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

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. 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. skeletal muscle myomesin heart myomesin embryonic heart-myomesin reverse transcriptase-polymerase chain reaction Hamburger-Hamilton stage phosphate-buffered saline base pair. Striated muscles are characterized by a very precise organization of contractile proteins into repeating structural subunits, the sarcomeres. A sarcomere is defined as the region between two Z-discs that anchor the thin (actin) filaments, with the thick (myosin) filaments being anchored in the center via a structure called the M-band. Elastic filaments composed of the giant protein titin stretch from the Z-disc to the M-band and may serve as a template for sarcomeric assembly and to maintain resting tension during the contraction cycle (for a review see Ref. 1.Gregorio C.C. Trombitas K. Centner T. Kolmerer B. Stier G. Kunke K. Suzuki K. Obermayr F. Herrmann B. Granzier H. Sorimachi H. Labeit S. J. 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Chem. 1984; 259: 13595-13604Abstract Full Text PDF PubMed Google Scholar). Many isoforms show a tissue and developmental stage-specific expression pattern (11.Sutherland C.J. Esser K.A. Elsom V.L. Gordon M.L. Hardeman E.C. Dev. Dyn. PubMed Scopus Google Scholar), but only a of the have been It has been that an component of the is expressed in several isoforms S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar, F. K. D. 1999; PubMed Scopus Google Scholar). Myomesin is in all of striated muscle and is to an in the of thick filaments with a its to proteins in M. K. D.O. J. PubMed Scopus Google Scholar). of in chicken heart have that myomesin in its pattern with the of the E. M. Perriard J.C. J. Cell Sci. 1999; 112: PubMed Google Scholar). that myomesin may be expressed in several isoforms from the that of chicken heart and skeletal muscle show of different Perriard J.C. J. Cell Biol. 1985; PubMed Scopus Google Scholar). two transcripts of different in chicken heart and skeletal muscle S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar). two isoforms only at C the major part of the which of a by a pattern of and is skeletal muscle isoform a of is to mammalian the heart isoform an at the C These isoforms as and H-myomesin are in Myomesin its structure with two M-band associated and proteins are and have a in 1999; PubMed Scopus Google Scholar). of myomesin is which described as a protein at the of the M-band in skeletal muscle J. Cell Biol. PubMed Scopus Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar). It has been that is splice of myomesin that is characterized by the of a between and F. K. D. 1999; PubMed Scopus Google Scholar). of as is in the of an avian to has been and the of myomesin isoform In to the of myomesin isoform diversity in we have the expression pattern of different myomesin isoforms in a of and isoform-specific antibodies. results that in chicken two alternative splicing events give rise to four myomesin in mammals, a splicing event to only two expression of the different isoforms is in a and developmental stage-specific In we have a myomesin isoform that is expressed during embryonic heart in which we have termed to and Dev. Dyn. 1992; PubMed Scopus Google Scholar). from the of the of the as embryonic from and of chicken and the system of with the system the by the of reverse by specific for different chicken myomesin isoforms from the chicken myomesin S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar). of all are in as and are are as and reverse are as and for the of the central of myomesin from the J. Biol. Chem. Full Text PDF PubMed Google Scholar) and are as reverse of by of specific for chicken and to the of in the of chicken myomesin from the S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar) and into the of the expression of chicken myomesin of the by from stage embryonic chicken into the and of and by the by and into the and of two and expressed in the and proteins from by and of the proteins by myomesin generated by either with the or the to the generated by with a to by A for all E. D. A Scholar). as and specific the and by and the of the characterized in C. Perriard J.C. J. Cell Biol. 1984; PubMed Scopus Google Scholar). from M. F. K. D.O. J. Cell Biol. 1996; PubMed Scopus Google Scholar) a of and as antibodies. and a of H. and skeletal from the by in a of and PubMed Scopus Google and for with of protein for the different tissue as by of a with in for at and in with and for with in reaction to the and and from chicken with in and as described A. D. J. Biol. Chem. Full Text PDF PubMed Google Scholar). with in and the with maintenance and the of and to the of the skeletal muscle the muscles of chicken in the of by a with a of with in chicken and with in for at with in for and in for with and in for primary and for at with for in and in as M. B. P. P. S. Perriard J.