Abstract:
:Acetylcholinesterase (AChE) is likely to have roles other than the hydrolysis of acetylcholine, e.g., related to developmental processes like neurite outgrowth, differentiation and adhesion. Here, we investigated whether AChE can function as a heterophilic cell adhesion molecule and searched for proteins interacting with it. Using the yeast two-hybrid method and a mouse brain cDNA library, we have identified an interaction between a partial cDNA encoding the globular domain IV of laminin chain beta1 and the amino acids 240-503 of mouse AChE. Biochemical co-immunoprecipitation assays confirmed the genetic results. We suggest that AChE, by interacting with laminin-1, is able to exert changes in adhesion signaling pathways.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Paraoanu LE,Layer PGdoi
10.1016/j.febslet.2004.08.078keywords:
subject
Has Abstractpub_date
2004-10-08 00:00:00pages
161-4issue
1-2eissn
0014-5793issn
1873-3468pii
S0014579304011159journal_volume
576pub_type
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