cfpdБюллетень физиологии и патологии дыханияBulletin Physiology and Pathology of Respiration1998-5029Дальневосточный научный центр физиологии и патологии дыханияcfpd-353Research ArticleСтатьиОЦЕНКА РОЛИ БЕЛКА HPS 70 В СИНЦИТИОТРОФОБЛАСТЕ ПЛАЦЕНТЫ ПРИ ОБОСТРЕНИИ ГЕРПЕС-ВИРУСНОЙ ИНФЕКЦИИ В ПЕРИОД ГЕСТАЦИИESTIMATION OF PROTEIN HPS 70 ROLE IN SYNCYTIOTROPHOBLAST OF PLACENTA AT EXACERBATION OF HERPES-VIRUS INFECTION DURING GESTATIONЛуценкоМихаил ТимофеевичLutsenkoMikhail T.Lucenkomt@mail.ruАндриевскаяИрина Анатольевнаcfpd@amur.ruДорофиенкоНиколай Николаевичcfpd@amur.ruДальневосточный научный центр физиологии и патологии дыхания Сибирского отделения РАМН, БлаговещенскFAR EASTERN SCIENCE CENTRE PHYSIOLOGY AND PATHOLOGY OF RESPIRATIONДальневосточный научный центр физиологии и патологии дыхания Сибирского отделения РАМН, БлаговещенскRussian Federation2011190220200391316Copyright © Луценко М.Т., Андриевская И.А., Дорофиенко Н.Н., 20202020Луценко М.Т., Андриевская И.А., Дорофиенко Н.Н.Lutsenko M.T., Андриевская И.А., Дорофиенко Н.Н.Данная работа распространяется под лицензией Creative Commons Attribution 4.0.This work is licensed under a Creative Commons Attribution 4.0 License.https://cfpd.elpub.ru/jour/article/view/353

Изучена роль белка теплового шока Hps 70 в гомогенатах плацент от женщин с герпесной инфекцией во время беременности и его влияние на структуру цитозоля и апоптоз ядер синцитиотрофобласта. Установлено уменьшение содержания Hps 70 в гомогенатах плацент от женщин с герпесной инфекцией во время беременности, нарушение структуры цитозоля (вакуолизация) и увеличение ядер синцитиотрофобласта в состоянии апоптоза.

The role of protein Hps 70 in homogenate of placentas from women with herpes infection during pregnancy and its influence on the structure of cytosol and syncytiotrophoblast nuclei apoptosis were studied. The decrease of protein Hps 70 in homogenate of placentas from women with herpes virus infection during pregnancy, the disorder of cytosol structure (vacuolization) and the increase of nuclei of syncytiotrophoblast in the state of apoptosis were revealed.

