МАРКЕРЫ ПРОЛИФЕРАЦИИ, ПРИМЕНЯЕМЫЕ В ГИСТОЛОГИЧЕСКИХИССЛЕДОВАНИЯХ



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Аннотация

В обзоре рассматриваются современные подходы к изучению пролиферативной активности клеток. В последние годы
были открыты ряд белков, участвующих в регуляции клеточного цикла, которые могут служить селективными маркерами
пролиферирующих клеток. В работе дана характеристика методов иммуноцитохимического выявления бромдезоксиуридина, белков PCNA, Ki-67, FEN-1, фосфорилированного гистона Н3 и циклинов; представлены сведения о роли этих белков
в регуляции клеточного цикла.

Об авторах

О В Кирик

Институт экспериментальной медициныСЗО РАМН

Email: olga_kirik@mail.ru
Отдел общей и частной морфологии (руков. - академик РАМН В.А. Нагорнев; Институт экспериментальной медициныСЗО РАМН

Г В Безнин

Институт экспериментальной медициныСЗО РАМН

Отдел общей и частной морфологии (руков. - академик РАМН В.А. Нагорнев; Институт экспериментальной медициныСЗО РАМН

Д Э Коржевский

Институт экспериментальной медициныСЗО РАМН

Отдел общей и частной морфологии (руков. - академик РАМН В.А. Нагорнев; Институт экспериментальной медициныСЗО РАМН

