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Prion Proteinleri ve Etki Mekanizmaları

Yıl 2023, , 23 - 33, 17.12.2023
https://doi.org/10.57244/dfbd.1229717

Öz

Proteinler bir organizmanın yaşamsal faaliyetlerinin yerine getirilmesinde ve regülasyonunda çok önemli etkileri olan biyolojik moleküllerdir. Organizmanın genomu tarafından kodlanan proteinlerin işlevsel olabilmesi için posttranskripsiyonel olarak modifiye edilmeleri gerekmektedir. Bu modifikasyonlar sonucunda proteinin fonksiyon göstermesinde başlıca rol oynayan üç boyutlu bir konformasyona sahip olur. Organizmada bu protein katlanmaları bazı kontrol sistemleri tarafından kontrol edilmekte ve hatalı katlanmış olan proteinler bu degredasyon sistemi tarafından imha edilmektedir. Ancak bazı durumlarda bu hatalı katlanan proteinler degredasyona uğramazlar ve normal fonksiyonlarını yerine getiremeyip organizmada bir takım bozuklukların veya hastalıkların ortaya çıkmasına sebep olurlar. Prionlar, insanları ve hayvanları etkileyen ölmcül nörodejeneratif hastalıklar grubundadır. Bu hastalıkların önemli bir özelliği kendiliğinden çoğalıp bulaşabilen ve sadece proteinden meydana gelen hücresel prion proteini (PrPSc) ile ilişkili olmalarıdır. Memeli glikoproteinleri grubuna dahil olan PrPSc’ler genellikle glikozilfosfatidilinositol (GPI) aracılığıyla membrana bağlı olarak bulunan proteinlerdir. Prion proteinlerinin normal biyolojik fonksiyonları, hatalı katlanan prion proteinleri ile ilişkilendirilmiş hastalıklar ve bu hastalıkların tedavisinde kullanılan güncel terapiler bu derlemenin konusunu oluşturmaktadır.

