Vainzof M, Passos-Bueno M R, Pavanello R C, Schreiber R, Zatz M
Departamento de Biologia, Universidade de São Paulo, Brazil.
J Med Genet. 1992 Jul;29(7):476-9.
The purpose of the present investigation was to assess the possibility of building a model to estimate, through dystrophin western blotting analysis, the expression of the DMD/BMD gene in muscle from heterozygotes. Dystrophin was analysed by mixing in increasing proportions (from 0% to 100%) aliquots of solubilised muscle from BMD patients with a qualitatively abnormal dystrophin and a normal male control. The intensity of the abnormal bands, which could be detected starting with 20% of muscle from the BMD patient, increased progressively according to the affected muscle concentration. In five obligate BMD carriers, two dystrophin bands were observed (corresponding to the products from the X bearing the normal and the BMD alleles), even among those with normal serum enzyme activities. Surprisingly, in the four obligate BMD carriers related to patients in whom an additional dystrophin fragment of 250 kd was present (two of them with raised serum enzymes), this band could not be seen, suggesting that the stability or the mechanism responsible for the synthesis of abnormal dystrophin products differs in heterozygotes compared to affected patients.
本研究的目的是评估通过肌营养不良蛋白免疫印迹分析构建一个模型的可能性，该模型用于估计杂合子肌肉中DMD/BMD基因的表达。通过将BMD患者溶解的肌肉等分试样（比例从0%增加到100%）与定性异常的肌营养不良蛋白和正常男性对照混合，对肌营养不良蛋白进行分析。从20%的BMD患者肌肉开始就能检测到异常条带的强度，其强度随着受影响肌肉浓度的增加而逐渐增强。在五名确诊的BMD携带者中，即使在那些血清酶活性正常的携带者中，也观察到了两条肌营养不良蛋白条带（对应于携带正常和BMD等位基因的X染色体产生的产物）。令人惊讶的是，在与存在250 kd额外肌营养不良蛋白片段的患者相关的四名确诊BMD携带者中（其中两名血清酶升高），未观察到该条带，这表明与受影响患者相比，杂合子中异常肌营养不良蛋白产物合成的稳定性或机制有所不同。
