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研究生:李慧芳
研究生(外文):Lee. Hui-fang
論文名稱:大白鼠骨骼肌於神經截斷後肌原纖維內titin蛋白質之變化
論文名稱(外文):Effect of denervation on titin in myofibrils of rat skeletal muscles
指導教授:劉克明劉克明引用關係馮琮涵馮琮涵引用關係
指導教授(外文):Liu, Keh-MinFong, T. H.
學位類別:碩士
校院名稱:高雄醫學大學
系所名稱:醫學研究所
學門:醫藥衛生學門
學類:醫學學類
論文種類:學術論文
論文出版年:2000
畢業學年度:88
語文別:中文
論文頁數:39
中文關鍵詞:titin神經截斷骨骼肌
外文關鍵詞:titindenervationskeletal muscle
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已有許多研究結果顯示截斷神經之後的肌肉會出現重量減輕,肌纖維萎縮以及收縮力減弱等現象。此外,收縮後回復至原來狀態所須的時間也有增長的情形,但是其原因仍然未明。目前已知肌肉放鬆的回復力主要來自肌原纖維內的巨型蛋白質(titin)。但是截斷神經對肌原纖維內titin蛋白質的影響則尚未明瞭。因此本實驗,我們將大白鼠的坐骨神經(sciatic nerve)截斷,促使比目魚肌(soleus)和脛前肌(anterior tibialis)萎縮,分離出肌肉中的 肌原纖維(myofibrils)後以電泳方法(SDS-PAGE)使蛋白質分離,再利用densitometry分析肌原纖維內titin,myosin和actin等蛋白質的含量。我們發現在截斷神經一天、一週變化不顯著,而在二週、三週、四週及八週後不論是比目魚肌或脛前肌,其肌原纖維內titin與myosin含量的相對比值(titin/myosin)皆有明顯降低的情形。利用抗titin 的單株抗體代號T12進行免疫螢光染色,在正常的肌原纖維內此抗體標幟的位置靠近Z-line,呈現平行Z-line的橫紋染色構造。而在截斷神經後萎縮的肌原纖維中,此橫紋染色構造則呈現點狀不完整的形式。由以上結果推測,截斷神經後titin蛋白質含量減少的速率較myosin與actin等蛋白質更為快速。可能由於titin蛋白質快速的減少因而使得截斷神經後的肌肉出現肌節不完整、收縮力減弱以及回復至原來狀態所須時間增長等現象。

Several studies have reported that denevated muscles undergo weight loss, fiber atrophy and force output reduction. Besides, an increase in relaxation time is also observed, but the causes are still not clear. The restoring force after contraction is found to originate from titin which is a giant myofibrillar protein. However, the effects of denervation on titin have not been examined. In the present study, denervation of rat soleus and anterior tibialis muscles were performed by segmental resection of the sciatic nerve. Using SDS-PAGE to separate the myofibrillar proteins and densitometry to analyze the amounts of titin、myosin and actin in myofibrils, we found that the ratio of titin/myosin obviously decreased in soleus and anterior tibialis muscles after four-weeks of denervation. Immunofluorescent for titin with monoclonal antibody T12 which specifically labeled a titin epitope near the Z-line displayed a typical striated staining pattern in normal myofibrils, but a spot staining pattern near the Z-line region in denervated myofibrils. These results suggested that titin declined faster than myosin and actin after denervation. This phenomenon might be correlated with sarcomere disassembly, the force output decrease and relaxtion time elongation observed in denervated muscles.

目次
英文摘要 1
中文摘要 2
緒論 3
材料與方法 6
結果 10
討論 13
參考文獻 16

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