Searchable abstracts of presentations at key conferences in endocrinology

ea0029p808 | Endocrine tumours and neoplasia | ICEECE2012

Insulin, IGF-II and a low-affinity insulin analog differentially regulate insulin receptor isoform A trafficking and induce a different balance of metabolic and mitogenic effects

Morcavallo A. , Genua M. , Palummo A. , Kletvikova E. , Jiracek J. , Brzozowski A. , Iozzo R. , Belfiore A. , Morrione A.

Introduction: The isoform A of the human insulin receptor (IR-A) binds insulin with high affinity, and binds IGF-II with a 3–10 folds lower affinity. Cells lacking the insulin-like Growth Factor-I receptor (IGF-IR) and overexpressing the human IR-A (R-/IR-A cells) respond to IGF-II with reduced metabolic effects but unaltered or increased mitogenesis as compared to insulin stimulation. We hypothesized that this altered ratio of metabolic-to-mitogenic effects of IGF-II in ...