SavedAdd your journal

Journals / Manas Journal of Agriculture Veterinary and Life Sciences / 2016 / Cilt: 6 - Sayı: 1

Structure and Functions of Acetylcholinesterase and Acetylcholinesterase Inhibitory Activity of Plants

Asetilkolinesterazın Yapısı ve Fonksiyonları ve Bitkilerin Asetilkolinesteraz İnhibitör Etkileri

Fatma Gonca KOÇANCI
Belma ASLIM
Pages
19–35
Publication Date
2016-06-01
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

In this review will be informed about the structure, functions of AChE and AChEi from plants.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Alzheimer's disease (AD), defined as a neurodegenerative condition, are characterized by progressive loss of memory.
📊
Key Findings & Data:Cholinergic loss is one of the most important marker of the accurate diagnosis of AD.
💡
Conclusion & Impact:In this review will be informed about the structure, functions of AChE and AChEi from plants.
🔬Design:Review & Systematic Survey
📍Scope:Comprehensive Sample
⚙️Variables:Asetilkolinesteraz (AChE) · Alzheimer hastalığı · Biktisel asetilkolinesteraz inhibitörleri (AChEi’leri)

Abstract

Alzheimer's disease (AD), defined as a neurodegenerative condition, are characterized by progressive loss of memory. Cholinergic loss is one of the most important marker of the accurate diagnosis of AD. Acetylcholinesterase inhibitors (AChEi) is the most important group of drugs for AD. But none of the indentified AChEi’s were able to cure the disease. For this reason, studies on the particularly determination of agents that have preventive and therapeutic potential on the AD become an important research field. Researchers have also begun to work on the the discovery of curative and preventive effect of the substance for AD. In this review will be informed about the structure, functions of AChE and AChEi from plants.

Özet

Alzheimer Hastalığı (AH), hafızanın sürekli bir şekilde azalması ile karakterize edilen nörodejeneratif bir durumdur. AH’nin kesin tanısında en önemli belirteçlerden biri kolinerjik kayıptır. AH’ye yönelik en önemli ilaç grubu asetilkolinesteraz inhibitörleridir (AChEi). Fakat mevcut AChEi ilaçların hiçbirinde tam başarı elde edilememiştir. Bu sebeple, AH üzerinde etkili olacak koruyucu ve tedavi edici potansiyeli olan ajanların tespitene yönelik çalışmalar önem kazanmıştır. Bu derlemede AChE’nin yapısı, fonksiyonları ve AChEi bitkiler hakkında bilgi verilecektir

🔖

Cite This Article

KOÇANCI, F. G., ASLIM, B. (2016). Structure and Functions of Acetylcholinesterase and Acetylcholinesterase Inhibitory Activity of Plants. Manas Journal of Agriculture Veterinary and Life Sciences, Cilt: 6 - Sayı: 1, 19–35. https://ajindex.com/articles/789277

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (20)

  1. Shute CCD, Lewis PR, Brain. 90 (1967) 497-520.
  2. Semba K, Behav Brain Res 115 (2000) 117–141.
  3. Sulak O, Malas MA, Süleyman Demirel Üniversitesi Tıp Fakültesi Dergisi:9-( 3 ) (2002) 14 - 17. Tripathi A, Srivastava UC, Annals of Neurosciences 15, (2008) 4. Bear MF, Connors BW, Paradiso MA, Lippincott William & Wilkins, Baltimore, 22-49, (2001) 791-795.
  4. Erickson JD, Varoqui H, Schafer MK, Modi W, Diebler MF, Weihe E, Rand J, Eiden LE, Bonner TI and Usdin TB, J.Biol.Chem. 269, (1994) 21929-21932.
  5. Weihe E, TaoCheng JH, Schafer MK, Erickson JD and Eiden LE, Proc.Natl.Acad.Sci.U.S.A. 93, (1996) 3547- Serdaroğlu P, Deymeer F, Kas ve Nöromüsküler Kavşak Hastalıkları. Nöroloji Ders E-Kitabı, Öge, A.E. Baykan, B. Editörler, http://www.itfnoroloji.org/kas/kas.html (Son erişim tarihi: 15.02.2011)
  6. Thacker PD, Drug Discovery Today, 1: (2003) 8- 9. Pillay R, Maharaj DS, Daniel S, Daya S, Prog Neuropsychopharmacol Biol Psychiatry, 27: (2003) 61-64.
  7. Sussman JL, Hare M, Frolow F, Oefner C, Goldman A, Toker L, Silman I, Science 253: (1991) 872–9.
  8. Sussman JL, Harel M, Frolow F, Varon L, Toker L, Futerman AH, and Silman I, C. J. Mol. Biol. 203 (1988) -823. Taylor P, J. Biol. Chem, 266 (1991) 4025-4028.
  9. Ma JC, Dougherty DA, Chem. ReV, 97 (5): (1997) 1303-1324.
  10. Harel M, Schalkt I, Ehret-Sabatiert L, Bouett F, Goeldnert M, Hirtht C, Axelsen PH, Silmanii I, Sussman JL Proceedings of the National Academy of Sciences of the United States of America, 90 (19): (1993) 9031-9035.
  11. Wiesner J, Kriz Z, Kuca K, Jun D, Koča J, Journal of Enzyme Inhibition and Medicinal Chemistry, 22:4 (2007) -424. Dan C, Ya-fei P, Chuan-jun L, Yun-feng X, Yu-ren J, 978 (2012) 953-51.
  12. Schumacher M, Camp S, Maulet Y, Newton M, MacPhee-Quigley K,Taylor SS, Friedmann T, Taylor P, Nature (1986) 407-9.
  13. Guo L, Theses, Dissertations, Professional Papers (2008) 421. Botti SA, Felder CE, Sussman JL, Silman I, Protein Eng 11, (1998) 415–420.
  14. Scholl FG, Scheiffele P, Trends Neurosci, 26 (2003) 618–624.
  15. Sharma KV, Koenigsberger C, Brimijoin S, Bigbee JW, J Neurosci Res 63, (2001) 165–175.
  16. Anderson AA, Ushakov DS, Ferenczi MA, Saffel JL, J Cell Physiol (2007) doi:10.1002/ jcp.21288. Genever PG, Birch MA, Brown E, Skerry TM, Bone 24, (1999) 297–303.
  17. Inkson CA, Brabbs AC, Grewal TS, Skerry TM, Genever PG, Bone 35, (2004) 819–827.
  18. Layer PG, Weikert T, Alber R, Cell Tissue Res 273, (1993) 219–226.
  19. Layer PG, Sporns O, Proc Natl Acad Sci USA 84, (1987) 284–288.
  20. Koenigsberger C, Chiappa S, Brimijoin S, J Neurochem 69, (1997) 1389–139