Ballard F J, Wallace J C, Francis G L, Read L C, Tomas F M
Cooperative Research Centre for Tissue Growth and Repair, Adelaide, Australia.
Int J Biochem Cell Biol. 1996 Oct;28(10):1085-7. doi: 10.1016/1357-2725(96)00056-8.
Des(1-3)IGF-I, a truncated variant of human IGF-I with the tripeptide Gly-Pro-Glu absent from the N-terminus, has been isolated from bovine colostrum, human brain and porcine uterus. This protein probably results from post-translational cleavage of IGF-I. Des(1-3)IGF-I generally is about 10-fold more potent than IGF-I at stimulating hypertrophy and proliferation of cultured cells, a consequence of much reduced binding to IGF-binding proteins, in turn caused by the absence of the glutamate at position 3. The increased potency is retained in part when the variant is administered in vivo, with selective anabolic effects particularly evident in gut tissues. Clinical opportunities for des(1-3)IGF-I have not yet been evaluated, but could apply in catabolic states as well as for the treatment of inflammatory bowel diseases.
脱(1-3)胰岛素样生长因子I(Des(1-3)IGF-I)是人类胰岛素样生长因子I(IGF-I)的一种截短变体,其N端缺少三肽Gly-Pro-Glu,已从牛初乳、人脑和猪子宫中分离出来。这种蛋白质可能是IGF-I翻译后切割的产物。在刺激培养细胞的肥大和增殖方面,脱(1-3)胰岛素样生长因子I通常比胰岛素样生长因子I强约10倍,这是由于与胰岛素样生长因子结合蛋白的结合大大减少所致,而这又是由第3位谷氨酸的缺失引起的。当该变体在体内给药时,其增强的效力部分得以保留,在肠道组织中选择性合成代谢作用尤为明显。脱(1-3)胰岛素样生长因子I的临床应用机会尚未得到评估,但可应用于分解代谢状态以及治疗炎症性肠病。