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The Human Choline Acetyltransferase Gene Encodes Two Proteins
Author(s) -
Grosman Daren D.,
Lorenzi Matthew V.,
Trinidad Alma C.,
Strauss William L.
Publication year - 1995
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1995.65020484.x
Subject(s) - choline acetyltransferase , nucleus basalis , microbiology and biotechnology , biology , biochemistry , acetylcholine , cholinergic neuron , endocrinology
Both, 2,500‐ and 6,000‐nucleotide (nt) mRNAs are generated by alternative splicing of the primary transcript from the human gene for choline acetyltransferase (ChAT), the 68‐kDa enzyme that synthesizes acetylcholine. In vitro translation of cRNA derived from a clone of the 2,500‐nt mRNA produced a protein with ChAT activity demonstrating that this transcript encodes the human ChAT enzyme. An antibody directed against a unique amino acid sequence predicted from the 6,000‐nt ChAT gene transcript identified a 27‐kDa protein on immunoblots of human nucleus basalis proteins. This protein was further shown to cross‐react with antibodies prepared against the 68‐kDa human ChAT enzyme. Gel‐filtration chromatography of human nucleus basalis proteins demonstrated that the 27‐kDa protein does not have ChAT activity, which eluted as a single peak coincident with that of the 68‐kDa enzyme. The 27‐kDa protein was, however, shown to colocalize with the ChAT enzyme in cholinergic neurons of the human spinal cord using immunohistochemical techniques.