Abstract
The expression of α-dystrobrevin and dystrophin in rat tibialis anterior muscles was chronologically evaluated during a cycle of regeneration after myonecrosis induced by the injection of cardiotoxin. In immunohistochemical studies, α-dystrobrevin and dystrophin were first stained weakly at the sarcolemma of some regenerating muscle fibers on day 5. On day 7, α-dystrobrevin was still stained weakly, whereas dystrophin was stained conspicuously. After day 10, α-dystrobrevin and dystrophin were both stained conspicuously on almost all regenerating muscle fibers. In the Western blot analysis, α-dystrobrevin and dystrophin were first detected as visible bands on days 5 and 7, respectively. The bands of α-dystrobrevin and dystrophin both darkened sequentially up to day 10. The protein levels based on the densitometrical analysis of the bands on each day were converted to the percentage of the protein level on day 28, which was taken as 100%. The sequential line based on these data showed that α-dystrobrevin and dystrophin reached 50% of the protein level on day 28 by 6.6 and 5.3 days, respectively. These data provide evidence that α-dystrobrevin regenerates more slowly than dystrophin in skeletal muscle.
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References
Ahn AH and Kunkel LM (1995) Syntrophin binds to an alternatively spliced exon ofdystrophin. J Cell Biol 128: 363–371.
Ambrose HJ, Blake DJ, Nawrotzki RA and Davies KE (1997) Genomic organization of the mouse dystrobrevin gene: comparative analysis with the dystrophin gene. Genomics 39: 359–369.
Blake DJ, Nawrotzki R, Loh NY, Górecki DC and Davies KE (1998) ?-Dystrobrevin, a member of the dystrophin-related protein family. Proc Natl Acad Sci USA 95: 241–246.
Blake DJ, Nawrotzki R, Peters MF, Froehner SC and Davies KE (1996) Isoform diversity of dystrobrevin, the murine 87-kDa postsynaptic protein. J Biol Chem 271: 7802–7810.
Butler MH, Douville K, Murnane AA, Kramarcy NR, Cohen JB, Sealock R and Froehner SC (1992) Association of the Mr 58,000 postsynaptic protein ofelectric tissue with Torpedo dystrophin and the Mr 87,000 postsynaptic protein. J Biol Chem 267: 6213–6218.
Carr CG, Fischbach D and Cohen JB (1989) A novel 87,000-Mr protein associated with acetylcholine receptors in Torpedo electric organ and vertebrate skeletal muscle. J Cell Biol 109: 1753–1764.
Dwyer TM and Froehner SC (1995) Direct binding of Torpedo syntrophin to dystrophin and the 87 kDa dystrophin homologue. FEBS Lett 375: 91–94.
Froehner SC, Adams ME, Peters MF and Gee SH (1997) Syntrophins: modular adapter proteins at the neuromuscular junction and the sarcolemma. Soc Gen Physiol Ser 52: 197–207.
Grady RM, Grange RW, Lau KS, Maimone MM, Nichol MC, Stull JT and Snes JR (1999) Role for ?-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies. Nat Cell Biol 1: 215–220.
Grady RM, Zhou H, Cunningham JM, Henry MD, Campbell KP and Sanes JR (2000) Maturation and maintenance of the neuromuscular synapse: genetic evidence for roles of the dystrophin-glycoprotein complex. Neuron 25: 279–293.
Hoffman EP, Fischbeck KH, Brown RH, Johnson M, Medori R, Loike JD, Harris JB, Waterston R, Brooke M, Specht L, Kupsky W, Chamberlain J, Caskey T, Shapiro F and Kunkel LM (1988) Characterization of dystrophin in muscle-biopsy specimens from patients with Duchenne's or Becker's muscular dystrophy. N Engl J Med 318: 1363–1368.
Hoffman EP, Knudson CM, Campbell KP and Kunkel LM (1987) Subcellular fractionation of dystrophin to the triads of skeletal muscle. Nature 330: 754–758.
Hoshino S, Ohkoshi O, Ishii A, Kameya S, Takeda S and Shoji S (2001) The expression of dystrophi n and 1-syntrophin during skeletal muscle regeneration. J Muscle Res Cell Motil 22: 185–191.
Kameya S, Miyagoe Y, Nonaka I, Ikemoto T, Endo M, Hanaoka K, Nabeshima Y and Takeda S (1999) ?1-syntrophin gene disruption results in the absence of neuronal-type nitric-oxide synthase at the sarcolemma but does not induce muscle degeneration. J Biol Chem 274: 2193–2200.
Lim LE, Duclos F, Broux O, Bourg N, Sunada Y, Allamand V, Meyer J, Richard I, Moomaw C, Slaughter C, Tomé FMS, Fardeau M, Jackson CE, Beckmann JS and Campbell KP (1995) ?-sarcoglycan: characterization and role in limb-girdle muscular dystrophy linked to 4q12. Nature Genet 11: 257–265.
Nawrotzki R, Loh NY, Ruegg MA, Davies KE and Blake DJ (1998) Characterization of ?-dystrobrevin in muscle. J Cell Sci 111: 2595–2605.
