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J Biol Chem, Vol. 275, Issue 14, 10256-10264, April 7, 2000

A Novel Marker for Vertebrate Embryonic Heart, the EH-myomesin Isoform*

Irina AgarkovaDagger , Daniel Auerbach, Elisabeth Ehler, and Jean-Claude Perriard§

From the Institute of Cell Biology, ETH-Zürich Hönggerberg, CH-8093 Zürich, Switzerland

Myomesin is a structural component of the M-band that is expressed in all types of striated muscle. Its primary function may be the maintenance of the thick filament lattice and its anchoring to the elastic filament system composed of titin. Different myomesin isoforms have been described in chicken and mice, but no particular function has been assigned to them. Here we investigate the spatio-temporal expression pattern of myomesin isoforms by means of reverse transcriptase-polymerase chain reaction and isoform-specific antibodies. We find that two alternative splicing events give rise to four myomesin isoforms in chicken contrary to only one splicing event with two possible isoforms in mice. A splicing event at the C terminus results in two splice variants termed H-myomesin and S-myomesin, which represent the major myomesin species in heart and skeletal muscle of avian species, respectively. In contrast, in mammalian heart and skeletal muscle only S-myomesin is expressed. In embryonic heart of birds and mammals, alternative splicing in the central part of the molecule gives rise to the isoform that we termed EH-myomesin. It represents the major myomesin isoform at early embryonic stages of heart but is rapidly down-regulated around birth. Thus, the strict developmental regulation of the EH-myomesin makes it an ideally suited marker for embryonic heart.


* This work was supported in part by Swiss National Science Foundation Grant 31.52417/97.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF185573 and AF185572.

Dagger Supported by the Stipendienkommission of the ETH.

§ To whom correspondence should be addressed. Tel.: 0041-1-6333359; Fax 0041-1-6331069; E-mail jcp@cell.biol.ethz.ch.


Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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