DEGRADATION AND DEPOSITION OF AMYLOID AA FIBRILS ARE TISSUE SPECIFIC
DEGRADATION AND DEPOSITION OF AMYLOID AA FIBRILS ARE TISSUE SPECIFIC
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DOI：
10.1021/bi00399a035
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发表时间：
1987-12-15
期刊：
影响因子：
2.9
通讯作者：
FRANGIONE, B
中科院分区：
文献类型：
--
作者：
PRELLI, F;PRAS, M;FRANGIONE, B
完整的氨基酸序列的两个相关的AA蛋白（先生9700和5300）来自甲状腺组织的患者，NOR，与常染色体隐性遗传病家族性地中海热进行了测定。在位置52处发现的杂合表明这些蛋白质是两个等位基因或同种型SAA前体分子的片段，其在不寻常的位点类似地降解并沉积在甲状腺中。降解似乎是组织和/或酶特异性的，因为两个片段的羧基末端是Ala-Ala，并且不同于从不同患者的各种组织中提取的其他AA淀粉样蛋白原纤维。电子显微镜研究表明，这些片段保留了天然淀粉样纤维的特征，在生理条件下，即使暴露于解离剂。
The complete amino acid sequences of two related AA proteins (Mr 9700 and 5300) derived from thyroid tissue from a patient, NOR, with the autosomal recessive disease familial Mediterranean fever were determined. Heterogeneity found at position 52 indicates these proteins are fragments of two allelic or isotypic SAA precursor molecules similarly degraded at unusual sites and deposited in the thyroid. Degradation appears to be tissue and/or enzyme(s) specific since the carboxy terminus of both fragments is Ala-Ala and is different from other AA amyloid fibrils extracted from various tissues in different patients. Electron micrographic studies reveal these fragments retain characteristics of native amyloid fibrils under physiological conditions even after exposure to dissociating agents.