Sequential and Asynchronous Strengthening of the Influence of Temperature on the Endo- and Exocytosis of Insulin in the Isolated Vertebrata Hepatocytes: Summing up Previous Studies.

Insulin internalization and processing of the Insulin Receptor Complex (IRC) inside the cell are important components of the intracellular Mechanism of Insulin Action (MIA). They define the continuation of intracellular signaling of IRC and allow utilization of the parts of the complex after ligand dissociation. Traditionally, changes in the insulin regulatory system associated with the vertebrate phylogenesis have been evaluated by changes of its two elements: the hormone and its receptor.

[Differences in dynamics of insulin and insulin-like growth I (IGF-I) receptors internalization in isolated rat hepatocytes].

Insulin and IGF-I are two related peptides performing in the mammalian body functionally different roles of the metabolic and growth hormones, respectively. Internalization of the insulin-receptor complex (IRC) is the most important chain of mechanism of the action of hormone. To elucidate differences in the main stages of internalization of the two related hormones, the internalization dynamics of 125I-insulin and 125I-IGF-I was traced in isolated rat hepatocytes at 37 and 12 degrees C.

[Peculiarities of distribution of 125-I-insulin and 125I-insulin-like growth factor-I (IGF-I) at internalization in isolated rat hepatocytes].

One of determining conditions of formation in vertebrate phylogenesis of hormonal systems of insulin and IGF-I--peptides common by origin, similar by structure and biological action is temperature factor. In differentiation of functional roles of two related hormones and important place id ascribed to mechanism of their intracellular action. Study of formation of the two hormonal systems in vertebrate phylogenesis necessitates knowledge of peculiarities of internalization of two related hormones in mammals.

[The structural organization of binding determinants in insulin-like growth factor-I (IGF-I) molecule].

Insulin-like growth factor I (IGF-I) is a peptide related to insulin and IGF-II. These three related peptides produce similar biological effects, but each of them has its irreplaceable physiological significance in the organism. Multisided functional role of IGF-I in the organisms is due to its unique binding properties.

[The binding ability of insulin-related peptides as the clue to their functional role in phylogenesis. Introduction to the problem].

The common plan of structure of the main peptides of the vertebrate insulin family--insulin itself, IGF-I, IGF-II, and relaxin--has distinct structural features. Each of the peptides performs its characteristic function. However, overlapping of insulin and IGF-I actions and its stability in the vertebrate phylogenesis have formed the concept of their regulation of growth and metabolism as a function fixed in phylogenesis for a certain type of structures.