Overlapping imprinting of oligopeptides in Chang liver cells. Data on the mechanism of hormone evolution.
Imprinting was induced with synthetic oligopeptides in Chang liver cell cultures to test these molecules for signal molecule value. Investigations into imprinting overlaps (cross-imprinting) have shown that all oligopeptides (di-, tetra- and pentapeptides) carrying a terminal proline group were able to imprint the cells for the pentapeptide Tyr-D-Met-Gly-Phe-Pro-NH2, which displayed an outstanding imprinting potential for itself and an extraordinary opioid activity as well. The fact that exclusively the proline-deficient oligopeptide (a tetrapeptide) failed to imprint for the pentapeptide in question, indicates a decisive role of proline in the transformation of molecules to signal carriers (hormones). The pentapeptide in question did imprint for the related molecules (except the dipeptide) but to a much lesser degree than for itself. The marked inferiority of the pentapeptide's cross-imprinting potential to its self-imprinting potential supports the hypothetical implication that a considerable difference between the specific and non-specific binding capacities of a molecule, if not the loss of non-specific binding was an essential prerequisite of transformation to a signal molecule, i.e. of hormone evolution.
D000818:Animals; D005075:Biological Evolution; D002460:Cell Line; D006728:Hormones / Q000502:physiology*; D008099:Liver / Q000187:drug effects / Q000502:physiology; D009842:Oligopeptides / Q000494:pharmacology* / Q000502:physiology; D021382:Protein Sorting Signals / Q000502:physiology; D011956:Receptors, Cell Surface / Q000187:drug effects / Q000502:physiology
D006728:Hormones; D009842:Oligopeptides; D021382:Protein Sorting Signals; D011956:Receptors, Cell Surface