Роль сурвивина в патогенезе наружного генитального эндометриоза, современные возможности применения

Мишарина Е.В., Ярмолинская М.И., Иващенко Т.Э., Андреева Н.Ю. Роль сурвивина в патогенезе наружного генитального эндометриоза, современные возможности применения. Гинекология. 2020; 22 (6): 11–15. DOI: 10.26442/20795696.2020.6.200486

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Misharina E.V., Yarmolinskaya M.I., Ivashchenko T.E., Andreyeva N.Yu. The role of survivin in the pathogenesis of genital endometriosis, current application possibilities (literature review). Gynecology. 2020; 22 (6): 11–15. DOI: 10.26442/20795696.2020.6.200486

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Аннотация

В структуре гинекологических заболеваний генитальный эндометриоз занимает третье место, а его частота имеет тенденцию к увеличению. Эндометриоз встречается у 5–10% женщин репродуктивного возраста, у 35–50% пациенток с бесплодием и у 70–80% женщин с хроническими тазовыми болями. Частота самопроизвольного прерывания беременности при эндометриозе колеблется от 10 до 50%. Заслуживает внимания тот факт, что задержка с постановкой диагноза и началом лечения составляет от 5 до 10 лет. Недостатки хирургического лечения заключаются в высокой частоте рецидивов (до 50% через 5 лет от начала лечения). Гормональные методы лечения являются эффективными, но и они имеют серьезные побочные эффекты, которые ограничивают их долгосрочное применение. Естественно, что большая практическая и социальная значимость генитального эндометриоза индуцировала многочисленные исследования, посвященные изучению этиологии и патогенеза, которые, однако, до настоящего времени окончательно не выяснены. Широкая распространенность генитального эндометриоза диктует необходимость поиска и разработки новых эффективных методов диагностики и лечения. В статье представлены данные о сурвивине, который является одним из членов семейства ингибиторов апоптоза, кодируемых геном BIRC5. Сурвивин принимает участие в патогенезе эндометриоза и может быть одним из ранних маркеров заболевания. Апоптоз представляет собой важный последний этап, который определяет судьбу клетки. Принимая во внимание последние разработки в поисках таргетной терапии эндометриоза, антагонисты белков ингибитора апоптоза, в том числе сурвивин, рассматривают в качестве потенциальной мишени. Влияние на процессы программируемой гибели клеток может быть достаточно перспективным направлением в терапии эндометриоза. Цель данного обзора литературы – оценить значение экспрессии сурвивина в патогенезе и диагностике эндометриоза. Проанализировано 43 источника литературы (отечественных и зарубежных) с использованием различных баз данных (PubMed, PubMed central, Google Scholar, UpToDate).

Ключевые слова: эндометриоз, сурвивин, апоптоз.

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In the structure of gynecological diseases, genital endometriosis takes the third place, and its frequency tends to increase. Endometriosis occurs in 5–10% of women of reproductive age, in 35–50% of patients with infertility and in 70–80% of women with chronic pelvic pain. The frequency of spontaneous abortion in endometriosis ranges fr om 10 to 50%. Noteworthy is the fact that the delay in diagnosing and starting treatment is 5 to 10 years. The disadvantages of surgical treatment are the high relapse rate (up to 50% after 5 years from the start of treatment). Hormonal treatments are effective, but they also have serious side effects that lim it them in the long run. Naturally, the great practical and social importance of genital endometriosis induced numerous studies on the etiology and pathogenesis, which, however, have not yet been fully elucidated. The widespread prevalence of genital endometriosis necessitates the search and development of new effective methods of diagnosis and treatment. The article presents data on survivin, which is one of the members of the family of apoptosis inhibitors encoded by the BIRC5 gene. Survivin is involved in the pathogenesis of endometriosis and may be one of the early markers of the disease. Apoptosis is an important last step that determines the fate of the cell. Given recent developments in the search for targeted therapy for endometriosis, antagonists of apoptosis inhibitor proteins, including survivin, are considered as a potential target. Influence on the processes of programmed cell death can be a rather promising direction in the treatment of endometriosis. The purpose of this review is to evaluate the significance of surviving expression in the pathogenesis and diagnosis of endometriosis. 43 literature sources (domestic and foreign) were analyzed using various database (PubMed, PubMed central, Google Scholar, UpToDate).

Key words: endometriosis, survivin, apoptosis.

