Receptor Structure and Activation The IGF-1 receptor shares significant structural homology with the insulin receptor, existing as a heterotetrameric complex of two extracellular -subunits (which contain the ligand binding sites) and two transmembrane -subunits (which possess intrinsic tyrosine kinase activity in their intracellular domains)
Studies also show that estrogen and phytoestrogens influence epigenetic modifications, preserving the integrity of the genome and reducing the accumulation of age-related changes (Kovcs et al., 2020
& McCarthy, M
In pre-clinical in-vitro and animal model studies, PNC-27 has demonstrated a range of significant oncological findings: Broad cancer cell selectivity demonstrated cytotoxicity against human metastatic colon adenocarcinoma, transformed rat brain capillary endothelial cells, cervical carcinoma, metastatic breast carcinoma, non-small cell lung carcinoma, osteosarcoma, pancreatic carcinoma, ovarian cancer, and multiple haematological malignancies while showing no effect on untransformed normal cell lines or human haematopoietic stem cells from cord blood p53-independent activity PNC-27 kills both MCF-7 breast cancer cells (expressing wild-type p53) and MDA-MB-157 cells (homozygously p53-deficient), as well as K562 leukaemia cells (p53-null) confirming its mechanism does not require functional p53 signalling Mitochondrial disruption beyond plasma membrane pore formation, PNC-27 enters cancer cells and disrupts mitochondrial membranes, confirmed by IEM with gold-labelled anti-PNC-27 antibody on cancer cell mitochondria
