대한의생명과학회지 (Biomedical Science Letters)
- 제10권1호
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- Pages.23-29
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- 2004
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- 1738-3226(pISSN)
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- 2288-7415(eISSN)
Identification of Non-Muscle Nebulin Isoform in Human Brain Library
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Joo, Young-Mi
(Department of Biomedical Laboratory Science, Inje University) ;
- Lee, Min-A (Department of Biomedical Laboratory Science, Inje University) ;
- Choi, Pyung-Rak (Department of Biomedical Laboratory Science, Inje University) ;
- Choi, Jae-Kyoung (Department of Biology, Inje University) ;
- Lee, Yeong-Mi (Department of Biomedical Laboratory Science, Inje University) ;
- Choi, Su-Il (Department of Biomedical Laboratory Science, Inje University) ;
- Kim, Myong-Shin (Department of Biomedical Laboratory Science, Inje University) ;
- Jeon, Eun-Hee (Department of Biomedical Laboratory Science, Inje University) ;
- Kim, So-Young (Department of Biomedical Laboratory Science, Inje University) ;
- Kim, Chong-Rak (Department of Biomedical Laboratiory Science)
- 발행 : 2004.03.01
초록
Nebulin is a (Mr 600∼900 kDa) large actin-binding protein specific to skeletal muscle and thought to act as a molecular template that regulates the length of thin filaments. Cardiac muscles of higher vertebrates have been shown earlier to lack nebulin. Recently, full-length nebulin mRNA transcripts have been detected in heart muscle, but at lower levels than in skeletal muscle. Nebulin expression also was detected in the kidney, eye, and otic canal, suggesting that nebulin isoforms may also be expressed in these organs. We have searched for nebulin isoforms in brain of human using PCR and Northern blot. Here, we provide evidence that nebulin mRNA transcripts are expressed in brain. Seven nebulin isoforms (B, C, D, E, F, G and H form) are obtained in human skeletal muscle and four isoforms (B, C, G and H form) in human brain cDNA library. We cloned the 1.3 kb of nebulin fragment from human adult brain library by PCR. The identity of the PCR product was confirmed by sequence analysis. The partial brain nebulin sequence was 99% identical to the skeletal muscle cDNA as determined by Blast alignment. It contains two simple-repeats HR1, HR2 and linker-repeats exon l35∼143 except exon 140. It was different from skeletal muscle B form, which contain HR1 and HR8. These data suggest that nebulin isoform diversity occurs even more extensively than previously known, likely contributing to the distinct thin filament architecture of different striated muscles.