IGF-1 DES

Vitamin D inhibits the RhoA/ROCK pathway and reduces cyclooxygenase-2 expression and prostaglandin E2 production in BPH stromal cells.; Higher dietary and supplemental vitamin D intake is associated with lower BPH prevalence.; Vitamin D analogues up to 6000 IU/day decreased prostate volume in BPH patients.; Pre-clinical trials showed vitamin D reduces BPH cell proliferation, even when induced by growth promoters like testosterone and IL-8.

IGF-1(des) expression caused hyperplastic prostate growth in all transgenic mice.; Well-differentiated hyperplastic lesions did not progress to adenocarcinoma within one year.; Crossing PB-Des mice with a prostate cancer model delayed organ-confined tumor progression and metastasis in young mice.; IGF-1(des) was absent in poorly differentiated primary tumors and metastases, indicating negative selection against IGF-1 action.

Des-IGF-1 (40 ng/ml) increased fEPSP slope by 40% in CA1 region.; Enhancement was postsynaptic and mediated by AMPA, not NMDA, receptors.; Effect was blocked by genistein and significantly reduced by PI3K inhibitors wortmannin and LY294002.; Acute des-IGF-1 action may contribute to cognitive improvement via AMPA receptor modulation.

Type 1 IGF receptor immunoreactivity increased ~3-fold in INL and GCL of diabetic rats vs controls.; Phospho-Akt (Thr 308) immunoreactivity increased 5-fold in GCL and 8-fold in INL of diabetic rats.; Des(1-3)IGF-1 treatment significantly reduced immunoreactive cells in both layers.; Preliminary results suggested VEGF levels may also be reduced by the treatment.

Des IGF-I decreased plasma glucose by about 50% without altering insulin or IGF-I levels.; Akt-1 phosphorylation at Ser473 increased in both skeletal and cardiac muscle.; p70 S6K phosphorylation at Thr421/Ser424 increased only in skeletal muscle.; FKHR phosphorylation increased only in cardiac muscle, while CREB phosphorylation remained unchanged.

IGFBP-3 inhibits IGF-I-induced receptor autophosphorylation and tyrosine kinase activity in a dose-dependent manner.; Inhibition occurs with IGF analogs des(1-3)IGF-I and [Q3A4Y15L16]-IGF-I, which have weak or no IGFBP affinity.; IGFBP-3 does not directly interact with the type 1 IGF receptor, as shown by cross-linking experiments.; The effect is specific to IGFBP-3 and the type 1 IGF receptor, with no inhibition by IGFBP-1, IGFBP-5, or on insulin receptor activation.

IGF-1 had a blood half-life of 4.5 min and remained intact for 20 min, entering brain and spinal cord linearly.; Intact radiolabeled IGF-1 was present in brain parenchyma 20 min after intravenous injection, not trapped in vasculature.; Nonradiolabeled IGF-1 enhanced influx after intravenous injection but inhibited it during in-situ perfusion, indicating protein binding effects.; Spinal cord uptake varied by region, with cervical fastest and thoracic slowest, comparable to brain.

IGF-1 mRNA increased in a time-dependent manner during BMDM development.; IGFBP-4 protein accumulation increased posttranscriptionally while its mRNA remained constant.; All three forms of IGF-1 potentiated proliferation of freshly isolated BMDM precursors.; Long R3 IGF-1 and des(1-3) IGF-1, but not rhIGF-1, enhanced BMDM differentiation on day 4.

What is IGF-1 DES?

IGF-1 DES (DES(1-3) IGF-1) is a naturally occurring truncated variant of insulin-like growth factor 1, lacking the N-terminal tripeptide Gly-Pro-Glu. This deletion reduces its affinity for IGF-binding proteins (IGFBPs), resulting in a significantly shorter half-life but enhanced local bioavailability and potency at the

How does IGF-1 DES work?

Truncated IGF-1 variant with high local potency and short half-life, studied for site-specific muscle growth.

What is the research status of IGF-1 DES?

IGF-1 DES is currently classified as preclinical, with 29 research references on record. This is for research purposes only and is not medical advice.