Xiao D M, Levine L
Prostaglandins. 1986 Nov;32(5):709-18. doi: 10.1016/0090-6980(86)90193-0.
Recombinant human interleukin-l (rIL-1) alpha and beta, which have 26% homology in their amino acid sequence, stimulated arachidonic acid metabolism by squirrel monkey smooth muscle cells and rat liver cells; their relative effectiveness, however, varied with the two cells. Recombinant IL-1 alpha was 3 times more effective than rIL-1 beta at stimulating arachidonic acid metabolism by the primate smooth muscle cells. Recombinant IL-1 alpha was 3 times less effective than rIL-1 beta when measured by their capacity to synergistically stimulate arachidonic acid metabolism of rat liver cells in the presence of palytoxin and anti-diuretic hormone (ADH). The rIL-1 alpha and rIL-1 beta also stimulated the release of radiolabelled arachidonic acid from the smooth muscle cells prelabelled with [3H]arachidonic acid. The two recombinant IL-1s have different heat stabilities, again when measured by their capacity to stimulate arachidonic acid metabolism; IL-1 alpha was more heat stable than IL-1 beta.
重组人白细胞介素-1(rIL-1)α和β,其氨基酸序列有26%的同源性,可刺激松鼠猴平滑肌细胞和大鼠肝细胞的花生四烯酸代谢;然而,它们的相对效力在这两种细胞中有所不同。在刺激灵长类平滑肌细胞的花生四烯酸代谢方面,重组IL-1α的效力是rIL-1β的3倍。当通过它们在岩沙海葵毒素和抗利尿激素(ADH)存在下协同刺激大鼠肝细胞花生四烯酸代谢的能力来衡量时,重组IL-1α的效力比rIL-1β低3倍。rIL-1α和rIL-1β还刺激了用[3H]花生四烯酸预标记的平滑肌细胞中放射性标记花生四烯酸的释放。再次通过它们刺激花生四烯酸代谢的能力来衡量时,这两种重组IL-1具有不同的热稳定性;IL-1α比IL-1β更耐热。