| Autor: |
G. A. P. Bruns, Louis M. Kunkel, T. J. Byers, Joan H.M. Knoll, Alan H. Beggs, Frederick M. Boyce |
| Rok vydání: |
1992 |
| Předmět: |
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| Zdroj: |
Journal of Biological Chemistry. 267:9281-9288 |
| ISSN: |
0021-9258 |
| DOI: |
10.1016/s0021-9258(19)50420-3 |
| Popis: |
Conserved sequences of dystrophin, beta-spectrin, and alpha-actinin were used to plan a set of degenerate oligonucleotide primers with which we amplified a portion of a human alpha-actinin gene transcript. Using this short clone as a probe, we isolated and characterized full-length cDNA clones for two human alpha-actinin genes (ACTN2 and ACTN3). These genes encode proteins that are structurally similar to known alpha-actinins with approximately 80% amino acid identity to each other and to the previously characterized human nonmuscle gene. ACTN2 is the human homolog of a previously characterized chicken gene while ACTN3 represents a novel gene product. Northern blot analysis demonstrated that ACTN2 is expressed in both skeletal and cardiac muscle, but ACTN3 expression is limited to skeletal muscle. As with other muscle-specific isoforms, the EF-hand domains in ACTN2 and ACTN3 are predicted to be incapable of binding calcium, suggesting that actin binding is not calcium sensitive. ACTN2 was mapped to human chromosome 1q42-q43 and ACTN3 to 11q13-q14 by somatic cell hybrid panels and fluorescent in situ hybridization. These results demonstrate that some of the isoform diversity of alpha-actinins is the result of transcription from different genetic loci. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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