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“–Žž�Aƒn�[ƒo�[ƒh‚ÌDr. Kunkel‚É‚æ‚Á‚ÄDMDŒ^ƒWƒXƒgƒ�ƒtƒB�[‚ÌŒ´ˆöˆâ“`Žq‚ª“¯’肳‚ê�AгŽÒ‚³‚ñ‚ÅŒ‡‘¹‚µ‚Ä‚¢‚镪Žq‚̓XƒyƒNƒgƒŠƒ“‚ÉŽ—‚½‹ØŒ`Ž¿–Œ— ‘Å‚¿‹�‘åƒ^ƒ“ƒpƒNŽ¿‚Å‚ ‚邱‚Æ‚ª”»–¾�Adystrophin‚Æ–½–¼‚³‚ꂽ*�i•ªŽq—ʂ̓XƒyƒNƒgƒŠƒ“‚Ì‚Q”{‚Å–ñ420kDa�j�B‚±‚Ìdystrophin‚𖌂ɂ‚Ȃ¬‚Ƃ߂Ă¢‚é–Œƒ^ƒ“ƒpƒNŽ¿•¡�‡‘Ì‚ð�A“¯Œ¤‹†Žº‚Ì‹g“cŽº’·�i“–Žž�j‚ª�¶‰»Šw“I‚É“¯’肳‚ê‚Ä‚¢‚½‚Ì‚Å�A‚»‚̉ð�͂̂¨Žè“`‚¢‚ð‚µ‚È‚ª‚ç�A�¶‰»Šw‚ÌŠî–{‚ðŠw‚ñ‚¾�B“–Žž�AƒXƒ^ƒ“ƒtƒH�[ƒh‚ÌDr. Campbell(�¡“ú‚̃WƒXƒgƒ�ƒtƒBƒ“Œ¤‹†‚Ì‘åŒä�Š)‚Æ‹£‘ˆ‚µ‚È‚ª‚ç‚ÌŒ¤‹†‚Å‚ ‚è�A‘½‚­‚̋ǖʂʼnŸ‚³‚ê‹C–¡‚ł͂ ‚Á‚½‚ª�Aƒ|ƒXƒhƒNˆê”N–Ú‚Ì�u�Å�‰‚ÌŽdŽ–�v‚ð“ÆŽ©‚É”­“W‚³‚¹�Aƒ†ƒj�[ƒN‚È•û–@‚Å‚»‚ê‚܂ŕs–¾‚¾‚Á‚½dystrophin•ªŽq�ã‚Ì–Œƒ^ƒ“ƒpƒNŽ¿Œ‹�‡•”ˆÊ‚ðŒ©‚Â‚¯�o‚µ�A‚Ü‚³‚É‚»‚̗̈悪�Aˆâ“`“I‚ÉŒ‡Ž¸‚µ‚½�ê�‡‚É�d“Ä‚È�Ç�ó‚ɂȂé—̈æ‚Å‚ ‚邱‚Æ‚ðŽ¦‚·‚±‚Æ‚ª‚Å‚«‚½�iNature‚É“Š�e‚µ�Arevise‚µ‚½Œã‚©‚ç�A‚â‚Á‚Ï‚ènature‚Ìscope‚É�‡‚í‚È‚¢‚©‚çƒ_ƒ�‚Æreject‚³‚ꂽ�j�B�C�s‚Æ‚µ‚Ä‚¨Žè“`‚¢‚Å‚â‚Á‚Ä‚¢‚éŽdŽ–‚©‚ç‚Ȃɂ©–Ê”’‚¢‚±‚Æ‚ðŒ©‚Â‚¯�o‚·‚±‚Æ‚ª�o—ˆ‚È‚¢‚©�A�A�A‚ƈê�¶Œœ–½�l‚¦‚Ä�Aˆê‚‚̃AƒCƒfƒA‚ðŽv‚¢‚‚«�A‚»‚ÌŽÀŒ±‚ªŒ©Ž–‚É�¬Œ÷‚µ‚½Žž‚Ì‚¤‚ꂵ‚³‚Í–Y‚ê‚ç‚ê‚È‚¢�B Œ¤‹†ŽÒ‚Æ‚µ‚Ä‚â‚Á‚Ä�s‚­ˆê‚‚̎©�M‚ɂȂÁ‚½�B‚±‚ê‚Í�ACambel‚Œ‚̈ê‚Â�æ‚ð�s‚­ŽdŽ–‚Å‚ ‚è�A‚»‚Ì“_‚Å‚à”ñ�í‚É‚¤‚ꂵ‚©‚Á‚½�B

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* ƒqƒgƒQƒmƒ€‚Ì�î•ñ‚à‚È‚¢‚±‚Ì“–Žž‚ÌKunkel”ŽŽm‚Ì�¬‰Ê‚Í�A‰ÆŒn•ª�Í‚©‚瓾‚ç‚ꂽ�î•ñ‚©‚çprobe‚Ì�î•ñ‚©‚ç�AгŽÒ‚³‚ñ‚ÅŒ‡Ž¸‚µ‚Ä‚¢‚é—̈æ‚ð�A�L‘å‚ȃQƒmƒ€�ã‚ňê•àˆê•à�A�uŽÀŒ±“I‚É�v‹l‚߂Ă¢‚­�i‚Ü‚³‚É�Achromosome walking‚ƌĂ΂ꂽ�j’n“¹‚ÈŒ¤‹†‚ÌŒ‹‰Ê‚Å‚ ‚è�Aƒqƒgˆâ“`•a‚ÌŒ´ˆöˆâ“`Žq‚ð�‡ˆâ“`Šw“I‚É“¯’肵‚½�A‚Ù‚Ú�Å�‰‚Ì�¬‰Ê‚Å‚ ‚邯�‚‚­•]‰¿‚³‚ê‚Ä‚¢‚é�B�B
   
   
  1992”N Yoshida M, Suzuki A, Shimizu T, * Ozawa E.
Proteinase-sensitive sites on isolated rabbit dystrophin. J. Biochem. 112: 433-439, 1992
     
    Suzuki A, Yoshida M, Yamamoto H, * Ozawa E.
Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxy-terminal domain. FEBS Lett. 308: 154-160, 1992
     
  1994”N Mizuno Y, Noguchi S, Yamamoto H, Yoshida M, Suzuki A, Hagiwara Y. et al. Selective defect of sarcoglycan complex in severe childhood autosomal recessive muscular dystrophy muscle. Biochem. Biophyis. Res. Commun. 203: 979-983, 1994
     
  Suzuki A, Yoshida M, Hayashi K, Mizuno Y, Hagiwara Y, * Ozawa E.
Molecular organization at the glycoprotein-binding site of dystrophin�\Three dystrophin-associated proteins, 43DAG(A3a), A0 and beta-A1, directly bind to the carboxy-terminal portion of dystrophin�\�@Eur. J. Biochem. 220: 283-292, 1994
     
    Yoshida M, Suzuki A, Yamamoto H, Mizuno Y, * Ozawa E.
Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside. Eur. J. Biochem. 222: 1055-106, 1994
     
  1995”N  Suzuki A, Yoshida M, * Ozawa E.
Mammalian alpha1 and beta1 syntrophin bind to the alternative splice-prone region of the dystrophin C-terminus. J. Cell. Biol. 128: 373-381, 1995
     
    * Ozawa E, Yoshida M, Suzuki A, Mizuno Y, Hagiwara Y, Noguchi S.(Review)
Dystrophin-associated proteins in muscular dystrophy. Hum. Mol. Genet. 4: 1711-1716, 1995