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Список литературы

1. Ярмолинская М.И., Айламазян Э.К. Генитальный эндометриоз. Различные грани проблемы. СПб.: Эко-Вектор, 2017.
[Yarmolinskaya M.I., Ailamazyan E.K. Genital endometriosis. Various facets of the problem. Saint Petersburg: Eco-Vector, 2017 (in Russian).]
2. Dohi T, Okada K, Xia F et al. An IAP-IAP complex inhibits apoptosis.
J Biol Chem 2004; 279 (33): 34087–90. DOI: 10.1074/jbc.C400236200
3. Aplin AE, Howe A, Alahari SK, Juliano RL. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol Rev 1998; 50 (2): 197–263. PMID: 9647866
4. Osuga Y. Novel therapeutic strategies for endometriosis: a pathophysiological perspective. Gynecol Obstet Invest 2008; 66 (Suppl. 1): 3–9. DOI: 10.1159/000148025
5. Kim SH, Ihm HJ, Oh YS et al. Increased nuclear expression of nuclear factor kappa-B p65 subunit in the eutopic endometrium and ovarian endometrioma of women with advanced stage endometriosis. Am J Reprod Immunol 2013; 70 (6): 497–508. DOI: 10.1111/aji.12161
6. Leyendecker G, Kunz G, Noe M et al. Endometriosis: a dysfunction and disease of the archimetra. Hum Reprod Update 1998; 4 (5): 752–62. DOI: 10.1093/humupd/4.5.752
7. Laudanski P, Charkiewicz R, Kuzmicki M et al. Profiling of selected angiogenesis-related genes in proliferative eutopic endometrium of women with endometriosis. Eur J Obstet Gynecol Reprod Biol 2014; 172: 85–92. DOI: 10.1016/j.ejogrb.2013.10.007
8. Gebel HM, Braun DP, Tambur A et al. Spontaneous apoptosis of endometrial tissue is impaired in women with endometriosis. Fertil Steril 1998; 69 (6): 1042–7. DOI: 10.1016/s0015-0282(98)00073-9
9. Shikone T, Yamoto M, Kokawa K et al. Apoptosis of human corpora lutea during cyclic luteal regression and early pregnancy. J Clin Endocrinol Metab 1996; 81 (6): 2376–80. DOI: 10.1210/jcem.81.6.8964880
10. Kokawa K, Shikone T, Nakano R. Apoptosis in the human uterine endometrium during the menstrual cycle. J Clin Endocrinol Metab 1996; 81 (11): 4144–7. DOI: 10.1210/jcem.81.11.8923873
11. Dmowski WP, Ding J, Shen J et al. Apoptosis in endometrial glandular and stromal cells in women with and without endometriosis. Hum Reprod 2001; 16 (9): 1802–8. DOI: 10.1093/humrep/16.9.1802
12. Jones RK, Searle RF, Bulmer JN. Apoptosis and bcl-2 expression in normal human endometrium, endometriosis and adenomyosis. Hum Reprod 1998; 13 (12): 3496–502. DOI: 10.1093/humrep/ 13.12.3496
13. Béliard A, Noël A, Foidart JM. Reduction of apoptosis and proliferation in endometriosis. Fertil Steril 2004; 82 (1): 80–5. DOI: 10.1016/j.fertnstert.2003.11.048
14. Vaskivuo TE, Stenbäck F, Karhumaa P et al. Apoptosis and apoptosis-related proteins in human endometrium. Mol Cell Endocrinol 2000; 165 (1–2): 75–83. DOI: 10.1016/s0303-7207(00)00261-6
15. Patel BG, Rudnicki M, Yu J et al. Progesterone resistance in endometriosis: origins, consequences and interventions. Acta Obstet Gynecol Scand 2017; 96 (6): 623–32. DOI: 10.1111/aogs.13156
16. Uegaki T, Taniguchi F, Nakamura K et al. Inhibitor of apoptosis proteins (IAPs) may be effective therapeutic targets for treating endometriosis. Hum Reprod 2015; 30 (1): 149–58. DOI: 10.1093/humrep/deu288
17. Londero AP, Calcagno A, Grassi T et al. Survivin, MMP-2, MT1-MMP, and TIMP-2: their impact on survival, implantation, and proliferation of endometriotic tissues. Virchows Arch 2012; 461 (5): 589–99. DOI: 10/1007/s00428-012-1301-4
18. Ambrosini G, Adida C, Altieri DC. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat Med 1997; 3 (8): 917–21. DOI: 10/1038/nm0897-917
19. Yamada Y, Kuroiva T, Nakagawa T et al. Transcriptional expression of survivin and its splice variants in brain tumors in humans. J Neurosurg 2003; 99 (4): 738–45. DOI: 10.1158/1535-7163 MCT-05-0375
20. Jung JE, Kim TK, Lee JS et al. Survivin inhibits anti-growth effect of p53 activated by aurora B. Biochem Biophis Res Commun 2005: 336 (4): 1164–71. DOI: 10.1016/j.bbrc.2005.08.235
21. Mita AC, Mita MM, Nawrocki ST et al. Survivin: key regulator Key regulator of mitosis and apoptosis and novel target for cancer therapeutics. Clin Cancer Res 2008; 14 (16): 5000–5. DOI: 10.1158/1078-0432.CCR-08-0746