синцитиотрофобластвирус герпесабелок теплового шока 70апоптозsincytiotrophoblastherpes virusprotein Hps 70apoptosisReferencesПогорелов В.М., Козинец Г.И. Морфология апоптоза при нормальном и злокачественном гемопоэзе // Гематология и трансфузиология. 1995. Т.43, №5. С.21-24.Погорелов В.М., Козинец Г.И. Морфология апоптоза при нормальном и злокачественном гемопоэзе // Гематология и трансфузиология. 1995. Т.43, №5. С.21-24.Characterization of a lidless form of the molecular chaperone DnaK: DnaK'S lid inhibits transition to the low affinity state / Buczynski G. [et al.] // J. Biol. Chem. 2001, Vol. 276, Iss.29. P.27231-27236.Characterization of a lidless form of the molecular chaperone DnaK: DnaK'S lid inhibits transition to the low affinity state / Buczynski G. [et al.] // J. Biol. Chem. 2001, Vol. 276, Iss.29. P.27231-27236.A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma 32 / Gamer J. [et al.] // EMBO J. 1996. Vol.15. P.607-617.A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma 32 / Gamer J. [et al.] // EMBO J. 1996. Vol.15. P.607-617.Glover J.R., Lindquist S. Hps 104, Hps 70, Hps 40: a novel chaperone system that rescues previously aggregated proteins // Cell. 1998. Vol.94. P.73-82.Glover J.R., Lindquist S. Hps 104, Hps 70, Hps 40: a novel chaperone system that rescues previously aggregated proteins // Cell. 1998. Vol.94. P.73-82.Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperon net work / Goloubinoff P. [et al.] // Proc. Natl. Acad. Sci. USA. 1999. Vol.96. P.13732-13737.Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperon net work / Goloubinoff P. [et al.] // Proc. Natl. Acad. Sci. USA. 1999. Vol.96. P.13732-13737.Hps 70 exerts anti-apoptotic function downstream of caspase-3-like proteases/ Jaattela M. [et al.] // EMBO J. 1998. Vol.17. P.6124-6134.Hps 70 exerts anti-apoptotic function downstream of caspase-3-like proteases/ Jaattela M. [et al.] // EMBO J. 1998. Vol.17. P.6124-6134.Jaattela M. Escaping cell death: survival proteins in cancer // Exp. Cell. Res. 1999. Vol.248. P.30-34.Jaattela M. Escaping cell death: survival proteins in cancer // Exp. Cell. Res. 1999. Vol.248. P.30-34.Karzai A., McMacken R. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein // J. Biol. Chem. 1996. Vol.271. P.11236-11246.Karzai A., McMacken R. A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein // J. Biol. Chem. 1996. Vol.271. P.11236-11246.DnaJ proteins / Laufer T. [et al.] // Molecular Chaperones in proteins: structure, function and mode of action. New York: Fink A. and Goto Y. Marcel Dekker, 1998. P.241-274.DnaJ proteins / Laufer T. [et al.] // Molecular Chaperones in proteins: structure, function and mode of action. New York: Fink A. and Goto Y. Marcel Dekker, 1998. P.241-274.Heat shock resistence conferred by expression of human Hps 27 gene in rodent cells / Landry I. [et al.] // J. Cell. Biol. 1989. Vol.109. P. 715.Heat shock resistence conferred by expression of human Hps 27 gene in rodent cells / Landry I. [et al.] // J. Cell. Biol. 1989. Vol.109. P. 715.Lee G.J., Garrett J. Method for the expression of proteins in vitro translation systems with co expression of folding helper proteins // J. Biol. Chem. 1995. Vol.270. P.1042-1048.Lee G.J., Garrett J. Method for the expression of proteins in vitro translation systems with co expression of folding helper proteins // J. Biol. Chem. 1995. Vol.270. P.1042-1048.Multistep mechanism of substrate binding determines chaperone activity of Hps 70 / Mayer M.P. [et al.] // Nat. Struct. Biol. 2000. Vol.7. P.586-593.Multistep mechanism of substrate binding determines chaperone activity of Hps 70 / Mayer M.P. [et al.] // Nat. Struct. Biol. 2000. Vol.7. P.586-593.Mayer M.P., Bakau B. Hps 70 chaperones: cellular functions and molecular mechanism // Cell. Mol. Life Sci. 2005. Vol.62, №6. P.670-684.Mayer M.P., Bakau B. Hps 70 chaperones: cellular functions and molecular mechanism // Cell. Mol. Life Sci. 2005. Vol.62, №6. P.670-684.Heat-inactivated proteins are rescued by the DnaK. J-GrpE set and ClpB chaperones / Motohashi K. [et al.] // Proc. Natl. Acad. Sci. USA. 1999. Vol.96. P.7184-7189.Heat-inactivated proteins are rescued by the DnaK. J-GrpE set and ClpB chaperones / Motohashi K. [et al.] // Proc. Natl. Acad. Sci. USA. 1999. Vol.96. P.7184-7189.Structural insights into substrate binding by the molecular chaperone DnaK / Pelleechia M. [et al.] // Nat. Struct. Biol. 2000. Vol.7. P.289-303.Structural insights into substrate binding by the molecular chaperone DnaK / Pelleechia M. [et al.] // Nat. Struct. Biol. 2000. Vol.7. P.289-303.Pratt W.B. The role of the Hps 90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase // Annu. Rev. Pharmacol. Toxicol. 1997. Vol.37. P.297-326.Pratt W.B. The role of the Hps 90-based chaperone system in signal transduction by nuclear receptors and receptors signaling via MAP kinase // Annu. Rev. Pharmacol. Toxicol. 1997. Vol.37. P.297-326.Queitsch C., Sangster T.A., Lindquist S. Hps 90 as capacitor of phenotypic variation // Nature. 2002. Vol.417. P.618-624.Queitsch C., Sangster T.A., Lindquist S. Hps 90 as capacitor of phenotypic variation // Nature. 2002. Vol.417. P.618-624.Roger J., Frappier H., Walden D.B. Translation of some Maire Small Heat Shock Proteins is initiated from internal in-frame AuGs // Genetics Society of America. 1998. Vol.148. P.471-478.Roger J., Frappier H., Walden D.B. Translation of some Maire Small Heat Shock Proteins is initiated from internal in-frame AuGs // Genetics Society of America. 1998. Vol.148. P.471-478.Rutherford S., Lindquist S. Hps 90 as a capacitor for morphological evolution // Nature. 1998. Vol.396. P.336-342.Rutherford S., Lindquist S. Hps 90 as a capacitor for morphological evolution // Nature. 1998. Vol.396. P.336-342.Sakahira H., Nagata S. Co-translational folding of caspase-activated DNase with Hps 70, Hps 40 and inhibitor of caspase-activated DNase // J. Biol. Chem. 1998. Vol.277. P.3364-3370.Sakahira H., Nagata S. Co-translational folding of caspase-activated DNase with Hps 70, Hps 40 and inhibitor of caspase-activated DNase // J. Biol. Chem. 1998. Vol.277. P.3364-3370.Slepenkov S., Witt S. Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state // J. Biol. Chem.. 2002. Vol.41. P.12224-12235.Slepenkov S., Witt S. Kinetic analysis of interdomain coupling in a lidless variant of the molecular chaperone DnaK: DnaK's lid inhibits transition to the low affinity state // J. Biol. Chem.. 2002. Vol.41. P.12224-12235.

The authors declare that there are no conflicts of interest present.