-C. PubMed Scopus Google Scholar). from at for from the into and to and Dev. Dyn. 1992; PubMed Scopus Google Scholar). an in in the in and at thick the a and the and as described with a microscope to a or system with an a the J.M. E. Perriard J.-C. PubMed Scopus Google Scholar). of the an microscope with an an the J. Mol. Biol. PubMed Scopus Google Scholar) at the for the with the a of C. C. of chicken and have been in the base with respectively. myomesin isoform transcripts are expressed in a and stage-specific we from chicken heart and skeletal muscles at different developmental stages the and in the of myomesin a from heart of different embryonic as as from stage and contrast, no in from stages of skeletal muscle or These results are with that the expression of isoform in chicken is to the heart S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar). we to isoform as the at the C a specific to the in the skeletal isoform of myomesin and in a of from heart and skeletal muscle and the of the from heart to be from the skeletal muscle the isoform transcript termed S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar) is expressed in types of striated muscle in but its expression level is in the heart. isoform is to as it is in chicken skeletal and the to the C terminus by alternative splicing is to as of and of myomesin has that alternative splicing of an between and gives rise to isoform that has been termed F. K. D. 1999; PubMed Scopus Google Scholar, J. Biol. Chem. Full Text PDF PubMed Google Scholar). no isoform been in chicken S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar) or myomesin U. K. Fürst D.O. J. Cell Sci. PubMed Google Scholar). we the and in and of which the we that the isoform the is only in chicken but that its expression is early embryonic stages a of to the transcript that the in and a of at stages of the to a myomesin isoform the between and as described S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar). In the of stage and in the by the In to the of the the and a stretch of that between and of chicken with the of F. K. D. 1999; PubMed Scopus Google Scholar) a and the of alternative splice in of chicken skeletal muscle of different stages the and rise to the only be from Thus, the between and is only in myomesin that is expressed in stages of chicken heart. We termed isoform it the In to investigate the expression of different myomesin isoforms in chicken at the protein we generated isoform-specific in of myomesin as the and at the C terminus of myomesin and the the and of the by of chicken tissue a protein with a of in of chicken heart and with of skeletal muscle a protein of in skeletal muscle but with heart the that of the S-myomesin isoform are in chicken no protein that expression of S-myomesin protein in the heart is to be by are a protein of in of embryonic chicken heart and with skeletal muscle of the myomesin isoforms by are in with the for and EH-myomesin S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar). that the expression of all myomesin isoforms is to striated muscle and that of the with muscle or tissue the by of chicken embryonic and skeletal muscle isoform-specific the M-band of the as by the with a sarcomeric which is in the Z-disc of the sarcomere with the M-band of embryonic chicken but an M-band is in skeletal muscle to a of the with S-myomesin which is to be in that the in skeletal muscle is to is by results no be in skeletal muscle. between the and the several of or four that in and that may to S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google expression of myomesin isoforms is in chicken of stage chicken with or with to sarcomeric and and to and the of the the of the skeletal muscle in the of the heart. the heart and no tissue and the the skeletal muscle and to a the heart the heart and with skeletal muscle or chicken skeletal We that is specific the results to an expression of S-myomesin in chicken heart with the very that the to be by in in with embryonic chicken but with embryonic chicken skeletal muscle These that all the myomesin isoforms in the M-band. In it be that in skeletal muscle only S-myomesin is all different isoforms are in embryonic sarcomeric is in Z-discs the it is possible to investigate of the myomesin isoforms is only in a of a by the of sarcomeric with that of the isoform-specific antibodies. of the two in that of the expression all isoform-specific the of all in Thus, as by all myomesin isoforms to be into the of the of the generated and the of we the of myomesin isoforms in during embryonic of stage chicken with isoform-specific in with sarcomeric and and of different myomesin isoforms be by the of heart and skeletal muscle and embryonic heart a the skeletal muscle tissue to a the heart in the in which the different types of striated muscles is with the sarcomeric or with These the from the and the of that in embryonic skeletal muscle only one myomesin isoform is all splice variants of myomesin be in the embryonic chicken heart. 