Nagata S, Fukunaga R
Osaka Bioscience Institute, Japan.
Prog Growth Factor Res. 1991;3(2):131-41. doi: 10.1016/s0955-2235(05)80004-3.
Granulocyte colony-stimulating factor (G-CSF) is a glycoprotein of Mr of about 20,000, which stimulates proliferation and differentiation of progenitor cells of neutrophils. Recent clinical application of G-CSF has proven that this hormone is effective in treatment of patients suffering from neutropenia. In the last few years, the biochemical and molecular nature of the G-CSF receptor has been characterized. The G-CSF receptor is a glycoprotein of Mr 100-130,000, and is expressed on the cell surface of various myeloid cells. A homodimer of this polypeptide can bind G-CSF with a high affinity, and transduce G-CSF-triggered growth signals into cells. Its extracellular domain contains a sequence of about 200 amino acids which can be found in various cytokine receptors. In addition, it contains an immunoglobulin-like domain and three fibronectin type III domains. The overall structure of the beta-chain (gp130) of the interleukin 6 receptor was found to be very similar to that of the G-CSF receptor.
粒细胞集落刺激因子（G-CSF）是一种分子量约为20,000的糖蛋白，可刺激中性粒细胞祖细胞的增殖和分化。G-CSF最近的临床应用已证明，这种激素在治疗中性粒细胞减少症患者方面是有效的。在过去几年中，G-CSF受体的生化和分子特性已得到表征。G-CSF受体是一种分子量为100 - 130,000的糖蛋白，在各种髓样细胞的细胞表面表达。该多肽的同型二聚体可以高亲和力结合G-CSF，并将G-CSF触发的生长信号传导到细胞中。其细胞外结构域包含约200个氨基酸的序列，该序列可在各种细胞因子受体中找到。此外，它还包含一个免疫球蛋白样结构域和三个纤连蛋白III型结构域。发现白细胞介素6受体的β链（gp130）的整体结构与G-CSF受体非常相似。