O V Kirik

G V Beznin

D E Korzhevskiy

Список литературы

  1. . Епифанова О.И., Терских В.В. и Захаров А.Ф. Радио автография. М., Высш. школа, 1977.
  2. Коржевский Д.Э. Пролиферативные зоны в эпителии сосудистых сплетений головного мозга эмбриона человека. Морфология, 1999, т. 115, вып. 3, с. 38-41.
  3. Коржевский Д.Э. Использование моноклональных антител к ядерному белку PCNA для выявления пролиферирующих клеток в развивающемся головном мозге эмбриона человека. Морфология, 2000, т. 118, вып. 5, с. 68-70.
  4. Омельченко Н.В., Коржевский Д.Э., Смирнов Е.Б. и Петрова Е.С. Ядрышковый аппарат пролиферирующих и дифференцирующихся клеток неокортекса эмбриона человека в период формирования кортикальной пластинки. Морфология, 1998, т. 113, вып. 2, с. 53-57.
  5. Упоров А.В. Активность пролиферации и ядрышковых организаторов клеток рака молочной железы как показатель биологического поведения опухоли: Автореф. дис. … канд. мед. наук. СПб., 1998.
  6. Упоров А.В., Цырлина Е.В., Семиглазов В.Ф. и Пожарисский К.М. Определение пролиферативной активности клеток рака молочной железы с использованием введения 5-бром-2ʹ-дезоксиуридина in vivo. Вопр. онкол., 1997, т. 43, с. 176-182.
  7. Barnes D.M. and Gillett C.E. Cyclin D1 in breast cancer. Breast Cancer Res. Treat., 1998, v. 52, № 1-3, p. 1-15.
  8. Bravo R., Fey S.J., Bellatin J. et al. Identification of a nuclear and of cytopeasmic polypeptide are whose relative proportion is sensitive to changes in the rate of cell proliferation. Exp. Cell. Res., 1981, v. 136, № 2, p. 311-319.
  9. Bravo R. and Macdonald-Bravo H. Changes in the nuclear distribution of cyclin (PCNA) but not its synthesis depend on DNA replication. EMBO J., 1985, v. 4, p. 655-661.
  10. Bravo R. and Macdonald-Bravo H. Existence of two populations of cyclin/proliferating cell nuclear antigen during the cell cycle: association with DNA replication sites. J. Cell Biol., 1987, v. 105, № 4, p. 1549-1554.
  11. Brooks D.J. and Garewal H.S. Measures of tumor proliferative activity. Int. J. Clin. Lab. Res., 1992, v. 22, № 4, p. 196-200.
  12. Buffo A., Rite I., Tripathi P. et al. Origin and progeny of reactive gliosis: a source of multipotent cells in the injured brain. Proc. Natl. Acad. Sci. USA, 2008, v. 105, № 9, p. 3581-3586.
  13. Bystron I., Molnar Z., Otellin V. and Blakemore C. Tangential networks of precocious neurons and early axonal outgrowth in the embryonic human forebrain. J. Neurosci., 2005, v. 25, p. 2781-2792.
  14. Celis J.E. and Madsen P. Increased nuclear cyclin/PCNA antigen staining of non S-phase transformed human amnion cells engaged in nucleotide excision DNA repair. FEBS Lett., 1986, v. 209, p. 277-283.
  15. Chen Y., Ai Y., Slevin J.R. et al. Progenitor proliferation in the adult hippocampus and substantia nigra induced by glial cell line-derived neurotrophic factor. Exp. Neurol., 2005, v. 196, № 1, p. 87-95.
  16. Cox L.S. Who binds wins: competition for PCNA rings out cellcycle changes. Trends Cell Biol., 1997, v. 7, № 12, p. 493-498.
  17. Duchrow M., Schl ter C. et al. Cell proliferation-associated nuclear antigen defined by antibody Ki-67: a new kind of cell cycle-maintaining proteins. Arch. Immunol. ther. Exp. (Warsz). 1995, v. 43, № 2, p. 117-121.
  18. Duchrow M., Schlüter C., Wohlenberg C. et al. Molecular characterization of the gene locus of the human cell proliferationassociated nuclear protein defined by monoclonal antibody Ki-67. Cell Prolif., 1996, v. 29, № 1, p. 1-12.
  19. Dyson M.H., Thomson S., Inagaki M. et al. MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10 or S28 via mitogen- and stress-activated kinase 1/2. Cell Sci., 2005, v. 118, Pt. 10, p. 2247-2259.
  20. Dyson M.H., Thomson S. and Mahadevan L.C. Heat shock, histone H3 phosphorylation and the cell cycle. Cell Cycle., 2005, v. 4, № 1, p. 13-17.
  21. Eberlin A., Grauffel C., Oulad-Abdelghani M. et al. Histone H3 tails containing dimethylated lysine and adjacent phosphorylated serine modifications adopt a specific conformation during mitosis and meiosis. Mol. Cell Biol., 2008, v. 28, № 5, p. 1739-1754.
  22. Gary R., Ludwig D.L., Cornelius H.L. et al. The DNA repair endonuclease XPR binds to proliferating cell nuclear antigen (PCNA) and shares sequence elements with the PCNA-binding region of FEN-1 and cyclin-dependent kinase inhibitor p21. J. Biol. Chem., 1997, v. 272, p. 24522-24529.
  23. Gerdes J., Li L., Schlueter C. et al. Immunobiochemical and molecular biologic characterization of the cell proliferationassociated nuclear antigen that is defined by monoclonal antibody Ki-67. Am. J. Pathol., 1991, v. 138, p. 867-873.
