Biochemical characterization of collagens synthesized by fibroblasts derived from normal and diseased human gingiva.
Biochemical characterization of collagens synthesized by fibroblasts derived from normal and diseased human gingiva.
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来自正常和患病人类牙龈的成纤维细胞合成的胶原蛋白的生化特征。
DOI：
10.1016/s0021-9258(17)33082-x
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发表时间：
1976
期刊：
影响因子：
--
通讯作者：
R. Page
中科院分区：
文献类型：
--
作者：
A. Narayanan;R. Page
用放射性氨基酸标记健康人和患病人牙龈成纤维细胞，研究其合成胶原蛋白的情况。十二烷基硫酸钠聚丙烯酰胺凝胶电泳的未处理的，减少，和胃蛋白酶处理的蛋白质的培养基和细胞提取物表明，这些细胞合成的胶原蛋白存在的前体形式。Ⅰ型胶原是主要成分。此外，来自正常组织的细胞合成的III型胶原的量从5%到30%不等。在患病组织的成纤维细胞培养物中未检测到III型胶原;然而，额外的胶原在2.5至5.0 M NaCl之间分离，占总量的22至29%。该胶原蛋白的α 1/α 2比为8.6，羟赖氨酸/赖氨酸比和溴化氰肽模式与α 1 [I]相似。得出结论，来源于患病牙龈的成纤维细胞合成组分（α 1）3的胶原，可能是I型胶原。
Fibroblasts obtained from healthy and diseased human gingiva were labeled with radioactive amino acids and the collagenous proteins synthesized were studied. Sodium dodecyl sulfate polyacrylamide gel electrophoresis of untreated, reduced, and pepsin-treated proteins of the medium and cell extract showed that the collagenous proteins synthesized by these cells exist in the precursor form. Type I collagen was the chief constituent. In addition, cells from normal tissue synthesized type III collagen in amounts varying from 5 to 30%. Type III collagen was not detected in the cultures of fibroblasts from diseased tissue; however, an additional collagen fractionated between 2.5 to 5.0 M NaCl and accounted for 22 to 29% of the total. This collagen had an alpha1/alpha2 ratio of 8.6 and hydroxylysine/lysine ratio and cyanogen bromide peptide pattern were similar to that of alpha1[I]. It is concluded that the fibroblasts derived from disease gingiva synthesize a collagen of composition (alpha1)3, probably of type I.