22. Mityaev MV, Kopantzev EP, Buzdin AA et al. Functional significance of a putative sp 1 transcription factor binding site in the survivin gene promoter. Biochemistry 2008; 73 (11): 1183–91. DOI: 10.1134/s0006297908110035
23. Van Antwerp DJ, Martin SJ, Verma IM, Green DR. Inhibition of TNF-induced apoptosis by NF-kappa B. Trends Cell Biol 1998; 8 (3): 107–11. DOI: 10.1016/s0962-8924(97)01215-4
24. Zhao X, Laver T, Hong SW et al. An NF-kappaBp65-cIAP2 link is necessary for mediating resistance to TNF-alpha induced cell death in gliomas. J Neurooncol 2011; 102 (3): 367–81. DOI: 10.1007/s11060-010-0346-y
25. Zhang J, Lu Y, Pienta KJ. Multiple roles of chemokine (C-C motif) ligand 2 in promoting prostate cancer growth. J Natl Cancer Inst 2010; 102 (8): 522–8. DOI: 10/1093/jnci/djq044
26. Sommer KW, Schamberger CJ, Schmidt GE et al. Inhibitor of apoptosis protein (IAP) survivin is upregulated by oncogenic c-H-Ras. Oncogene 2003; 22 (27): 4266–80. DOI: 10/1158/1535-7163.MCT-05-0375
27. Vaira V, Lee CW, Goel HL et al. Regulation of survivin expression by IGF-1/mTOR signaling. Oncogene 2007; 26 (19): 2678–84. DOI: 10/1038/sj.onc.1210094
28. Wheatley SP, Alteri DC. Survivin at a glance. J Cell Sci 2019; 132 (7): 217–52. DOI: 10.1242/jcs.223826
29. Li F, Aljahbali L, Ling X. Cancer therapeutics using survivin BIRS5 as a target: what can we do after over two decades of study. J Clin Cancer Res 2019; 38 (368): 1–76. DOI: 10.1186/s13046-019-1362-1
30. Ghosh JC, Dohi T, Kang BH et al. Hsp60 regulation of tumor cell apoptosis. J Biol Chem 2008; 283 (8): 5188–94. DOI: 10.1074/jbc.M705904200
31. Tamm I, Wang Y, Sausville E et al. IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD 95). Bax, caspases, and antinuclear drugs. Cancer Res 1998; 58 (3): 5315–20. ID: 32783524
32. Sosaki T, Lopes MB, Hankins GR et al. Expression of survivin, an inhibitor of apoptosis protein, in tumors of the nervous system. Acta Neuropathol 2002; 194 (1): 105–9. DOI: 10.1007/s00401-002-0532-x
33. Kelly RJ, Lopez-Chavez A, Citrin D et al. Impacting tumor cell-fate by targeting the inhibitor of apoptosis protein survivin. Mol Cancer 2011; 10: 35. DOI: 10.1186/1476-4598-10-35
34. Pfister C, Ritz R, Endemann E et al. Evidence of ubiquitous in vivo and in vitro expression of pro-apoptotic Smac/DIABLO protein in meningioma cell lines. Oncol Rep 2009; 21 (5): 1181–8. DOI: 10/3892/or_00000339
35. Verhagen AM, Ekert PG, Pakusch M et al. Identification of DIABLO? A mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 2000; 102 (1): 575–85. DOI: 10/1016/s0092-8674(00)00009-x
36. Wang P, Zhen H, Zhang J et al. Survivin promotes glioma angiogenesis through vascular endothelial growth factor and basic fibroblast growth factor in vitro and in vivo. Mol Carcinog 2012; 51 (7): 586–95. DOI: 10/1002/mc.20829
37. Shi DG, Fan Y, Zhu F et al. Effect of RNA interference targeting-survivin on the invasiveness of human glioma cells in vitro. Nan Fang Yi Ke Da Xue Xue Bao 2009; 29 (6): 1156–58. PMID: 19726348.
38. Yin G, Zhu T, Zhao X et al. Decreased expression of surviving, estrogen and progesterone receptors in endometrial tissues after radiofrequency treatment of dysfunctional uterine bleeding. World J Surg Oncol 2012; 10 (100): 2–16. DOI: 10.1186/1477-7819-10-100
39. Acimovic M, Vidacovic S, Milic N et al. Survivin and VEGF as novel biomarkers in diagnosis of endometriosis. J Med Biochem 2016; 35 (1): 63–8. DOI: 10.1515/jomb-2015-0005
40. Fujino K, Ueda M, Takechara M et al. Transcriptional expression of survivin and its splice variants in endometriosis. Mol Hum Reprod 2006; 12 (6): 383–8. DOI: 10.1093/molhr/gal042
41. Watanabe A, Taniguchi F, Isawa M et al. The role of survivin in the resistance of endometriotic stromal cells to drug-induced apoptosis. Hum Reprod 2009; 24 (12): 3172–9. DOI: 10.1093/humrepp/dep305
42. Mabrouk M, Elmakky A, Carameli E et al. Performance of peripheral (serum and molecular) blood markers for diagnosis of endometriosis. Arch Gynecol Obstet 2012; 285 (5): 1307–12. DOI: 10.1007/s00404-011-2122-4
43. Fulda S, Vucic D. Targeting IAP proteins for therapeutic intervention in cancer. Nat Rev Drug Discov 2012; 11: 109. DOI: 10.1038/nrd3698

