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From protein to peptides: A spectrum of non-hydrolytic functions of acetylcholinesterase
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نویسنده
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halliday a.c. ,greenfield s.a.
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منبع
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protein and peptide letters - 2012 - دوره : 19 - شماره : 2 - صفحه:165 -172
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چکیده
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Acetylcholinesterase (ache),a member of the α/β-hydrolase fold superfamily of proteins,is a serine hydrolase responsible for the hydrolysis of the well studied neurotransmitter acetylcholine (ach). however,it is becoming clear that ache has a range of actions other than this 'classical' role. non-classical ache functions have been identified in apoptosis,stress-responses,neuritogenesis,and neurodegeneration. furthermore,these non-classical roles are attributable not only to the native protein,which appears to act as a mediary binding protein under a number of circumstances,but also to peptides cleaved from the parent protein. peptides cleaved from ache can act as independent signalling molecules. here we discuss the implications of non-hydrolytic functions of this multi-tasking protein. © 2012 bentham science publishers.
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کلیدواژه
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Acetylcholinesterase; Adhesion; Apoptosis; Neurogenesis; Non-hydrolytic function; Signalling peptide
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آدرس
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department of pharmacology,university of oxford,mansfield rd,oxford, United Kingdom, department of pharmacology,university of oxford,mansfield rd,oxford, United Kingdom
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Authors
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