  24. Gerlach C., Golding M., Larue L. et al. Ki-67 immunoexpression is a robust marker of proliferative cells in the rat. Lab. Invest., 1997, v. 77, № 6, p. 697-698.
  25. Gerlach C., Sakkab D.Y., Scholzen T. et al. Ki-67 expression during rat liver regeneration after partial hepatectomy. Hepatology, 1997, v. 26, № 3, p. 573-578.
  26. Gorczyca W., Sarode V., Juan G. et al. Laser scanning cytometric analysis of cyclin B1 in primary human malignancies. Mol. Pathol., 1997, v. 10, № 5, p. 457-462.
  27. Goto H., Tomono Y., Ajiro K. et al. Identification of a novel phosphorylation site on histone H3 coupled with mitotic chromosome condensation. Biol. Chem., 1999, v. 274, № 36, p. 25543-25549.
  28. Gratzner H.G. Monoclonal antibody to 5-bromo- and 5-iododeoxyuridine: a new reagent for detection of DNA replication. Science, 1982, v. 218, № 4571, p. 474-475.
  29. Hans F. and Dimitrov S. Histone H3 phosphorylation and cell division. Oncogene, 2001, v. 20, № 24, p. 3021-3027.
  30. Hall P.A., Kearsey J.M., Coates P.J. et al. Characterization of the interaction between PCNA and Gadd45. Oncogene, 1995, v. 10, № 12, p. 2427-2433.
  31. Harrington J.J. and Lieber M.R. The characterization of a mammalian DNA structure-specific endonuclease. EMBO J., 1994, v. 13, p. 1235-1246.
  32. Hirata A., Inada K., Tsukamoto T. et al. Characterization of a monoclonal antibody, HTA28, recognizing a histone H3 phos phorylation site as a useful marker of M-phase cells. J. Histochem. Cytochem., 2004, v. 52, № 11, p. 1503-1509.
  33. Juan G., Traganos F., James W.M. et al. Histone H3 phosphorylation and expression of cyclins A and B1 measured in individual cells during their progression through G2 and mitosis. Cytometry, 1998, v. 32, № 2, p. 71-77.
  34. Kato J., Matsushime H., Hiebert S.W. et al. Direct binding of cyclin D to the retinoblastoma gene product (pRb) and pRb phosphorylation by the cyclin D-dependent kinase CDK4. Genes Dev., 1993, v. 7, № 3, p. 331-342.
  35. Kelman Z. PCNA: structure, functions and interactions. Oncogene, 1997, v. 14, № 6, p. 629-640.
  36. Kenny L.M., Vigushin D.M., Al-Nahhas A. et al. Quantification of cellular proliferation in turmor and normal tissue of patients with breast cancer by [18F]fluorothymidine-positron emission tomography imaging evaluation of analytical methods. Cancer Res., 2005, v. 65, p. 10104-10112.
  37. Key G., Petersen J.L., Becker M.H. et al. New antiserum against Ki-67 antigen suitable for double immunostaining of paraffin wax sections. J. Clin. Pathol., 1993, v. 46, № 12, p. 1080-1084.
  38. Kim K., Biade S. and Matsumoto Y. Involvement of flap endonuclease 1 in base excision DNA repair. J. Biol. Chem., 1998, v. 273, p. 8842-8848.
  39. Koburg E. and Maurer W. Autoradiographic studies with 3H-thymidine on the duration of desoxyribonucleic acid synthesis and its time lapse in the intestinal epithelium and other cell types in the mouse. Biochim. Biophys. Acta, 1962, v. 61, p. 229-242.
  40. Levin D.S., Bai W., Yao N. et al. An interaction between DNA ligase I and proliferating cell nuclear antigen: implications for Okazaki fragment synthesis and joining. Proc. Natl. Acad. Sci. USA, 1997, v. 94, p. 12862-12868.
  41. Li X., Li J., Harrington M.R. et al. Lagging strand DNA syntesis at the eucariotic replication fork involves binding and stimulation of FEN-1 by PCNA. J. Biol. Chem., 1995, v. 270, р. 22109-22112.
  42. Liu Y., Kao H.I. and Bambara R.A. Flap endonuclease 1: a central component of DNA metabolism. Annu. Rev. Biochem., 2004, v. 73, p. 589-615.
  43. Maga G., Villani G., Tillement V. et al. Okazaki fragment processing: modulation of the strand displacement activity of DNA polymerase delta by the concerted action of replication protein A, proliferating cell nuclear antigen, and flap endonuclease-1. Proc. Natl. Acad. Sci. USA, 2001, v. 98, p. 14298-14303.
  44. Matsuoka S., Yamaguchi M. and Matsukage A. D-type cyclinbinding regions of proliferating cell nuclear antigen. J. Biol. Chem., 1994, v. 269, № 15, p. 11030-11036.
  45. Matsushime H., Quelle D.E., Shurtleff S.A. et al. D-type cyclindependent kinase activity in mammalian cells. Mol. Cell Biol., 1994, v. 14, № 3, p. 2066-2076.
  46. McCallum D.E. and Hall P.A. Biochemical characterization of pKi67 with the identification of a mitotic-specific form associated with hyperphosphorylation and altered DNA binding. Exp Cell Res., 1999, v. 252, № 1, p. 186-198.
  47. McCormick D., Chong H., Hobbs C. et al. Detection of the Ki-67 antigen in fixed and wax-embedded sections with the monoclonal antibody MIB1. Histopathology, 1993, v. 22, № 4, p. 355-360.