________________________________________________

1. Yarmolinskaya M.I., Ailamazyan E.K. Genital endometriosis. Various facets of the problem. Saint Petersburg: Eco-Vector, 2017 (in Russian).
2. Dohi T, Okada K, Xia F et al. An IAP-IAP complex inhibits apoptosis.
J Biol Chem 2004; 279 (33): 34087–90. DOI: 10.1074/jbc.C400236200
3. Aplin AE, Howe A, Alahari SK, Juliano RL. Signal transduction and signal modulation by cell adhesion receptors: the role of integrins, cadherins, immunoglobulin-cell adhesion molecules, and selectins. Pharmacol Rev 1998; 50 (2): 197–263. PMID: 9647866
4. Osuga Y. Novel therapeutic strategies for endometriosis: a pathophysiological perspective. Gynecol Obstet Invest 2008; 66 (Suppl. 1): 3–9. DOI: 10.1159/000148025
5. Kim SH, Ihm HJ, Oh YS et al. Increased nuclear expression of nuclear factor kappa-B p65 subunit in the eutopic endometrium and ovarian endometrioma of women with advanced stage endometriosis. Am J Reprod Immunol 2013; 70 (6): 497–508. DOI: 10.1111/aji.12161
6. Leyendecker G, Kunz G, Noe M et al. Endometriosis: a dysfunction and disease of the archimetra. Hum Reprod Update 1998; 4 (5): 752–62. DOI: 10.1093/humupd/4.5.752
7. Laudanski P, Charkiewicz R, Kuzmicki M et al. Profiling of selected angiogenesis-related genes in proliferative eutopic endometrium of women with endometriosis. Eur J Obstet Gynecol Reprod Biol 2014; 172: 85–92. DOI: 10.1016/j.ejogrb.2013.10.007
8. Gebel HM, Braun DP, Tambur A et al. Spontaneous apoptosis of endometrial tissue is impaired in women with endometriosis. Fertil Steril 1998; 69 (6): 1042–7. DOI: 10.1016/s0015-0282(98)00073-9
9. Shikone T, Yamoto M, Kokawa K et al. Apoptosis of human corpora lutea during cyclic luteal regression and early pregnancy. J Clin Endocrinol Metab 1996; 81 (6): 2376–80. DOI: 10.1210/jcem.81.6.8964880
10. Kokawa K, Shikone T, Nakano R. Apoptosis in the human uterine endometrium during the menstrual cycle. J Clin Endocrinol Metab 1996; 81 (11): 4144–7. DOI: 10.1210/jcem.81.11.8923873
11. Dmowski WP, Ding J, Shen J et al. Apoptosis in endometrial glandular and stromal cells in women with and without endometriosis. Hum Reprod 2001; 16 (9): 1802–8. DOI: 10.1093/humrep/16.9.1802
12. Jones RK, Searle RF, Bulmer JN. Apoptosis and bcl-2 expression in normal human endometrium, endometriosis and adenomyosis. Hum Reprod 1998; 13 (12): 3496–502. DOI: 10.1093/humrep/ 13.12.3496
13. Béliard A, Noël A, Foidart JM. Reduction of apoptosis and proliferation in endometriosis. Fertil Steril 2004; 82 (1): 80–5. DOI: 10.1016/j.fertnstert.2003.11.048
14. Vaskivuo TE, Stenbäck F, Karhumaa P et al. Apoptosis and apoptosis-related proteins in human endometrium. Mol Cell Endocrinol 2000; 165 (1–2): 75–83. DOI: 10.1016/s0303-7207(00)00261-6
15. Patel BG, Rudnicki M, Yu J et al. Progesterone resistance in endometriosis: origins, consequences and interventions. Acta Obstet Gynecol Scand 2017; 96 (6): 623–32. DOI: 10.1111/aogs.13156
