IDENTIFICATION OF SOLUBLE FORMS OF THE FIBROBLAST GROWTH-FACTOR RECEPTOR IN BLOOD
IDENTIFICATION OF SOLUBLE FORMS OF THE FIBROBLAST GROWTH-FACTOR RECEPTOR IN BLOOD
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DOI：
10.1073/pnas.91.19.9170
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发表时间：
1994-09-13
影响因子：
11.1
通讯作者：
BAIRD, A
中科院分区：
文献类型：
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作者：
HANNEKEN, A;YING, WB;BAIRD, A
我们从人血浆和小牛血清中纯化了三种酸性 (FGF-1) 和碱性 (FGF-2) 成纤维细胞生长因子结合蛋白（FGF-BP1、FGF-BP2 和 FGF-BP3），并证明了这些循环 FGF-BP 在血液中的存在。每种都是高亲和力 FGF 受体 (FGFR-1) 的截短形式。 FGF-BP1 和 FGF-BP2 的估计分子量分别为 70-85 kDa 和 55-60 kDa，并通过使用 I-125 标记的 FGF-2 配体印迹进行检测。使用四种不同的 FGFR-1 抗体进行的免疫印迹表明，FGF-BP1 和 FGF-BP2 在免疫学和生化方面与 FGFR-1 的胞外结构域相关。反相 HPLC 色谱法将 FGF-BP2 分解为两种蛋白质，估计分子量分别为 55 kDa 和 60 kDa。 FGF-BP2 和 FGF-BP3 氨基末端的蛋白质测序揭示了其与人 FGFR-1 的双 IgG 环形式的胞外结构域的一致性。 FGF-BP 不需要肝素即可在亲和柱上结合 FGF-2，但肝素确实可以增强其从血液中的回收率。这些 FGF-BP 可能在调节 FGF 和 FGF 生长因子家族其他成员的生物活性方面发挥重要的生理作用。
We have purified three acidic (FGF-1) and basic (FGF-2) fibroblast growth factor binding proteins (FGF-BP1, FGF-BP2, and FGF-BP3) from human plasma and calf serum and demonstrate the presence of these circulating FGF-BPs in blood. Each are truncated forms of the high-affinity FGF receptor (FGFR-1). FGF-BP1 and FGF-BP2 have estimated molecular masses of 70-85 kDa and 55-60 kDa, respectively, and are detected by using I-125-labeled FGF-2 ligand blotting. Immunoblotting with four distinct antibodies to FGFR-1 reveals that FGF-BP1 and FGF-BP2 are immunologically and biochemically related to the extracellular domain of FGFR-1. Reverse-phase HPLC chromatography resolves FGF-BP2 into two proteins with estimated molecular masses of 55 kDa and 60 kDa. Protein sequencing of the amino terminus of FGF-BP2 and FGF-BP3 reveals identity with the extracellular domain of the two-IgG-loop form of human FGFR-1. The FGF-BPs do not require heparin to bind FGF-2 on affinity columns, but heparin does enhance their recovery from blood. These FGF-BPs may play an important physiological role in regulating the biological activity of FGF and the other members of the FGF family of growth factors.