Key result
Targeted TPM1kappa inhibition disrupts myofibril structure and function in embryonic hearts.
Why the study?
A novel striated tropomyosin isoform TPM1kappa was recently discovered in hearts, but its functional role in myofibril organization was unclear.
The novel striated tropomyosin isoform TPM1kappa is essential for proper myofibril organization and function in embryonic hearts.
No immediate clinical implications from axolotl model; extends tropomyosin biology but leaves open human disease relevance.
Striated muscle tropomyosin (TM) is described as containing ten exons; 1a, 2b, 3, 4, 5, 6b, 7, 8, and 9a/b. Exon 9a/b has critical troponin binding domains and is found in striated muscle isoforms. We have recently discovered a smooth (exon 2a)/striated (exons 9a/b) isoform expressed in amphibian, avian, and mammalian hearts, designated as an isoform of the TPM1 gene (TPM1kappa). TPM1kappa expression was blocked in whole embryonic axolotl heart by transfection of exon-specific anti-sense oligonucleotide. Reverse transcriptase polymerase chain reaction (RT-PCR) confirmed lower transcript expression of TPM1kappa and in vitro analysis confirmed the specificity of the TPM1kappa anti-sense oligonucleotide. Altered expression of the novel TM isoform disrupted myofibril structure and function in embryonic hearts.
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Zajdel et al. (2005) studied Embryonic axolotl hearts. Exon-specific anti-sense oligonucleotide targeting TPM1kappa was evaluated on Myofibril structure and function. Anti-sense-mediated inhibition of the novel striated tropomyosin isoform TPM1kappa disrupted myofibril structure and function in embryonic axolotl hearts.
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