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GF1-DES is considered to be a highly potent version of IGF1 by some bodybuilders, the myth claims that it may increase local prolifiration and that the product is much more effective then the endogenous IGF1 our body produce. I've been asked again and again whether there is a scientific prove for this claim,
Hereinafter you may see some scientific literature that confirms the extremely high potency of the IGF1-DES as well as some indications for therapeutic applications for it
ormat: AbstractSend to
Int J Biochem Cell Biol. 1996 Oct;28(10):1085-7.
Des(1-3)IGF-I: a truncated form of insulin-like growth factor-I.
Ballard FJ1, Wallace JC, Francis GL, Read LC, Tomas FM.
Author information
Abstract
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.
Hereinafter you may see some scientific literature that confirms the extremely high potency of the IGF1-DES as well as some indications for therapeutic applications for it
ormat: AbstractSend to
Int J Biochem Cell Biol. 1996 Oct;28(10):1085-7.
Des(1-3)IGF-I: a truncated form of insulin-like growth factor-I.
Ballard FJ1, Wallace JC, Francis GL, Read LC, Tomas FM.
Author information
Abstract
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.
