Possible regulation of FGF activity by syndecan, an integral membrane heparan sulfate proteoglycan.
Possible regulation of FGF activity by syndecan, an integral membrane heparan sulfate proteoglycan.
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Syndecan(一种完整膜硫酸乙酰肝素蛋白多糖)可能调节 FGF 活性。
DOI:
10.1111/j.1749-6632.1991.tb49029.x
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发表时间:
1991
影响因子:
5.2
通讯作者:
Hooper,KC
中科院分区:
文献类型:
--
作者:
Bernfield,M;Hooper,KC
The fibroblast growth factors (FGFs) have affinity for heparin (for reviews see References 1, 2, and 3). This binding is not likely a physiological interaction because heparin itself is not usually found in the extracellular space (for extensive discussions, see References 4 and 5). Heparin proteoglycans are intracellular, within the secretory granules of mast cells and basophils, and can become extracellular when these cells degranulate at sites of specific immune reactions. Heparin binding by these extracellular growth factors likely represents interactions with the heparinlike molecule, heparan sulfate, that is found within cells, at the cell surface, and within the extracellular matrix. Many cells possess so-called low-affinity receptors for basic FGF (bFGF)(Kd ca. 2 nM, ca. 0.5-2 x 10 ‘binding sites per cell) on their surfaces.’These “receptors” have all the properties of heparan sulfate proteoglycans; the bound FGF can be displaced by treatment with heparin or heparan sulfate and can be removed by digestion with heparitinase or proteases.’