16. Uegaki T, Taniguchi F, Nakamura K et al. Inhibitor of apoptosis proteins (IAPs) may be effective therapeutic targets for treating endometriosis. Hum Reprod 2015; 30 (1): 149–58. DOI: 10.1093/humrep/deu288
17. Londero AP, Calcagno A, Grassi T et al. Survivin, MMP-2, MT1-MMP, and TIMP-2: their impact on survival, implantation, and proliferation of endometriotic tissues. Virchows Arch 2012; 461 (5): 589–99. DOI: 10/1007/s00428-012-1301-4
18. Ambrosini G, Adida C, Altieri DC. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat Med 1997; 3 (8): 917–21. DOI: 10/1038/nm0897-917
19. Yamada Y, Kuroiva T, Nakagawa T et al. Transcriptional expression of survivin and its splice variants in brain tumors in humans. J Neurosurg 2003; 99 (4): 738–45. DOI: 10.1158/1535-7163 MCT-05-0375
20. Jung JE, Kim TK, Lee JS et al. Survivin inhibits anti-growth effect of p53 activated by aurora B. Biochem Biophis Res Commun 2005: 336 (4): 1164–71. DOI: 10.1016/j.bbrc.2005.08.235
21. Mita AC, Mita MM, Nawrocki ST et al. Survivin: key regulator Key regulator of mitosis and apoptosis and novel target for cancer therapeutics. Clin Cancer Res 2008; 14 (16): 5000–5. DOI: 10.1158/1078-0432.CCR-08-0746
22. Mityaev MV, Kopantzev EP, Buzdin AA et al. Functional significance of a putative sp 1 transcription factor binding site in the survivin gene promoter. Biochemistry 2008; 73 (11): 1183–91. DOI: 10.1134/s0006297908110035
23. Van Antwerp DJ, Martin SJ, Verma IM, Green DR. Inhibition of TNF-induced apoptosis by NF-kappa B. Trends Cell Biol 1998; 8 (3): 107–11. DOI: 10.1016/s0962-8924(97)01215-4
24. Zhao X, Laver T, Hong SW et al. An NF-kappaBp65-cIAP2 link is necessary for mediating resistance to TNF-alpha induced cell death in gliomas. J Neurooncol 2011; 102 (3): 367–81. DOI: 10.1007/s11060-010-0346-y
25. Zhang J, Lu Y, Pienta KJ. Multiple roles of chemokine (C-C motif) ligand 2 in promoting prostate cancer growth. J Natl Cancer Inst 2010; 102 (8): 522–8. DOI: 10/1093/jnci/djq044
26. Sommer KW, Schamberger CJ, Schmidt GE et al. Inhibitor of apoptosis protein (IAP) survivin is upregulated by oncogenic c-H-Ras. Oncogene 2003; 22 (27): 4266–80. DOI: 10/1158/1535-7163.MCT-05-0375
27. Vaira V, Lee CW, Goel HL et al. Regulation of survivin expression by IGF-1/mTOR signaling. Oncogene 2007; 26 (19): 2678–84. DOI: 10/1038/sj.onc.1210094
28. Wheatley SP, Alteri DC. Survivin at a glance. J Cell Sci 2019; 132 (7): 217–52. DOI: 10.1242/jcs.223826
29. Li F, Aljahbali L, Ling X. Cancer therapeutics using survivin BIRS5 as a target: what can we do after over two decades of study. J Clin Cancer Res 2019; 38 (368): 1–76. DOI: 10.1186/s13046-019-1362-1
30. Ghosh JC, Dohi T, Kang BH et al. Hsp60 regulation of tumor cell apoptosis. J Biol Chem 2008; 283 (8): 5188–94. DOI: 10.1074/jbc.M705904200
31. Tamm I, Wang Y, Sausville E et al. IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD 95). Bax, caspases, and antinuclear drugs. Cancer Res 1998; 58 (3): 5315–20. ID: 32783524
32. Sosaki T, Lopes MB, Hankins GR et al. Expression of survivin, an inhibitor of apoptosis protein, in tumors of the nervous system. Acta Neuropathol 2002; 194 (1): 105–9. DOI: 10.1007/s00401-002-0532-x
