^a   Zakharova, Liudmila A ^a   Astakhova, Tatiana M ^a   Karpova, Yaroslava D ^a   Melnikova, Victoria I ^a   Dmitrieva, Svetlana B ^a   Lyupina, Yulia V ^a   Erokhov, Pavel A ^a  

^a KOL TSOV INSTITUTE OF DEVELOPMENTAL BIOLOGY   (Russian Federation)

Author keywords

Embryonic and early postnatal development; Immune proteasomes; Periarterial lymphoid sheath; Rat spleen and liver; T cellular immunity; White pulp

Indexed keywords

PROTEASOME; PROTEIN LMP2; PROTEIN LMP7; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

ANIMAL EXPERIMENT; ARTICLE; B LYMPHOCYTE; CELLULAR IMMUNITY; CONTROLLED STUDY; EMBRYO; EMBRYO DEVELOPMENT; IMMUNOBLOTTING; IMMUNOFLUORESCENCE; IMMUNOHISTOCHEMISTRY; LIVER; LIVER CELL; LYMPHOID ORGAN; NONHUMAN; ONTOGENY; PERINATAL PERIOD; PRIORITY JOURNAL; PROTEIN LOCALIZATION; RAT; SPLEEN; SPLEEN CELL; T LYMPHOCYTE;

ANIMALS; CYSTEINE ENDOPEPTIDASES; EMBRYONIC DEVELOPMENT; FEMALE; IMMUNITY, CELLULAR; LIVER; LYMPHOID TISSUE; MULTIENZYME COMPLEXES; PREGNANCY; RATS; RATS, WISTAR; SPLEEN; T-LYMPHOCYTES; TISSUE DISTRIBUTION;

RATTUS;

EID: 61849168043     PISSN: 00088749     EISSN: 10902163     Source Type: Journal    
DOI: 10.1016/j.cellimm.2009.01.004     Document Type: Article

References (29)

