Neurobiology of Disease Inhibition of FK506 Binding Proteins Reduces -Synuclein Aggregation and Parkinson’s Disease-Like Pathology

نویسندگان

  • Melanie Gerard
  • Angélique Deleersnijder
  • Veronique Daniëls
  • Sarah Schreurs
  • Sebastian Munck
  • Veerle Reumers
  • Hans Pottel
  • Yves Engelborghs
  • Chris Van den Haute
  • Jean-Marc Taymans
  • Zeger Debyser
  • Veerle Baekelandt
چکیده

Melanie Gerard,1,4 Angélique Deleersnijder,1,5 Veronique Daniëls,5 Sarah Schreurs,3 Sebastian Munck,6 Veerle Reumers,5 Hans Pottel,2 Yves Engelborghs,3 Chris Van den Haute,5 Jean-Marc Taymans,5 Zeger Debyser,1,4 and Veerle Baekelandt5 Laboratories of 1Biochemistry and 2Biophysics, Interdisciplinary Research Centre, Katholieke Universiteit Leuven-Kortrijk, B-8500 Kortrijk, Flanders, Belgium, 3Laboratory of Biomolecular Dynamics, Katholieke Universiteit Leuven, B-3001 Leuven, Flanders, Belgium, and Laboratories of 4Molecular Virology and Gene Therapy and 5Neurobiology and Gene Therapy and 6Flanders Institute for Biotechnology Department of Developmental and Molecular Genetics, Katholieke Universiteit Leuven, B-3000 Leuven, Flanders, Belgium

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Clioquinol-induced ordered conformational behavior in alpha-synuclein: promising relevance for therapeutic approach to Parkinson's disease

Parkinson?¦s disease (PD) is a devastating and an intricate complex neurological disorder that results from the progressive degeneration of nerve cells in Substantia nigra that controls movement. The pathological hallmark of PD is the formation of insoluble protein aggregates known as lewey bodies. Alpha-synuclein is the major constituent of these fibrillar structures. Alpha-synuclein a 140 ami...

متن کامل

Clioquinol-induced ordered conformational behavior in alpha-synuclein: promising relevance for therapeutic approach to Parkinson's disease

Parkinson?¦s disease (PD) is a devastating and an intricate complex neurological disorder that results from the progressive degeneration of nerve cells in Substantia nigra that controls movement. The pathological hallmark of PD is the formation of insoluble protein aggregates known as lewey bodies. Alpha-synuclein is the major constituent of these fibrillar structures. Alpha-synuclein a 140 ami...

متن کامل

Alpha-synuclein induced apoptosis and proliferation interacted with CD44 in human lymphocytes

Human ?-synuclein is a 140 amino acid protein with little or no secondary structure. The ?-synuclein is expressed at high levels in the brain and enriched in neural synaptic terminals but its physiological function remains largely unknown. More recently, ?-synuclein has been shown to be one of the principal componets of Lewy bodies, neuronal inclusions that are found in diverse human neurodegen...

متن کامل

Alpha-synuclein induced apoptosis and proliferation interacted with CD44 in human lymphocytes

Human ?-synuclein is a 140 amino acid protein with little or no secondary structure. The ?-synuclein is expressed at high levels in the brain and enriched in neural synaptic terminals but its physiological function remains largely unknown. More recently, ?-synuclein has been shown to be one of the principal componets of Lewy bodies, neuronal inclusions that are found in diverse human neurodegen...

متن کامل

Fk506&reduces&neuroinflammation&and&dopaminergic& Neurodegeneration&in&an&α8synuclein8based&rat&model&for& Parkinson's&disease.% Fk506 Reduces Neuroinflammation and Dopaminergic Neurodegeneration in an - Synuclein-based Rat Model for Parkinson's Disease Authors

Alpha-synuclein (-synuclein) is considered a key player in Parkinson's disease (PD), but the exact relationship between-synuclein aggregation and dopaminergic (DA) neurodegeneration remains unresolved. There is increasing evidence that neuroinflammatory processes are closely linked to DA cell death, but whether the inflammatory process is causally involved in PD or rather reflects secondary con...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2010