33. Kelly RJ, Lopez-Chavez A, Citrin D et al. Impacting tumor cell-fate by targeting the inhibitor of apoptosis protein survivin. Mol Cancer 2011; 10: 35. DOI: 10.1186/1476-4598-10-35
34. Pfister C, Ritz R, Endemann E et al. Evidence of ubiquitous in vivo and in vitro expression of pro-apoptotic Smac/DIABLO protein in meningioma cell lines. Oncol Rep 2009; 21 (5): 1181–8. DOI: 10/3892/or_00000339
35. Verhagen AM, Ekert PG, Pakusch M et al. Identification of DIABLO? A mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 2000; 102 (1): 575–85. DOI: 10/1016/s0092-8674(00)00009-x
36. Wang P, Zhen H, Zhang J et al. Survivin promotes glioma angiogenesis through vascular endothelial growth factor and basic fibroblast growth factor in vitro and in vivo. Mol Carcinog 2012; 51 (7): 586–95. DOI: 10/1002/mc.20829
37. Shi DG, Fan Y, Zhu F et al. Effect of RNA interference targeting-survivin on the invasiveness of human glioma cells in vitro. Nan Fang Yi Ke Da Xue Xue Bao 2009; 29 (6): 1156–58. PMID: 19726348.
38. Yin G, Zhu T, Zhao X et al. Decreased expression of surviving, estrogen and progesterone receptors in endometrial tissues after radiofrequency treatment of dysfunctional uterine bleeding. World J Surg Oncol 2012; 10 (100): 2–16. DOI: 10.1186/1477-7819-10-100
39. Acimovic M, Vidacovic S, Milic N et al. Survivin and VEGF as novel biomarkers in diagnosis of endometriosis. J Med Biochem 2016; 35 (1): 63–8. DOI: 10.1515/jomb-2015-0005
40. Fujino K, Ueda M, Takechara M et al. Transcriptional expression of survivin and its splice variants in endometriosis. Mol Hum Reprod 2006; 12 (6): 383–8. DOI: 10.1093/molhr/gal042
41. Watanabe A, Taniguchi F, Isawa M et al. The role of survivin in the resistance of endometriotic stromal cells to drug-induced apoptosis. Hum Reprod 2009; 24 (12): 3172–9. DOI: 10.1093/humrepp/dep305
42. Mabrouk M, Elmakky A, Carameli E et al. Performance of peripheral (serum and molecular) blood markers for diagnosis of endometriosis. Arch Gynecol Obstet 2012; 285 (5): 1307–12. DOI: 10.1007/s00404-011-2122-4
43. Fulda S, Vucic D. Targeting IAP proteins for therapeutic intervention in cancer. Nat Rev Drug Discov 2012; 11: 109. DOI: 10.1038/nrd3698

Авторы

Е.В. Мишарина*1, М.И. Ярмолинская1,2, Т.Э. Иващенко1, Н.Ю. Андреева1

1 ФГБНУ «Научно-исследовательский институт акушерства, гинекологии и репродуктологии им. Д.О. Отта», Санкт-Петербург, Россия;
2 ФГБОУ ВО «Северо-Западный государственный медицинский университет им. И.И. Мечникова» Минздрава России, Санкт-Петербург, Россия
*mishellena@gmail.com

________________________________________________

Elena V. Misharina*1, Maria I. Yarmolinskaya1,2, Tatiana E. Ivashchenko1, Nelly Yu. Andreyeva1

1 Ott Research Institute of Obstetrics, Gynecology and Reproductology, Saint Petersburg, Russiа;
2 Mechnikov North-Western State Medical University, Saint Petersburg, Russia
*mishellena@gmail.com

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