BIOMAT Database Logo BIOMAT Database Logo

The human choline acetyltransferase gene encodes two proteins. 1995

D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Department of Molecular and Cellular Pharmacology, University of Miami School of Medicine, FL 33101, USA.

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.

UI MeSH Term Description Entries
D007527 Isoenzymes Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics. Alloenzyme,Allozyme,Isoenzyme,Isozyme,Isozymes,Alloenzymes,Allozymes
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D009474 Neurons The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM. Nerve Cells,Cell, Nerve,Cells, Nerve,Nerve Cell,Neuron
D010275 Parasympathetic Nervous System The craniosacral division of the autonomic nervous system. The cell bodies of the parasympathetic preganglionic fibers are in brain stem nuclei and in the sacral spinal cord. They synapse in cranial autonomic ganglia or in terminal ganglia near target organs. The parasympathetic nervous system generally acts to conserve resources and restore homeostasis, often with effects reciprocal to the sympathetic nervous system. Nervous System, Parasympathetic,Nervous Systems, Parasympathetic,Parasympathetic Nervous Systems,System, Parasympathetic Nervous,Systems, Parasympathetic Nervous
D002795 Choline O-Acetyltransferase An enzyme that catalyzes the formation of acetylcholine from acetyl-CoA and choline. EC 2.3.1.6. Choline Acetylase,Choline Acetyltransferase,Acetylase, Choline,Acetyltransferase, Choline,Choline O Acetyltransferase,O-Acetyltransferase, Choline
D005796 Genes A category of nucleic acid sequences that function as units of heredity and which code for the basic instructions for the development, reproduction, and maintenance of organisms. Cistron,Gene,Genetic Materials,Cistrons,Genetic Material,Material, Genetic,Materials, Genetic
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D014176 Protein Biosynthesis The biosynthesis of PEPTIDES and PROTEINS on RIBOSOMES, directed by MESSENGER RNA, via TRANSFER RNA that is charged with standard proteinogenic AMINO ACIDS. Genetic Translation,Peptide Biosynthesis, Ribosomal,Protein Translation,Translation, Genetic,Protein Biosynthesis, Ribosomal,Protein Synthesis, Ribosomal,Ribosomal Peptide Biosynthesis,mRNA Translation,Biosynthesis, Protein,Biosynthesis, Ribosomal Peptide,Biosynthesis, Ribosomal Protein,Genetic Translations,Ribosomal Protein Biosynthesis,Ribosomal Protein Synthesis,Synthesis, Ribosomal Protein,Translation, Protein,Translation, mRNA,mRNA Translations

Related Publications

D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Two mRNAs are transcribed from the human gene for choline acetyltransferase.
October 1992, DNA and cell biology,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Transcriptional regulation of the human choline acetyltransferase gene.
January 1996, Progress in brain research,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Cyclic AMP regulation of the human choline acetyltransferase gene.
March 1993, Neurochemical research,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
The human cytomegalovirus UL35 gene encodes two proteins with different functions.
March 2002, Journal of virology,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Identification and analysis of the human choline acetyltransferase gene promoter.
March 1993, Neuroreport,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Human choline acetyltransferase gene: localization of alternative first exons.
March 1995, Journal of neuroscience research,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
The choline acetyltransferase of human placenta.
March 1966, The Biochemical journal,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Localization of the choline acetyltransferase (CHAT) gene to human chromosome 10.
February 1990, Genomics,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Human facial nucleus: choline acetyltransferase and calcitonin gene-related peptide.
December 1994, European archives of oto-rhino-laryngology : official journal of the European Federation of Oto-Rhino-Laryngological Societies (EUFOS) : affiliated with the German Society for Oto-Rhino-Laryngology - Head and Neck Surgery,
D D Grosman, and M V Lorenzi, and A C Trinidad, and W L Strauss
Coregulation of two embedded gene products, choline acetyltransferase and the vesicular acetylcholine transporter.
August 1995, Journal of neurochemistry,
Copied contents to your clipboard!