caa a22 4500 397493975 CHVBK 20180308164516.0 cr unu---uuuuu 161202e199510 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a124980 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a124980 Temporally Distinctive Changes of Alternative Splicing Patterns during Myogenic Differentiation of C2C12 Cells [Elektronische Daten] [Yoshinari Harada, Masahiko Nakamura, Akira Asano] It is well known that skeletal muscle differentiation is accompanied by the appearance of many muscle-specific components and that some of these components are generated through muscle-specific alternative splicing. It is not clear, however, in what manner, including timing, the system that regulates the muscle-specific splicing reactions is constructed during the process of myogenic differentiation. We simultaneously examined the changes in several splicing patterns for the neural cell adhesion molecule (NCAM), β-tropomyosin, and M-type pyruvate kinase genes during myogenic differentiation of cultured myoblasts using the reverse transcription-polymerase chain reaction method. The NCAM glycosyl-phosphatidylinositol anchor form increased in preference to the transmembrane form immediately after the induction of differentiation, while the selection of NCAM MSD1 (muscle-specific domain 1) exons started and abruptly increased at about the time when cell-fusion appeared. M2-type pyruvate kinase was gradually substituted for the Ml-type molecule. Skeletal muscle-type β-tropomyosin was predominantly selected even in myoblasts in the growth medium. As a result, each transcript of these genes independently showed a temporally distinctive pattern of change in isoform selection during the myogenic differentiation of C2C12 cells. These observations suggest that some independent regulation of alternative splicing reactions should occur during myogenic differentiation. © Oxford University Press Regular Papers nationallicence alternative splicing nationallicence C2C12 nationallicence muscle-specific domain nationallicence myogenic differentiation nationallicence neural cell adhesion molecule nationallicence Harada Yoshinari Institute for Protein Research, Osaka University, Suita, Osaka 565 aut Nakamura Masahiko Institute for Protein Research, Osaka University, Suita, Osaka 565 aut Asano Akira Institute for Protein Research, Osaka University, Suita, Osaka 565 aut The Journal of Biochemistry Oxford University Press 118/4(1995-10), 780-790 0021-924X 118:4<780 1995 118 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a124980 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a124980 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Harada Yoshinari Institute for Protein Research, Osaka University, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Nakamura Masahiko Institute for Protein Research, Osaka University, Suita, Osaka 565 aut NATIONALLICENCE 700 1- Asano Akira Institute for Protein Research, Osaka University, Suita, Osaka 565 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 118/4(1995-10), 780-790 0021-924X 118:4<780 1995 118 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford