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目的探讨转甲状腺素蛋白(transthyretin,TTR)在家族性淀粉样变多发性神经性损害(familial amyloidotic polyneuropathy,FAP)中的淀粉样变形成机制。方法 (1)利用质量分析装置法(matrix assisted laser desorption ionisation time-of-flight massspectrometry,MALDI-TOF/MS)测定TTR基因突变类型。(2)刚果红染色(Congo red,CR)结合偏振光显微镜检查鉴定心脏组织是否发生淀粉样变沉积。(3)免疫组化染色鉴定淀粉样变沉积蛋白类型。(4)组织形态学分析确定TTR淀粉样变沉积程度及其分布特点。结果 (1)MALDI-TOF/MS分析结果说明基因突变类型为ATTRVal30Met。(2)FAP患者心脏组织CR染色与偏振光显微镜检查确定淀粉样变沉积阳性,且心肌纤维间隙存有明显淀粉样变沉积。(3)免疫组化染色结果显示淀粉样变沉积前蛋白为TTR。结论 FAP ATTRVal30Met患者心肌间隙与疏松间质处,淀粉样变沉积明显,提示机体内TTR的载体运输或蛋白化学修饰等因素在淀粉样变形成机制中,可能具有重要作用。
Objective To investigate the mechanism of transehyretin (TTR) amyloidosis in familial amyloidotic polyneuropathy (FAP). Methods (1) The type of TTR gene mutation was determined by matrix assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF / MS). (2) Congo red staining (CR) combined with polarized light microscopy to identify whether the occurrence of amyloidosis in cardiac tissue deposition. (3) Immunohistochemistry to identify the type of amyloid deposition protein. (4) histomorphological analysis to determine the degree of TTR amyloidosis and its distribution characteristics. Results (1) MALDI-TOF / MS analysis showed that the gene mutation type was ATTRVal30Met. (2) CR staining and polarized light microscopy of cardiac tissue in patients with FAP confirmed positive amyloid deposition, and significant amyloid deposition in the myocardial fiber interstitial space. (3) The results of immunohistochemistry showed that the pre-amyloid deposition protein was TTR. Conclusions FTA ATTRVal30Met in patients with myocardial interstitial interstitial space and amyloidosis obvious, suggesting that TTR carrier transport or protein chemical modification and other factors in the mechanism of amyloidosis may play an important role.