Hydrophobic protein that copurifies with human brain acetylcholinesterase: amino acid sequence, genomic organization, and chromosomal localization.

Abstract:

:The mechanism of attachment of acetylcholinesterase (AChE) to neuronal membranes in interneuronal synapses is poorly understood. We have isolated, sequenced, and cloned a hydrophobic protein that copurifies with AChE from human caudate nucleus and that we propose forms a part of a complex of membrane proteins attached to this enzyme. It is a short protein of 136 amino acids and has a molecular mass of 18 kDa. The sequence contains stretches of both hydrophobic and hydrophilic amino acids and two cysteine residues. Analysis of the genomic sequence reveals that the coding region is divided among five short exons. Fluorescence in situ hybridization localizes the gene to chromosome 6p21.32-p21.2. Northern blot analysis shows that this gene is widely expressed in the brain with an expression pattern that parallels that of AChE.

journal_name

J Neurochem

authors

Navaratnam DS,Fernando FS,Priddle JD,Giles K,Clegg SM,Pappin DJ,Craig I,Smith AD

doi

10.1046/j.1471-4159.2000.0742146.x

keywords:

subject

Has Abstract

pub_date

2000-05-01 00:00:00

pages

2146-53

issue

5

eissn

0022-3042

issn

1471-4159

journal_volume

74

pub_type

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