Kaynakça

  • Ankara Üniversitesi Veterinerlik Fakültesi. (2017). veterinary.ankara.edu.tr/ fidanci/Ders_Notlari/AA-Proteinler.pdf (Erişim Tarihi:15.12. 2017).
  • Antony, H., Wiegmans, A. P., Wei, M. Q., Chernoff, Y. O., Khanna, K. K., & Munn, A. L. (2012). Potential roles for prions and protein-only inheritance in cancer. Cancer and Metastasis Reviews, 31, 1-19. doi: 10.1007/s10555-011-9325-9.
  • Benetti, F., & Legname, G. (2015). New insights into structural determinants of prion protein folding and stability. Prion, 9(2), 119-124. doi: 10.1080/19336896.2015.1022023.
  • Chakraborty, C., Nandi, S., & Jana, S. (2005). Prion disease: a deadly disease for protein misfolding. Current Pharmaceutical Biotechnology, 6(2), 167-177. doi: 10.2174/1389201053642321.
  • Chaudhuri, T. K., & Paul, S. (2006). Protein‐misfolding diseases and chaperone‐based therapeutic approaches. The FEBS journal, 273(7), 1331-1349. doi: 10.1111/j.1742-4658.2006.05181.x.
  • Grassmann, A., Wolf, H., Hofmann, J., Graham, J., & Vorberg, I. (2013). Cellular aspects of prion replication in vitro. Viruses, 5(1), 374-405.doi: 10.3390/v5010374.
  • Haltia, M. (2000). Human prion diseases. Annals of medicine, 32(7), 493-500. doi: 10.3109/07853890009002025.
  • Heinemann, V. (2005). Gemcitabine in metastatic breast cancer. Expert review of anticancer therapy, 5(3), 429-443. doi: 10.1586/14737140.5.3.429.
  • Holman, R. C., Belay, E. D., Christensen, K. Y., Maddox, R. A., Minino, A. M., Folkema, A. M., Haberling, D. L., Hammett, T. A., Kochanek, K. D., Sejvar, J. J., & Schonberger, L. B. (2010). Human prion diseases in the United States. PloS one, 5(1), e8521. doi: 10.1371/journal.pone.0008521.
  • Hosszu, L. L. P., Trevitt, C. R., Jones, S., Batchelor, M., Scott, D. J., Jackson, G. S., Collinge, J., Waltho, J. P., & Clarke, A. R. (2009). Conformational properties of beta-PrP. The Journal of biological chemistry, 284(33), 21981–21990. doi: 10.1074/jbc.M809173200.
  • Hüseyinoğlu, N. (2011). Bulașıcı süngerimsi ensefalopatiler: Halk sağlığı açısından güncel bir bakıș. Kafkas Tıp Bilimleri Dergisi, 1(1), 34-40. doi: 10.5505/kjms.2011.98608
  • Imran, M., & Mahmood, S. (2011). An overview of human prion diseases. Virology journal, 8, 559. doi: 10.1186/1743-422X-8-559
  • Jansen, C., Van Swieten, J. C., Capellari, S., Strammiello, R., Parchi, P., & Rozemuller, A. J. M. (2009). Inherited Creutzfeldt–Jakob disease in a Dutch patient with a novel five octapeptide repeat insertion and unusual cerebellar morphology. Journal of Neurology, Neurosurgery & Psychiatry, 80(12), 1386-1389. doi: 10.1136/jnnp.2008.169359.
  • Ji, H.F., & Zhang, H.Y. (2010). β-sheet constitution of prion proteins. Trends in biochemical sciences, 35(3), 129-134. doi: 10.1016/j.tibs.2009.12.002.
  • Kocabay, S., ve Geçkil, H., (2013). Ölümcül proteinler: prionlar, Science in school, 15 Ladogana, A., Puopolo, M., Croes, E. A., Budka, H., Jarius, C., Collins, S., Klug, G. M., Sutcliffe, T., Giulivi, A., Alperovitch, A., Delasnerie-Laupretre, N., Brandel, J. P., Poser, S., Kretzschmar, H., Rietveld, I., Mitrova, E., Cuesta, J.deP., Martinez-Martin, P., Glatzel, M., Aguzzi, A., … Zerr, I. (2005). Mortality from Creutzfeldt-Jakob disease and related disorders in Europe, Australia, and Canada. Neurology, 64(9), 1586–1591. doi: 10.1212/01.WNL.0000160117.56690.B2
  • Linden, R. (2017). The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules. Frontiers in molecular neuroscience, 10, 77. doi: 10.3389/fnmol.2017.00077
  • Lupi, O., & Peryassu, M. A. (2007). An emerging concept of prion infections as a form of transmissible cerebral amyloidosis. Prion, 1(4), 223–227. doi: 10.4161/pri.1.4.5816
  • Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P., & Wüthrich, K. (2005). Prion protein NMR structures of cats, dogs, pigs, and sheep. Proceedings of the National Academy of Sciences of the United States of America, 102(3), 640–645. doi: 10.1073/pnas.0408937102
  • Marijanovic, Z., Caputo, A., Campana, V., & Zurzolo, C. (2009). Identification of an intracellular site of prion conversion. PLoS pathogens, 5(5), e1000426. doi: 10.1371/journal.ppat.1000426
  • Mastrianni, J. A., & Roos, R. P. (2000). The prion diseases. Seminars in neurology, 20(3), 337–352. doi: 10.1055/s-2000-9396
  • Prusiner S. B. (1982). Novel proteinaceous infectious particles cause scrapie. Science (New York, N.Y.), 216(4542), 136–144. doi: 10.1126/science.6801762
  • Prusiner, S. B., Hadlow, W. J., Eklund, C. M., Race, R. E., & Cochran, S. P. (1978). Sedimentation characteristics of the scrapie agent from murine spleen and brain. Biochemistry, 17(23), 4987–4992. doi: 10.1021/bi00616a020
  • Scientific Research An Academic Publisher. (2017). http://file.scirp.org/Html/6-8201833_24987.html (Erişim Tarihi:15.12.2017)
  • Srivastava, A., Sharma, S., Sadanandan, S., Gupta, S., Singh, J., Gupta, S., Haridas, V., & Kundu, B. (2017). Modulation of prion polymerization and toxicity by rationally designed peptidomimetics. The Biochemical journal, 474(1), 123–147. doi: 10.1042/BCJ20160737
  • Stahl, N., Borchelt, D. R., Hsiao, K., & Prusiner, S. B. (1987). Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell, 51(2), 229–240. doi: 10.1016/0092-8674(87)90150-4
  • Şevik, M. (2014). Prion Hastalıkları Terapötik Yaklaşımları. Istanbul Medical Journal, 15(2)
  • Thackray, A. M., & Bujdoso, R. (2002). PrP(c) expression influences the establishment of herpes simplex virus type 1 latency. Journal of virology, 76(5), 2498–2509. doi: 10.1128/jvi.76.5.2498-2509.2002
  • The New York Times.(2017).https://www.nytimes.com/2016/11/23, (Erişim Tarihi:15.12.2017)
  • Van der Kamp, M. W., & Daggett, V. (2010). Influence of pH on the human prion protein: insights into the early steps of misfolding. Biophysical journal, 99(7), 2289–2298. doi: 10.1016/j.bpj.2010.07.063
  • Velayos, J. L., Irujo, A., Cuadrado-Tejedor, M., Paternain, B., Moleres, F. J., & Ferrer, V. (2010). Cellular prion protein in the central nervous system of mammals. Anatomoclinical associations. Neurología (English Edition), 25(4), 228-233. doi: 0.1016/S2173-5808(10)70046-8
  • Watts, J. C., & Westaway, D. (2007). The prion protein family: diversity, rivalry, and dysfunction. Biochimica et biophysica acta, 1772(6), 654–672. doi: 10.1016/j.bbadis.2007.05.001
  • Westergard, L., Christensen, H. M., & Harris, D. A. (2007). The cellular prion protein (PrP(C)): its physiological function and role in disease. Biochimica et biophysica acta, 1772(6), 629–644. doi: 10.1016/j.bbadis.2007.02.011
  • Wulf, M. A., Senatore, A., & Aguzzi, A. (2017). The biological function of the cellular prion protein: an update. BMC biology, 15(1), 34. doi:10.1186/s12915-017-0375-5
  • Yıldön, T. (2017). Prion, https://yildontanju.tr.gg/Prion.htm (Erişim Tarihi: 15.12.2017) Yılmaz, H., (2002). Prion Hastalıkları-Bulaşabilen Süngerimsi Ensefalopatiler. Ankem Dergisi, 16 (3): 161-166
  • Young, K., Jones, C. K., Piccardo, P., Lazzarini, A., Golbe, L. I., Zimmerman, T. R., Jr, Dickson, D. W., McLachlan, D. C., St George-Hyslop, P., & Lennox, A. (1995). Gerstmann-Sträussler-Scheinker disease with mutation at codon 102 and methionine at codon 129 of PRNP in previously unreported patients. Neurology, 45(6), 1127–1134. doi: 10.1212/wnl.45.6.1127
  • Zhou, X., Cai, J. G., Zhu, W. W., Zhao, H. Y., Wang, K., & Zhang, X. F. (2015). Boswellic acid attenuates asthma phenotype by downregulation of GATA3 via nhibition of PSTAT6. Genetics and molecular research : GMR, 14(3), 7463–7468. doi:10.4238/2015.July.3.22
Yıl 2023, , 23 - 33, 17.12.2023
https://doi.org/10.57244/dfbd.1229717

