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