Insulin is a secreted peptide hormone that elicits metabolic effects such as increases in glucose uptake and glycogen synthesis leading to a decrease in blood glucose concentration. Insulin is first formed as a precursor molecule, preproinsulin, which is later cleaved to proinsulin and finally to the mature insulin hormone. Mature insulin consists of 51 amino acids, contained within an A chain and a B chain that are connected by two disulfide bridges. It increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin is secreted by the pancreas at basal levels in the absence of exogenous stimuli, with secretion increasing in response to glucose. Insulin action is effected by the binding of insulin to cell-surface receptors on the target cell membrane. Defects of insulin are the cause of hyperproinsulinemia and of type-II diabetes mellitus.
Background References
1. Lines KE et al. Epigenetic pathway inhibitors represent potential drugs for treating pancreatic and bronchial neuroendocrine tumors. Oncogenesis 6:e332 (2017).
2. Perez-Basterrechea M et al. Fibroblasts accelerate islet revascularization and improve long-term graft survival in a mouse model of subcutaneous islet transplantation. PLoS One 12:e0180695 (2017).
Immunohistochemical analysis of paraffin-embedded human pancreas tissue with Mouse anti-Insulin antibody (EM1701-33) at 1/5,000 dilution.
The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes. The tissues were blocked in 1% BSA for 20 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (EM1701-33) at 1/5,000 dilution for 1 hour at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
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