Tanaka M, Kataoka H, Nagata K, Nagasawa H, Suzuki A
Department of Applied Biological Chemistry, University of Tokyo, Japan.
Regul Pept. 1995 Jun 27;57(3):311-8. doi: 10.1016/0167-0115(95)00044-C.
Bombyxin is a brain secretory peptide of the silkmoth Bombyx mori whose amino acid sequence shows considerable sequence homology with vertebrate insulin-family peptides. We found that a Bombyx cell line, named BM-N4, showed morphological changes when bombyxin was added to the culture medium at doses as low as 10(-10) M. Bombyxin-treated cells displayed a series of morphological modifications: 1 to 2 weeks after introduction of bombyxin, the cells increased in size, then they trended to aggregate, or took a spindle shape. These changes of the cells were bombyxin specific, not induced by other vertebrate insulin-family peptides. To prove that these modifications of the cells are mediated by receptors on the cell surface of the cells, we performed a receptor binding assay using 125I-labeled bombyxin. Scatchard analysis of the binding assay indicated that this cell line has a single class of receptors for bombyxin with a Kd = 2.36 +/- 0.56 nM and each cell has 15,800 +/- 1400 binding sites on the cell surface.
家蚕素是家蚕(Bombyx mori)的一种脑分泌肽,其氨基酸序列与脊椎动物胰岛素家族肽具有相当高的序列同源性。我们发现,一种名为BM-N4的家蚕细胞系,当在培养基中添加低至10^(-10) M剂量的家蚕素时,会出现形态变化。经家蚕素处理的细胞呈现出一系列形态改变:加入家蚕素1至2周后,细胞体积增大,随后趋于聚集,或呈纺锤形。细胞的这些变化是家蚕素特异性的,并非由其他脊椎动物胰岛素家族肽诱导产生。为证明细胞的这些改变是由细胞表面受体介导的,我们使用125I标记的家蚕素进行了受体结合试验。结合试验的Scatchard分析表明,该细胞系具有一类家蚕素受体,Kd = 2.36 +/- 0.56 nM,每个细胞在细胞表面有15,800 +/- 1,400个结合位点。