Öz

Kaynakça

  • Ankara Üniversitesi Veterinerlik Fakültesi. (2017). veterinary.ankara.edu.tr/ fidanci/Ders_Notlari/AA-Proteinler.pdf (Erişim Tarihi:15.12. 2017).
  • Antony, H., Wiegmans, A. P., Wei, M. Q., Chernoff, Y. O., Khanna, K. K., & Munn, A. L. (2012). Potential roles for prions and protein-only inheritance in cancer. Cancer and Metastasis Reviews, 31, 1-19. doi: 10.1007/s10555-011-9325-9.
  • Benetti, F., & Legname, G. (2015). New insights into structural determinants of prion protein folding and stability. Prion, 9(2), 119-124. doi: 10.1080/19336896.2015.1022023.
  • Chakraborty, C., Nandi, S., & Jana, S. (2005). Prion disease: a deadly disease for protein misfolding. Current Pharmaceutical Biotechnology, 6(2), 167-177. doi: 10.2174/1389201053642321.
  • Chaudhuri, T. K., & Paul, S. (2006). Protein‐misfolding diseases and chaperone‐based therapeutic approaches. The FEBS journal, 273(7), 1331-1349. doi: 10.1111/j.1742-4658.2006.05181.x.
  • Grassmann, A., Wolf, H., Hofmann, J., Graham, J., & Vorberg, I. (2013). Cellular aspects of prion replication in vitro. Viruses, 5(1), 374-405.doi: 10.3390/v5010374.
  • Haltia, M. (2000). Human prion diseases. Annals of medicine, 32(7), 493-500. doi: 10.3109/07853890009002025.
  • Heinemann, V. (2005). Gemcitabine in metastatic breast cancer. Expert review of anticancer therapy, 5(3), 429-443. doi: 10.1586/14737140.5.3.429.
  • Holman, R. C., Belay, E. D., Christensen, K. Y., Maddox, R. A., Minino, A. M., Folkema, A. M., Haberling, D. L., Hammett, T. A., Kochanek, K. D., Sejvar, J. J., & Schonberger, L. B. (2010). Human prion diseases in the United States. PloS one, 5(1), e8521. doi: 10.1371/journal.pone.0008521.
  • Hosszu, L. L. P., Trevitt, C. R., Jones, S., Batchelor, M., Scott, D. J., Jackson, G. S., Collinge, J., Waltho, J. P., & Clarke, A. R. (2009). Conformational properties of beta-PrP. The Journal of biological chemistry, 284(33), 21981–21990. doi: 10.1074/jbc.M809173200.
  • Hüseyinoğlu, N. (2011). Bulașıcı süngerimsi ensefalopatiler: Halk sağlığı açısından güncel bir bakıș. Kafkas Tıp Bilimleri Dergisi, 1(1), 34-40. doi: 10.5505/kjms.2011.98608
  • Imran, M., & Mahmood, S. (2011). An overview of human prion diseases. Virology journal, 8, 559. doi: 10.1186/1743-422X-8-559
  • Jansen, C., Van Swieten, J. C., Capellari, S., Strammiello, R., Parchi, P., & Rozemuller, A. J. M. (2009). Inherited Creutzfeldt–Jakob disease in a Dutch patient with a novel five octapeptide repeat insertion and unusual cerebellar morphology. Journal of Neurology, Neurosurgery & Psychiatry, 80(12), 1386-1389. doi: 10.1136/jnnp.2008.169359.
  • Ji, H.F., & Zhang, H.Y. (2010). β-sheet constitution of prion proteins. Trends in biochemical sciences, 35(3), 129-134. doi: 10.1016/j.tibs.2009.12.002.
  • Kocabay, S., ve Geçkil, H., (2013). Ölümcül proteinler: prionlar, Science in school, 15 Ladogana, A., Puopolo, M., Croes, E. A., Budka, H., Jarius, C., Collins, S., Klug, G. M., Sutcliffe, T., Giulivi, A., Alperovitch, A., Delasnerie-Laupretre, N., Brandel, J. P., Poser, S., Kretzschmar, H., Rietveld, I., Mitrova, E., Cuesta, J.deP., Martinez-Martin, P., Glatzel, M., Aguzzi, A., … Zerr, I. (2005). Mortality from Creutzfeldt-Jakob disease and related disorders in Europe, Australia, and Canada. Neurology, 64(9), 1586–1591. doi: 10.1212/01.WNL.0000160117.56690.B2
  • Linden, R. (2017). The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules. Frontiers in molecular neuroscience, 10, 77. doi: 10.3389/fnmol.2017.00077
  • Lupi, O., & Peryassu, M. A. (2007). An emerging concept of prion infections as a form of transmissible cerebral amyloidosis. Prion, 1(4), 223–227. doi: 10.4161/pri.1.4.5816
  • Lysek, D. A., Schorn, C., Nivon, L. G., Esteve-Moya, V., Christen, B., Calzolai, L., von Schroetter, C., Fiorito, F., Herrmann, T., Güntert, P., & Wüthrich, K. (2005). Prion protein NMR structures of cats, dogs, pigs, and sheep. Proceedings of the National Academy of Sciences of the United States of America, 102(3), 640–645. doi: 10.1073/pnas.0408937102
