title: Overlapping imprinting of oligopeptides in Chang liver cells. Data on the mechanism of hormone evolution.
abstract: 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.
mesh_terms: 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
chemical_list: D006728:Hormones; D009842:Oligopeptides; D021382:Protein Sorting Signals; D011956:Receptors, Cell Surface