Insulin resistent diet
Low insulin levels in the blood have the opposite effect by promoting widespread catabolism. Insulin (from the Latin, insula meaning island) is a peptide hormone produced by beta cells of the pancreatic islets. For uses of insulin in treating diabetes, see insulin (medication). The human insulin protein is composed of 51 amino acids, and has a molecular mass of 5808 Da. There are a variety of treatment regimens, none of which are entirely satisfactory. Bovine insulin differs from human in only three amino acid residues, and porcine insulin in one. Even insulin from some species of fish is similar enough to human to be clinically effective in humans. It is a dimer of an A-chain and a B-chain, which are linked together by disulfide bonds. Insulin from animal sources differs somewhat in effectiveness (in carbohydrate metabolism effects) from human insulin because of these variations.
Within vertebrates, the amino acid sequence of insulin is strongly conserved. In general, the A-boxes bind to Pdx1 factors, E-boxes bind to NeuroD, C-boxes bind to MafA, and cAMP response elements to CREB. A variety of mutant alleles with changes in the coding region have been identified. If pancreatic beta cells are destroyed by an autoimmune reaction, insulin can no longer be synthesized or be secreted into the blood. Insulin in some invertebrates is quite similar in sequence to human insulin, and has similar physiological effects. It is therefore an anabolic hormone, promoting the conversion of small molecules in the blood into large molecules inside the cells. INS, IDDM, IDDM1, IDDM2, ILPR, IRDN, MODY10, insulin. Several regulatory sequences in the promoter region of the human insulin gene bind to transcription factors. CAAT enhancer binding (CEB) (partly overlapping A2 and C1).
