[Polycationic peptides as nonhormonal regulators of chemosignal systems].
This review summarizes and analyzes both literature data and results of our own studies on molecular mechanisms of action of natural and artificially created polycationic peptides on functional activity of heterotrimeric G-proteins and G-protein-coupled signal systems. There are considered peptide toxins from insect venom, synthetic peptides that are derivatives of cytoplasmic loops of receptors of the serpentine type as well as artificially created peptides with linear, branched, and dendrimere structures. Action of most of these peptides on activity of G-proteins is highly selective and those themselves are able to mimic the hormone-activated receptor to be thereby non-hormonal regulators of the signal systems coupled with heterotrimeric G-proteins.
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D000595:Amino Acid Sequence; D000818:Animals; D020962:Heterotrimeric GTP-Binding Proteins / Q000378:metabolism* / Q000502:physiology; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008555:Melitten / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D018000:Receptors, Peptide / Q000502:physiology; D015398:Signal Transduction / Q000187:drug effects* / Q000502:physiology; D014862:Wasp Venoms / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*
D036341:Intercellular Signaling Peptides and Proteins; D010455:Peptides; D018000:Receptors, Peptide; D014862:Wasp Venoms; D008555:Melitten; C037500:mastoparan; D020962:Heterotrimeric GTP-Binding Proteins