Interaction of plasma fibronectin with gelatin and complement C1q.
Interaction of plasma fibronectin with gelatin and complement C1q.
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血浆纤连蛋白与明胶和补体 C1q 的相互作用。
DOI：
10.1016/0161-5890(83)90068-8
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发表时间：
1983
影响因子：
3.6
通讯作者：
Miekka,SI
中科院分区：
文献类型：
--
作者：
Ingham,KC;Brew,SA;Miekka,SI
各种技术已被用来检查人血浆纤连蛋白（Fn）与补体C1 q的相互作用相比，与明胶在磷酸盐缓冲盐水在pH 7.4。通过加入明胶，3 H-Fn通过聚乙二醇（PEG）的沉淀被转移到低得多的聚合物浓度，并且在较小程度上，通过C1 q。沉淀of 3-Fn在C1 q的存在下是接近的C1 q单独在相同的条件下，表明亲合性的Fn固相C1 q的，类似的相互作用被视为与热不溶的C1 q。纤维连接蛋白与明胶-琼脂糖凝胶和C1 q-琼脂糖凝胶紧密结合，这种结合可被明胶抑制，但不被C1 q抑制。明胶的存在下，阻碍了阳极迁移的Fn在生理条件下的免疫电泳过程中，而C1 q只有在低离子强度的影响。Fn，单独和预孵育明胶或C1 q的排阻色谱法，也与明胶形成强复合物，但不与C1 q一致。在分析ultracentrage，Fn的沉降不受C1 q的存在下，而类似的Fn和明胶的混合物表现出快速沉降边界和显着的12 S Fn峰耗尽。用Fn滴定荧光素标记的I型胶原α 2链，可使荧光偏振增强，而加入未标记的α 2链或明胶可逆转荧光偏振，但C1 q或C1 q的胃蛋白酶衍生的胶原样结构域则不能逆转荧光偏振。这些观察结果表明，Fn与C1 q的液相相互作用比与明胶弱得多，但Fn确实对固相C1 q具有明显的亲和力。这种相互作用可能意味着Fn在从循环中清除免疫复合物中的作用。
A variety of techniques have been used to examine the interaction of human plasma fibronectin (Fn) with complement C1q in comparison to that with gelatin in phosphate buffered saline at pH 7.4. The precipitation of3H-Fn by polyethylene glycol (PEG) was shifted to much lower concentrations of the polymer by addition of gelatin, and to a lesser extent, by C1q. Precipitation of3-Fn in the presence of C1q was close to that of C1q alone under identical conditions suggesting an affinity of Fn for solid phase C1q; a similar interaction was seen with heat-insolubilized C1q. Fibronectin bound tightly to gelatin-Sepharose and C1q-Sepharose and this binding could be inhibited by gelatin but not by C1q. The presence of gelatin retarded the anodal migration of Fn during immunoelectrophoresis under physiological conditions whereas C1q had an effect only at low ionic strength. Exclusion chromatography of Fn, alone and preincubated with gelatin or C1q, was also consistent with the formation of strong complexes with gelatin but not with C1q. In the analytical ultracentrifuge, the sedimentation of Fn was not affected by the presence of C1q, whereas similar mixtures of Fn and gelatin exhibited a fast-sedimenting boundary and marked depletion of the 12S Fn peak. Titration of fluorescein-labeledα2chains of type I collagen with Fn produced an increase in fluorescence polarization which could be reversed by addition ofunlabeledα2chains or gelatin but not by C1q or the pepsin-derived collagen-like domain of C1q. These observations indicate that the fluid-phase interaction of Fn with C1q is much weaker than that with gelatin but that Fn does have appreciable affinity for solid-phase C1q. Such interaction could signify a role for Fn in the clearance of immune complexes from circulation.
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球状蛋白的可逆缔合过程。
影响因子：
3.9
作者：
R. Steiner
通讯作者：
R. Steiner
C1 抑制剂依赖性人补体成分 C1 与免疫复合物结合的解离。
影响因子：
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DOI：
--
发表时间：
1982
期刊：
Journal of immunology (Baltimore, Md. : 1950)
影响因子：
--
作者：
Pearlstein,E;Sorvillo,J;Gigli,I
通讯作者：
Gigli,I
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影响因子：
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作者：
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影响因子：
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作者：
DESSAU, W;ADELMANN, BC;MARTIN, GR
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