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Research compoundEndocrine Signaling Research

IGF-1 DES

Also known as: DES(1-3)IGF-1

IGF-1 DES, or des(1-3)IGF-I, is a naturally occurring truncated form of insulin-like growth factor I lacking its first three amino acids. Research consists of older rodent, pig-cell and transgenic-mouse studies, mostly from the 1990s.

Evidence: preclinical · Older rodent and cell studies

At a glance

Class
Naturally occurring truncated IGF-I variant
Developer
No pharmaceutical developer
FDA status
Not FDA-approved
Human data
None identified
Animal / lab data
Rat dexamethasone model; rat mammary development; rat granulosa cells; pig muscle cells; transgenic mice

Where it’s been studied

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  • 1MuscleDexamethasone model, rat (1992); porcine embryonic muscle cells (1999)
  • 2Ovary & mammary glandRat granulosa cells (1992); rat mammary development (1992); transgenic mice (2001)
  • 3GutGut weight in dexamethasone model, rat (1992)
  • 4Cell studiesRat granulosa cells and porcine myogenic cells (1992, 1999)

Mechanism studied

Established: des(1-3)IGF-I binds IGF-binding proteins weakly but binds the type I IGF receptor normally [2]. In rat granulosa cells it was about 10-fold more potent than intact IGF-I when binding proteins were present, and roughly equipotent when they were removed, so its higher potency is attributed to escaping binding-protein inhibition [2]. Proposed: the same mechanism is used to explain its greater potency in whole-animal models [1][3].

What the research shows

StudyModelReported resultSource
IGF-I variants in dexamethasone-exposed rats [1]Rat
Male rats (150 g) given dexamethasone to induce a catabolic state; IGF-I, des(1-3)IGF-I or LR3 IGF-I for 7 days
des(1-3)IGF-I and LR3 IGF-I were about 2.5-fold more potent than IGF-I; gut weight rose by up to 45%.Peer-reviewed
Biochemical Journal 1992
Binding proteins and IGF-I action in granulosa cells [2]Cell
Cultured rat ovarian granulosa cells, FSH-stimulated progesterone output
des(1-3)IGF-I was about 10-fold more potent than intact IGF-I with binding proteins present; roughly equipotent when binding proteins were depleted.Peer-reviewed
Journal of Clinical Investigation 1992
Mammary gland development in rats [3]Rat
Hypophysectomized, castrated, estradiol-supplemented immature male rats
Both IGF-I forms induced terminal end bud and alveolar formation; des(1-3)IGF-I was at least 5 times more potent than intact IGF-I.Peer-reviewed
PNAS 1992
IGFBP-3 in porcine muscle cells [4]Cell
Porcine embryonic myogenic cells, serum-free, 24 hours
IGF-I and des(1-3)IGF-I each reduced IGFBP-3 in conditioned media about threefold.Peer-reviewed
Journal of Cellular Physiology 1999
Mammary overexpression in transgenic mice [5]Mouse
Transgenic mice overexpressing des(1-3) human IGF-I in mammary tissue (WAP-DES) vs littermates
Higher mammary weight and lower apoptosis during natural involution; no difference during forced involution, when IRS-1/Akt signaling fell sharply.Peer-reviewed
Endocrinology 2001

Human trials are listed for research context only; outcomes are reported in the linked publications. Animal and lab results do not establish effects in humans.

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More in Endocrine Signaling Research

Sources

  1. Tomas FM et al. (1992) Source
  2. Adashi EY et al. (1992). doi:10.1172/JCI116028 Source
  3. Ruan W et al. (1992) Source
  4. Yang F et al. (1999). doi:10.1002/(SICI)1097-4652(199902)178:2<227::AID-JCP12>3.0.CO;2-W Source
  5. Hadsell DL et al. (2001). doi:10.1210/endo.142.4.8087 Source
For research use only. Not for human or veterinary use. Not a drug, food or cosmetic, and not intended to diagnose, treat, cure or prevent any disease. This library summarizes published research for educational purposes. PureLab Performance Inc.