High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells--implications for the modulation of FGF-2.
High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells--implications for the modulation of FGF-2.
复制标题
DOI：
10.1083/jcb.128.6.1221
复制
发表时间：
1995-03
影响因子：
7.8
通讯作者：
BAIRD, A
中科院分区：
文献类型：
--
作者：
HANNEKEN, A;MAHER, PA;BAIRD, A
我们最近表征了三种FGF结合蛋白（FGF- bp），它们是高亲和力FGF受体的细胞外结构域的可溶性形式（Hanneken， A. M.， W. Ying， N. Ling和A. Baird）。Proc。国家的。学会科学。美国。1994. 91:9170 - 9174)。这些蛋白在血液中循环，并被认为可以调节FGF蛋白家族的生物活性。免疫组织化学研究表明，这些可溶性截断的FGF受体也存在于视网膜血管内皮细胞的基底膜中。这些免疫反应蛋白可以用抗体检测到FGFR-1的细胞外结构域，但不能用抗体检测到FGFR-1的近膜结构域或细胞质结构域。在FGFR-1细胞外区域用抗体对人视网膜提取物进行Western blotting，可检测到85kd和55kd的特异性低分子质量蛋白，其大小与fgf - bp相对应，而针对该受体细胞质区域的抗体无法检测到这些蛋白。这种受体与细胞外基质的相互作用不依赖于FGF-2的存在。肝素酶去除FGF-2后，在血管基底膜中仍可检测到免疫反应性受体。此外，在用2 M NaCl去除内源性FGF-2后，FGFR-1的重组细胞外结构域继续与角膜内皮细胞基质结合。酸处理，已被证明会破坏蛋白质与细胞外基质的相互作用，导致FGF受体基质形式的存在显著减少。这种损失可以通过外源性培养FGFR-1的重组细胞外结构域来恢复。该报告首次证明了高亲和力生长因子受体的截断形式可以定位于细胞外基质。这些发现增加了与细胞外基质相关的结合蛋白（IGFBP-5）的列表，并提出了一种潜在的新的调节机制来控制细胞外基质中FGF和其他肽生长因子的生物可利用性。
We recently characterized three FGF-binding proteins (FGF-BPs) which are soluble forms of the extracellular domains of the high affinity FGF receptors (Hanneken, A. M., W. Ying, N. Ling, and A. Baird. Proc. Natl. Acad. Sci. USA. 1994. 91:9170-9174). These proteins circulate in blood and have been proposed to modulate the biological activity of the FGF family of proteins. Immunohistochemical studies now demonstrate that these soluble, truncated FGF receptors are also present in the basement membranes of retinal vascular endothelial cells. These immunoreactive proteins can be detected with antibodies raised to the extracellular domain of FGFR-1 but not with antibodies raised to either the juxtamembrane domain or the cytoplasmic domain of FGFR-1. Western blotting of human retinal extracts with the antibody raised to the extracellular domain of FGFR-1 detects specific, low molecular mass proteins at 85 kD and 55 kD, corresponding in size to the FGF-BPs, which are not detected with antibodies against the cytoplasmic domain of the receptor. The interaction of this receptor with the extracellular matrix is not dependent on the presence of FGF-2. Immunoreactive receptors are still detected in vascular basement membranes after the removal of FGF-2 with heparitinase. In addition, the recombinant extracellular domain of FGFR-1 continues to bind to corneal endothelial cell matrix after endogenous FGF-2 has been removed with 2 M NaCl. Acid treatment, which has been shown to disrupt protein interactions with the extracellular matrix, leads to a significant reduction in the presence of the matrix form of the FGF receptor. This loss can be restored with exogenous incubations of the recombinant extracellular domain of FGFR-1. This report is the first demonstration that a truncated form of a high affinity growth factor receptor can be localized to the extracellular matrix. These findings add to the list of binding proteins associated with the extracellular matrix (IGFBP-5) and suggest a potentially new regulatory mechanism for controlling the biological availability of FGF, and other peptide growth factors, in the extracellular matrix.
登录
查看更多内容
DOI：
10.3109/08977199109000276
发表时间：
1991-01-01
期刊：
Growth factors (Chur, Switzerland)
影响因子：
--
作者：
Kiefer, M C;Baird, A;Barr, P J
通讯作者：
Barr, P J
DOI：
10.1083/jcb.107.2.743
发表时间：
1988-08
期刊：
The Journal of cell biology
影响因子：
--
作者：
Saksela O;Moscatelli D;Sommer A;Rifkin DB
通讯作者：
Rifkin DB
DOI：
10.1073/pnas.87.22.8702
发表时间：
1990-11-01
影响因子：
11.1
作者：
FUKUNAGA, R;SETO, Y;NAGATA, S
通讯作者：
NAGATA, S
影响因子：
5.3
作者：
JOHNSON, DE;LEE, PL;WILLIAMS, LT
通讯作者：
WILLIAMS, LT
影响因子：
11.4
作者：
TAKAKI, S;TOMINAGA, A;TAKATSU, K
通讯作者：
TAKATSU, K