IGF-1 plays an important role in growth and continues to have anabolic effects in adults – meaning that it can induce hypertrophy of skeletal muscle and other target tissues.

Mice lacking the IGF-1 receptor die late in development, and show a dramatic reduction in body mass.

The precursor is then glycosylated, proteolytically cleaved, and crosslinked by cysteine bonds to form a functional transmembrane αβ chain.

[5] The α chains are located extracellularly, while the β subunit spans the membrane and is responsible for intracellular signal transduction upon ligand stimulation.

The IGFR signalling pathway is of critical importance during normal development of mammary gland tissue during pregnancy and lactation.

"This mutation is predicted to prevent formation of several hydrogen bonds within the cysteine-rich domain of the receptor’s ligand-binding extracellular subunit.

It is further implicated in breast cancer by increasing the metastatic potential of the original tumour by conferring the ability to promote vascularisation.

Increased levels of the IGF-IR are expressed in the majority of primary and metastatic prostate cancer patient tumors.

[17] Evidence suggests that IGF-IR signaling is required for survival and growth when prostate cancer cells progress to androgen independence.

[22] Lung cancer cells stimulated using glucocorticoids were induced into a reversible dormancy state which was dependent on the IGF-1R and its accompanying survival signaling pathways.

Prominent in current research are three main classes of inhibitor: Insulin-like growth factor 1 receptor has been shown to interact with: There is evidence to suggest that IGF1R is negatively regulated by the microRNA miR-7.