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The Human Aromatic l ‐Amino Acid Decarboxylase Gene Can Be Alternatively Spliced To Generate Unique Protein Isoforms
Author(s) -
O'Malley Karen L.,
Harmon Steve,
Moffat Mark,
UhlandSmith Ann,
Wong Shou
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.1471-4159.1995.65062409.x
Subject(s) - aromatic l amino acid decarboxylase , gene isoform , alternative splicing , exon , biology , complementary dna , gene , microbiology and biotechnology , amino acid , tryptophan hydroxylase , biochemistry , transfection , rna splicing , protein isoform , serotonin , enzyme , rna , receptor , serotonergic
Aromatic l ‐amino acid decarboxylase (AADC) is expressed in a wide variety of tissues, including those where it is known to convert l ‐DOPA and 5‐hydroxytryptophan to dopamine and serotonin, respectively. AADC has been cloned from many species and shown to undergo alternative splicing within its 5′ untranslated region. Here, we report that the human AADC gene can undergo additional alternative splicing of exon 3, generating two different protein isoforms (termed AADC 480 and AADC 442 ). Both transcripts are widely expressed, with AADC 442 predominating in many neuronal and nonneuronal tissues. When homogenates were prepared from COS‐7 cells transfected with expression vectors containing either cDNA, AADC 480 catalyzed the decarboxylation of both l ‐DOPA and 5‐hydroxytryptophan. AADC 442 was inactive in either assay. These findings suggested that AADC 442 may have a different function in non‐monoamine‐expressing tissues. Taken together, these results suggest that the human AADC gene undergoes complex processing, leading to the formation of both tissue‐specific transcripts as well as unique protein isoforms.