Nicholson LVB, Davison K, Falkous G, Harwood C, O'Donnell E, Slater CR and Harris JB (1989) Dystrophin in skeletal muscle I. Western blot analysis using a monoclonal antibody. J Neurol Sci 94: 125–136.
Noguchi S, McNally EM, Othmane KB, Hagiwara Y, Mizuno Y, Yoshida M, Yamamoto H, Bönnemann CG, Gussoni E, Denton PH, Kyriakides T, Middleton L, Hentati F, Hamida MB, Nonaka I, Vance JM, Kunkel LM and Ozawa E (1995) Mutations in the dystrophin-associated protein ?-sarcoglycan in chromosome 13 muscular dystrophy. Science 270: 819–822.
Ohlendieck K, Matsumura K, Ionasescu VV, Towbin JA, Bosch EP, Weinstein SL, Sernett SW and Campbell KP (1993) Duchenne muscular dystrophy: deficiency of dystrophin-associated proteins in the sarcolemma. Neurology 43: 795–800.
Ohlendieck K (1996) Towards an understanding of the dystrophin-glycoprotein complex: linkage between the extracellular matrix and the membrane cytoskeleton in muscle fibers. Eur J Cell Biol 69: 1–10.
Passos-Bueno MR, Moreira ES, Vainzof M, Marie SK and Zatz M (1996) Linkage analysis in autosomal recessive limb-girdle muscular dystrophy (AR LGMD) maps a sixth form to 5q33-34 (LGMD2F) and indicates that there is at least one more subtype of AR LGMD. Hum Mol Genet 5: 815–820.
Peters MF, Adams ME and Froehner SC (1997a) Differential association of syntrophin pairs with dystrophin complex. J Cell Biol 138: 81–93.
Peters MF, O'Brien KF, Sadoulet-Puccio HM, Kunkel LM, Adams ME and Froehner SC (1997b) ?-Dystrobrevin, a new member of the dystrophin family. J Biol Chem 272: 31,561–31,569.
Peters MF, Sadoulet-Puccio HM, Mark Grady R, Kramarcy NR, Kunkel LM, Sanes JR, Sealock R and Froehner SC (1998) Differential membrane localization and intermolecular associations of ?-dystrobrevin isoforms in skeletal muscle. J Cell Biol 142: 1269–1278.
Puca AA, Nigro V, Piluso G, Belsito A, Sampaolo S, Quaderi N, Rossi E, Di Iorio G, Ballabio A and Franco B (1998) Identification and characterization of a novel member of the dystrobrevin gene family. FEBS Lett 425: 7–13.
Roberds SL, Leturcq F, Allamand V, Piccolo F, Jeanpierre M, Anderson RD, Lim LE, Lee JC, Tomé FMS, Romero NB, Fardeau M, Beckmann JS, Kaplan JC and Campbell KP (1994) Missense mutations in the Adhalin gene linked to autosomal recessive muscular dystrophy. Cell 78: 625–633.
Sadoulet-Puccio HM, Khurana TS, Cohen JB and Kunkel LM (1996) Cloning and characterization of the human homologue of a dystrophin related phosphoprotein found at the Torpedo electric organ post-synaptic membrane. Hum Mol Genet 5: 489–496.
Sadoulet-Puccio HM, Rajala M and Kunkel LM (1997) Dystrobrevin and dystrophin: an interaction through coiled-coil motifs. Proc Natl Acad Sci USA 94: 12,413–12,418.
Sunada Y and Campbell KP (1995) Dystrophin-glycoprotein complex: molecular organization and critical roles in skeletal muscle. Curr Opin Neurol 8: 379–384.
Suzuki A, Yoshida M, Yamamoto H and Ozawa E (1992) Glycoprotein-binding site of dystrophin is confined to the cystein-rich domain and the first half of the carboxy-terminal domain. FEBS Lett. 308: 154–160.
Suzuki A, Yoshida M and Ozawa E (1995) Mammalian ?1-and ?1-syntrophin bind to the alternative splice-prone region of the dystrophin COOH terminus. J Cell Biol 128: 373–381.
Wagner KR, Cohen JB and Huganir RL (1993) The 87K postsynaptic membrane protein from Torpedo is a protein-tyrosine kinase substrate homologous to dystrophin. Neuron 10: 511–522.
Yoshida M, Hama H, Ishikawa-Sakurai M, Imamura M, Mizuno Y, Araishi K, Wakabayashi-Takai E, Noguchi S, Sasaoka T and Ozawa E (2000) Biochemical evidence for association of dystrobrevin with the sarcoglycan-sarcospan complex as a basis for understanding sarcoglycanopathy. Hum Mol Genet 9: 1033–1040.
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Hoshino, S., Ohkoshi, N., Ishii, A. et al. The expression of α-dystrobrevin and dystrophin during skeletal muscle regeneration. J Muscle Res Cell Motil 23, 131–138 (2002). https://doi.org/10.1023/A:1020256316659
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DOI: https://doi.org/10.1023/A:1020256316659