1. Van Rees E.P., Dijkstra C.D., and Sminia T. Ontogeny of the rat immune system: an immunohistochemical approach. Dev. Comp. Immunol. 14 (1990) 9-18
2. Veerman A.J.P. The postnatal development of the white pulp in the rat spleen and the onset of immunocompetence against a thymus-independent and a thymus-dependent antigen. Z. Immun. Forsch. 150 (1975) 45-59
3. Rock K.L., and Goldberg A.L. Degradation of cell proteins and the generation of MHC class I-presented peptides. Annu. Rev. Immunol. 17 (1999) 739-779
4. Dahlmann B. Proteasomes. Essays Biochem. 41 (2005) 31-48
5. Strehl B., Seifert U., Kruger E., Heink S., Kuckelkorn U., and Kloetzel P.-M. Interferon-γ, the functional plasticity of the ubiquitin-proteasome system, and MHC class I antigen processing. Immunol. Rev. 207 (2005) 19-30
6. Unno M., Mizushima T., Morimoto Yu., Tomisugi Yo., Tanaka K., Yasuoka N., and Tsukihara T. The structure of the mammalian 20S proteasome at 2.75 Å resolution. Structure 10 (2002) 609-618
7. Cascio P., Hilton C., Kisselev A.F., Rock K.L., and Goldberg A.L. 26S proteasomes and immunoproteasomes produce mainly N-extended versions of an antigenic peptide. EMBO J. 20 (2001) 2357-2366
8. Goldberg A.L. Functions of the proteasome: from protein degradation and immune surveillance to cancer therapy. Biochem. Soc. Trans. 35 (2007) 12-17
9. Sharova N. Immune proteasomes and immunity. Ontogenez 37 (2006) 171-178
10. Khan S., van den Broek M., Schwarz K., de Giuli R., Diener P.A., and Groettrup M. Immunoproteasomes largely replace constitutive proteasomes during an antiviral and antibacterial immune response in the liver. J. Immunol. 167 (2001) 6859-6868
11. Heink S., Ludwig D., Kloetzel P.-M., and Kruger E. IFNγ-induced immune adaptation of the proteasome system is an accelerated and transient response. Proc. Natl. Acad. Sci. USA 102 (2005) 9241-9246
12. Chatterjee-Kishore M., Wright K.L., Ting J.P.Y., and Stark G.R. How Stat1 mediates constitutive gene expression: a complex of unphosphorylated Stat1 and IRF1 supports transcription of the LMP2 gene. EMBO J. 19 (2000) 4111-4122
13. Dahlmann B., Ruppert T., Kuehn L., Merforth S., and Kloetzel P.-M. Different proteasome subtypes in a single tissue exhibit different enzymatic properties. J. Mol. Biol. 303 (2000) 643-653
14. Noda C., Tanahashi N., Shimbara N., Hendil K.B., and Tanaka K. Tissue distribution of constitutive proteasomes, immunoproteasomes, and PA28 in rats. Biochem. Biophys. Res. Commun. 277 (2000) 348-354
15. Astakhova T.M., and Sharova N.P. Exclusion of immune proteasomes from mouse ascitic carcinoma Krebs-II cells. Izv. Acad. Nauk. Ser. Biol. 3 (2006) 275-283
16. Lowry O.H., Rosebrough N.J., Farr A.L., and Randall R.J. Protein measurement with the Folin reagent. J. Biol. Chem. 193 (1951) 265-275
17. A.J. Smolen, Image analytic techniques for quantification of immunohistochemical staining in the nervous system, in: P.M. Conn (Ed.), Methods in Neurosciences. Quantitative and Qualitative Microscopy, Academic Press, San Diego, 1990, pp. 208-229.
18. Frentzel S., Kuhn-Hartmann I., Gernold M., Gott P., Seelig A., and Kloetzel P.-M. The major-histocompatibility-complex-encoded beta-type proteasome subunits LMP2 and LMP7. Evidence that LMP2 and LMP7 are synthesized as proproteins and that cellular levels of both mRNA and LMP-containing 20S proteasomes are differentially regulated. Eur. J. Biochem. 216 (1993) 119-126
19. Groettrup M., Standera S., Stohwasser R., and Kloetzel P.-M. The subunits MECL-1 and LMP2 are mutually required for incorporation into the 20 S proteasome. Proc. Natl. Acad. Sci. USA 94 (1997) 8970-8975
20. Griffin T.A., Nandi D., Cruz M., Fehling H.J., van Kaer L., Monaco J.J., and Colbert A. Immunoproteasome assembly. Cooperative incorporation of interferon γ (IFN-γ)-inducible subunits. J. Exp. Med. 187 (1998) 97-104
21. Woollett G.R., Barclay A.N., Puklavec M., and Williams A.F. Molecular and antigenic heterogeneity of the rat leukocyte-common antigen from thymocytes and T and B lymphocytes. Eur. J. Immunol. 15 (1985) 168-173
22. Kurata M., Iidaka T., Hamada Y., and Horii I. Simultaneous measurement of nucleated cell counts and cellular differentials in rat bone marrow. Examination using flow cytometer. J. Toxicol. Sci. 32 (2007) 289-299
23. Fu Y.-X., and Chaplin D.D. Development and maturation of secondary lymphoid tissues. Annu. Rev. Immunol. 17 (1999) 399-433
24. Dullmann J., Feldhaus S., Van Damme E.J.M., Peumans W.J., and Schumacher U. Lectin histochemistry of the spleen: a new lectin visualizes the stromal architecture of white pulp and the sinuses of red pulp. J. Histochem. Cytochem. 48 (2000) 923-931
25. Caudill C., Jayarapu K., Elenich L., Monaco J.J., Colbert R.A., and Griffin T.A. T cells lacking immunoproteasome subunits MECL-1 and LMP7 hyperproliferate in response to polyclonal mitogens. J. Immunol. 176 (2006) 4075-4082
26. Douagi I., Colucci F., Di Santo J.P., and Cumano A. Identification of the earliest prethymic bipotent T/NK progenitor in murine fetal liver. Blood 99 (2002) 463-471
27. Ohteki T., Abo T., Seki S., Kobata T., Yagita H., Okumura K., and Kumagai K. Predominant appearance of γ/δ T lymphocytes in the liver of mice after birth. Eur. J. Immunol. 21 (1991) 1733-1740
28. Block T.M., Mehta A.S., Blumberg B.S., and Dwek R.A. Does rapid oligomerization of hepatitis B envelope proteins play a role in resistance to proteasome degradation and enhance chronicity?. DNA Cell Biol. 25 (2006) 165-170
29. Robek M.D., Garcia M.L., Boyd B.S., and Chisari F.V. Role of immuproteasome catalytic subunits in the immune response to hepatitis B virus. J. Virol. 81 (2007) 483-491