  48. McGowan C.H. and Russell P. Cell cycle regulation of human WEE1. EMBO J., 1995, v. 14, p. 2166-2175.
  49. McKinley J.N., Knott K.K. and Thompson H.J. Effect of fixation and epitope retrieval on BrdU indices in mammary carcinomas. J. Histochem. Cytochem., 2000, v. 48, № 3, p. 355-362.
  50. Morgan D.O. Principes of CDK regulation. Nature, 1995, v. 374, p. 131-134.
  51. Nowak S.J. and Corces V.G. Phosphorylation of histone H3 correlates with transcriptionally active loci. Genes Dev., 2000, v. 14, № 23, p. 3003-3013.
  52. Payton M. and Coats S. Cyclin E2, the cycle continues. Int. J. Biochem. Cell Biol., 2002, v. 34, p. 315-320.
  53. Pines J. Cyclins and cyclin-dependent kinases: a biochemical view. Biochem., 1995, v. 308, p. 697-711.
  54. Prigent C. and Dimitrov S. Phosphorylation of serine 10 in histone H3, what for- J. Cell Sci., 2003, v. 116, 3677-3685.
  55. Quastler H. and Sherman F.G. Cell population kinetics in the intestinal epithelium of the mouse. Exp. Cell Res., 1959, v. 17, № 3, p. 420-438.
  56. Schurtenberger P., Egelhaaf S.U., Hindges R. et al. The solution structure of functionally active human proliferating cell nuclear antigen determined by small-angle neutron scattering. J. Mol. Biol., 1998, v. 275, № 1, p. 123-132.
  57. Seigneurin D. and Guillaud P. Ki-67 antigen, a cell cycle and tumor growth marker. Pathol. Biol., 1991, v. 39, № 10, p. 1020-1028.
  58. Shen B., Singh P., Liu R. et al. Multiple but dissectible functions of FEN-1 nucleases in nucleic acid processing, genome stability and diseases. Bioessays, 2005, v. 27, p. 717-729.
  59. Sherr C.J. G1 phase progression: cycling on cue. Cell, 1994, v. 79, № 4, p. 551-555.
  60. Smith M.L., Chen I.T., Zhan Q. et al. Interaction of the p53regulated protein Gadd45 with proliferating cell nuclear antigen. Science, 1994, v. 266, № 5189, P1376-1380.
  61. Spyratos F., Ferrero-Pous M., Trassard M. et al. Correlation between MIB-1 and other proliferation markers: clinical implication of the MIB-1 cutoff value. Cancer, 2002, v. 94, p. 2151-2159.
  62. Sramkoski R.M., Wormsley S.W., Bolton W.E. et al. Simultaneous detection of cyclin B1, p105, and DNA content provides complete cell cycle phase fraction analysis of cell that endoreduplicate. Cytometry, 1999, v. 35, № 3, p. 274-283.
  63. Stillman B. Cell cycle control of DNA replicaton. Science, 1996, v. 274, p. 1659-1664.
  64. Sutherland G.R. The role of nucleotides in human fragile site expression. Mutat. Res., 1988, v. 200, № 1-2, p. 207-213.
  65. Suurmejer A.J.H. and Boon M.E. Pretreatment in a high pressure microwave processor for MIB-1 immunostaining of cytological smears and paraffin tissue sections to visualize the various phases of the mitotic cycle. J. Histochem. Cytochem., 1999, v. 47, № 8, p. 1015-1020.
  66. Takasaki Y., Deng J.S. and Tan E.M. A nuclear antigen associated with cell proliferation and blast transformation. J. Exp. Med., 1981, v. 154, № 6, p. 1899-1909.
  67. Toschi L. and Bravo R. Changes in cyclin/proliferating cell nuclear antigen distribution during DNA repair synthesis. J. Cell Biol., 1988, v. 107, p. 1623-1628.
  68. Tough D.F. and Sprent J. Turnover of naive- and memory-phenotype T cells. J. Exp. Med., 1994, v. 179, № 4, p. 1127-1135.
  69. Turchi J.J., Huang L., Murante R.S. et al. Enzymatic completion of mammalian lagging-strand DNA replication. Proc. Natl. Acad. Sci. USA, 1994, v. 91, p. 9803-9807.
  70. Waga S., Bauer G. and Stillman B. Reconstitution of complete SV40 DNA replication with purified replication factors. J. Biol. Chem., 1994, v. 269, p. 10923-10934.
  71. Waga S., Hannon G.J., Beach D. and Stillman B. The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA. Nature, 1994, v. 369, p. 574-578.
  72. Wen Y., Yang S., Lui R. and Simpkins J.W. Cell-cycle regulators are involved in transient cerebral ischemia induced neuronal apoptosis in female rats. FEBS Lett., 2005, v. 579, № 21, p. 4591-4599.
  73. Xu F.M., Greenspan J.A. and Davidson R.L. Replicationdependent mutagenesis by 5-bromodeoxyuridine: identification of base change and sequence effects on mutability. Somat. Cell Mol. Genet., 1990, v. 16, № 5, p. 477-486.
  74. Yu C.C. and Filipe M.I. Update on proliferation-associated antibodies applicable to formalin-fixed paraffin-embedded tissue and their clinical applications. Histochem J., 1993, v. 25, № 12, p. 843-853.
  75. Yuzhakov A., Kelman Z., Hurwitz J. and O'Donnell M. Multiple competition reactions for RPA order the assembly of the DNA polymerase delta holoenzyme. EMBO J., 1999, v. 18, № 21, p. 6189-6199.

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