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Primary structure of acetylcholinesterase: implications for regulation and function.
Federation Proceedings
|December 1, 1986
Summary
Researchers isolated a Torpedo californica acetylcholinesterase (AChE) cDNA, revealing the full amino acid sequence. This sequence, characteristic of secreted proteins, shows homology to serine hydrolases and thyroglobulin.
Area of Science:
- Biochemistry
- Molecular Biology
- Neuroscience
Background:
- Acetylcholinesterase (AChE) is a crucial enzyme in neurotransmission.
- Understanding AChE's structure is key to its function and potential therapeutic targeting.
Purpose of the Study:
- To isolate and characterize the cDNA encoding Torpedo californica acetylcholinesterase (AChE).
- To deduce the complete amino acid sequence of the processed AChE protein.
- To investigate the molecular basis of AChE polymorphism.
Main Methods:
- cDNA isolation and sequencing from Torpedo californica.
- Amino acid sequence deduction from nucleotide sequence.
- Tryptic peptide mapping and sequencing for validation.
Main Results:
- The nucleotide sequence of AChE cDNA was determined, allowing deduction of the full 575-amino acid sequence.
- The deduced sequence includes a hydrophobic leader peptide and features characteristic of secreted globular proteins.
- Eight cysteines and four N-linked glycosylation sites were identified, with the active-site serine at residue 200.
- Sequence analysis revealed local homology to serine hydrolases and global homology to thyroglobulin.
Conclusions:
- The isolated cDNA corresponds to the mRNA for the 11 S form of AChE.
- The deduced amino acid sequence provides insights into AChE structure, including disulfide linkages and glycosylation.
- Further studies comparing different AChE forms and cDNA clones are needed to fully understand AChE polymorphism.