  • Marijanovic, Z., Caputo, A., Campana, V., & Zurzolo, C. (2009). Identification of an intracellular site of prion conversion. PLoS pathogens, 5(5), e1000426. doi: 10.1371/journal.ppat.1000426
  • Mastrianni, J. A., & Roos, R. P. (2000). The prion diseases. Seminars in neurology, 20(3), 337–352. doi: 10.1055/s-2000-9396
  • Prusiner S. B. (1982). Novel proteinaceous infectious particles cause scrapie. Science (New York, N.Y.), 216(4542), 136–144. doi: 10.1126/science.6801762
  • Prusiner, S. B., Hadlow, W. J., Eklund, C. M., Race, R. E., & Cochran, S. P. (1978). Sedimentation characteristics of the scrapie agent from murine spleen and brain. Biochemistry, 17(23), 4987–4992. doi: 10.1021/bi00616a020
  • Scientific Research An Academic Publisher. (2017). http://file.scirp.org/Html/6-8201833_24987.html (Erişim Tarihi:15.12.2017)
  • Srivastava, A., Sharma, S., Sadanandan, S., Gupta, S., Singh, J., Gupta, S., Haridas, V., & Kundu, B. (2017). Modulation of prion polymerization and toxicity by rationally designed peptidomimetics. The Biochemical journal, 474(1), 123–147. doi: 10.1042/BCJ20160737
  • Stahl, N., Borchelt, D. R., Hsiao, K., & Prusiner, S. B. (1987). Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell, 51(2), 229–240. doi: 10.1016/0092-8674(87)90150-4
  • Şevik, M. (2014). Prion Hastalıkları Terapötik Yaklaşımları. Istanbul Medical Journal, 15(2)
  • Thackray, A. M., & Bujdoso, R. (2002). PrP(c) expression influences the establishment of herpes simplex virus type 1 latency. Journal of virology, 76(5), 2498–2509. doi: 10.1128/jvi.76.5.2498-2509.2002
  • The New York Times.(2017).https://www.nytimes.com/2016/11/23, (Erişim Tarihi:15.12.2017)
  • Van der Kamp, M. W., & Daggett, V. (2010). Influence of pH on the human prion protein: insights into the early steps of misfolding. Biophysical journal, 99(7), 2289–2298. doi: 10.1016/j.bpj.2010.07.063
  • Velayos, J. L., Irujo, A., Cuadrado-Tejedor, M., Paternain, B., Moleres, F. J., & Ferrer, V. (2010). Cellular prion protein in the central nervous system of mammals. Anatomoclinical associations. Neurología (English Edition), 25(4), 228-233. doi: 0.1016/S2173-5808(10)70046-8
  • Watts, J. C., & Westaway, D. (2007). The prion protein family: diversity, rivalry, and dysfunction. Biochimica et biophysica acta, 1772(6), 654–672. doi: 10.1016/j.bbadis.2007.05.001
  • Westergard, L., Christensen, H. M., & Harris, D. A. (2007). The cellular prion protein (PrP(C)): its physiological function and role in disease. Biochimica et biophysica acta, 1772(6), 629–644. doi: 10.1016/j.bbadis.2007.02.011
  • Wulf, M. A., Senatore, A., & Aguzzi, A. (2017). The biological function of the cellular prion protein: an update. BMC biology, 15(1), 34. doi:10.1186/s12915-017-0375-5
  • Yıldön, T. (2017). Prion, https://yildontanju.tr.gg/Prion.htm (Erişim Tarihi: 15.12.2017) Yılmaz, H., (2002). Prion Hastalıkları-Bulaşabilen Süngerimsi Ensefalopatiler. Ankem Dergisi, 16 (3): 161-166
  • Young, K., Jones, C. K., Piccardo, P., Lazzarini, A., Golbe, L. I., Zimmerman, T. R., Jr, Dickson, D. W., McLachlan, D. C., St George-Hyslop, P., & Lennox, A. (1995). Gerstmann-Sträussler-Scheinker disease with mutation at codon 102 and methionine at codon 129 of PRNP in previously unreported patients. Neurology, 45(6), 1127–1134. doi: 10.1212/wnl.45.6.1127
  • Zhou, X., Cai, J. G., Zhu, W. W., Zhao, H. Y., Wang, K., & Zhang, X. F. (2015). Boswellic acid attenuates asthma phenotype by downregulation of GATA3 via nhibition of PSTAT6. Genetics and molecular research : GMR, 14(3), 7463–7468. doi:10.4238/2015.July.3.22
Toplam 36 adet kaynakça vardır.

Ayrıntılar

Birincil Dil Türkçe
Konular Mühendislik
Bölüm Makaleler
Yazarlar

Lütfiye Kadıoğlu Dalkılıç

Abdullah Aslan 0000-0002-6243-4221

Yayımlanma Tarihi 17 Aralık 2023
Gönderilme Tarihi 5 Ocak 2023
Yayımlandığı Sayı Yıl 2023

Kaynak Göster

APA Kadıoğlu Dalkılıç, L., & Aslan, A. (2023). Prion Proteinleri ve Etki Mekanizmaları. Doğu Fen Bilimleri Dergisi, 6(1), 23-33. https://doi.org/10.57244/dfbd.1229717