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We two and but no specific the species have C that from in the of species, the which generated the of myomesin M. F. K. D.O. J. Cell Biol. 1996; PubMed Scopus Google Scholar), to be Despite the that the is between S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar), the myomesin in all muscle very in In heart and skeletal muscle of and the the same of as the which that species only the S-myomesin isoform in heart and skeletal in skeletal muscle of and the myomesin isoform in the heart of the generated the of myomesin with of species, we the in is to a splicing event or to a of Despite the that the to be the of myomesin the same from to mammalian results of that is a in myomesin isoform expression during embryonic heart In to that is the at the protein we chicken heart and skeletal muscle tissue of different developmental stages isoform-specific the we a of for H-myomesin in heart of different stages of In embryonic a and at it by a A in of S-myomesin is by the heart Thus, at early H-myomesin and S-myomesin are in the with the level of S-myomesin being the to be in to the for A of the from heart and skeletal that the expression level of S-myomesin in heart is at of in skeletal muscle In skeletal muscle S-myomesin is the only isoform expressed at developmental is no in with the at the early developmental the of the is to an of the of the of the S-myomesin only the H-myomesin the is the the of the with the and only a very be in the heart of and that the the H-myomesin as as the S-myomesin, the during early embryonic heart but that is at the of be with the in skeletal muscle at stage with the a to in the same heart but in skeletal muscle that only the H-myomesin but S-myomesin in the its expression is to be at the of the into the different myomesin to as to be for embryonic chicken heart. the EH-myomesin isoform is expressed in embryonic of mammalian species, we of different developmental stages by and In embryonic heart two with in and of myomesin and at the of and at stages and and be in skeletal muscles of that the is to the of the In embryonic heart a is by the and the and a of In as as in skeletal is the only isoform and isoform the it is by the Thus, we that the of an embryonic isoform of myomesin in termed is for avian as as for mammalian species and is a marker for embryonic heart. the base 4: PubMed Scopus Google Scholar) the of the we to one which from a of heart. that represents the of the is with the and chicken between the and and the chicken is and similarity with of the in a from a heart and for chicken and and that the expression of EH-myomesin serve as a marker for embryonic heart. spatio-temporal expression pattern of different myomesin isoforms in birds as as in and results that the myomesin isoform S-myomesin to be to the function of the myomesin it is the only myomesin isoform expressed in striated muscle of mammals, and in avian skeletal muscle. at the C terminus gives rise to H-myomesin which represents the major myomesin species in avian muscle. of the in the central part of the myomesin molecule to the EH-myomesin which is for the embryonic heart of and We find that the splice H-myomesin is expressed in of all isoform has a and with the that S-myomesin in skeletal muscle from the same the with with the the primary of the is between different avian species, but the heart of the splice and the We that the of the or of myomesin in avian muscle that are in the primary A in the of the myomesin to the a M. K. D.O. J. PubMed Scopus Google Scholar, D. S. Keller S. Leu M. Ehler E. Perriard J.C. Mol. Biol. 1999; PubMed Scopus Google Scholar), but at the same its from one species to S. Keller S. Haussmann I. Auerbach D. Perriard E. Muhlebach S. Perriard J.-C. J. Biol. Chem. 1996; 271: 19042-19052Abstract Full Text Full Text PDF PubMed Scopus (20) Google Scholar). it is H-myomesin is in In the of and mammals, only S-myomesin is expressed in heart and skeletal Thus, the of H-myomesin may be part of that birds from the we find that myomesin isoforms of heart and skeletal muscle in and in In we is to an the the with of Different be to splicing events or to as the in is to an the of the of or species have to be In to of S-myomesin be in chicken we that is to the of the splicing and that S-myomesin a major in muscle of the embryonic a specific myomesin isoform is expressed in heart that is characterized by the of the that EH-myomesin to a splice of called F. K. D. 1999; PubMed Scopus Google J. 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