The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Alternative spliced variants of the alpha-methylacyl-CoA racemase gene and their expression in prostate cancer.

Alpha-methyacyl-CoA racemase (AMACR), a mitochondrial and peroxisomal enzyme essential in lipid metabolism, is overexpressed in prostate cancer. Two different AMACR transcripts (designated IA and IIA), each derived from five exons, have been reported. AMACR IA, the most abundant form, encodes a 382-amino acid protein (Mw 42 kDa, pI 6.07). AMACR IIA contains an alternative fifth exon that has extensive homology to the human fumarate hydratase (FH) and encodes a 288-amino acid protein (Mw 32 kDa, pI 9.6). Here we report additional variants of IA and IIA whereby the transcripts lack exon 3 and are designated as IB (Mw 22 kDa, pI 10.31) and IIB (Mw 31 kDa, pI 9.44). Due to a frameshift, the alternative fifth exon in the IIA transcript encodes a polypeptide that differs from FH. In contrast, the IIB transcript, generated as a result of the dual alternative splicing events, encodes a polypeptide homologous with a highly conserved region of FH. We also identified a shorter variant form of IIA (IIAs, Mw 28 kDa, pI 9.65), which lacks the 5' half of the alternative fifth exon. The carboxy termini of all five gene products differ as a result of the alternative splicing events. In prostate tumor tissues that overexpressed AMACR, both the A and B forms were overexpressed, suggesting coregulation. Only the predominant AMACR IA has an acidic pI and contains the previously identified peroxisomal targeting signal (PTS1) peptide, while the other four variants are basic proteins that lack the peroxisomal targeting signal peptide. These observations have implications for the cellular localization and function of these AMACR variants.[1]

References

 
WikiGenes - Universities