Regulatory Action of Synthetic Cationic Peptides Containing Residues of Glutamic Acid on Functional Activity of Components of the Adenylyl Cyclase Signal System

Ao, Shpakov; Korol'kov, V. I.; Guryanov, Ivan; Vlasova, E. N.; Plesneva, S. A.; Kuznetsova, L. A.; Воробьев, В. И.; Чихиржина, Е. В.; Vlasov, G. P.; Pertseva, M. N.

doi:10.1023/b:joey.0000031003.08816.c2

Cited by 3 publications

(6 citation statements)

References 19 publications

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“…LHR peptides are more specific, which we believe to be due to their lower positive charge. In this connection, it is to be noted that the polycationic peptides that have no homology with receptor pro teins, including polycationic toxins from insect ven oms, bacterial peptide autoinducters, and unnatural peptides with regular structure are able to directly interact with G protein α subunits (Shpakov et al, 2004Shpakov and Pertseva, 2008;Shpakov, 2010;Shpakov et al, 2010b).…”

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confidence: 99%

The secondary structure of peptides derived from the third intracellular loop of the serpentine-type receptors and its interrelation with their biological activity

et al. 2012

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Section: Discussionmentioning

confidence: 99%

The secondary structure of peptides derived from the third intracellular loop of the serpentine-type receptors and its interrelation with their biological activity

et al. 2012

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“…The nerve-ganglion fraction was obtained by the method described in [2]. The activity of adenylate cyclase (EC 4.6.1.1) was determined as described in [3]; GTP-binding activity, by the methods described in [4,5] with our modifications [6]. The We discovered that octopamine, dopamine, and serotonin (although less effectively) at concentrations of 10 -7 -10 -4 M stimulated the basal activity of adenylate cyclase in the fraction of molluscan nerve ganglia in a concentration-dependent manner (Fig.…”

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confidence: 99%

Molecular mechanisms of the regulatory effect of biogenic amines on the functional activity of the adenylate cyclase signal system in nerve ganglia of the mollusk Anodonta cygnea

Shipilov

Guryanov

et al. 2005

Dokl Biochem Biophys

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Hormone-sensitive adenylate cyclase signal system (ACSS) consisting of three major components-a receptor, a heterotrimeric G protein, and an adenylatecyclase system fragment-plays a key role in implementation of the regulatory effect of a broad spectrum of hormones and neurotransmitters of cells of vertebrates and invertebrates. Studying the molecular mechanisms of action of these regulatory molecules on the functional activity of adenylate cyclase is one of the key problems in biochemistry and molecular endocrinology, which is of great theoretical and practical importance for medicine and pharmacology. In the past years, a considerable success was achieved in studying the ACSS in the nervous system of vertebrates, and a relationship between disturbance in its functioning and development of a number of diseases of the human and animals was established. However, the ACSS in nervous tissue of invertebrates has been studied much less extensively [1]. To this end, it should be mentioned that studying the ACSS in nervous tissue of invertebrates is necessary for understanding the pathways whereby the sensitivity of nervous tissue to hormones is formed and the molecular mechanisms underlying their regulatory effect on neural cells.The goal of this study was to perform a comparative study of the effect of biogenic amines (octopamine, dopamine, serotonin, and noradrenalin) on the functional activity of ACSS components (G proteins and adenylate cyclase) in nerve ganglia of the fresh-water bivalve Anodonta cygnea , as well as to study the molecular mechanisms of their action using antagonists of receptors of biogenic amines and the synthetic peptides 385-394 and 346-355, representing the C-terminal segments of α -subunits of G proteins of the stimulatory (G s ) and inhibitory (G i 2 ) types, respectively.This was the first study to demonstrate that biogenic amines stimulate the activity of adenylate cyclase and the GTP-binding activity of G proteins in the nerve ganglia of the mollusk A. cygnea in a concentrationdependent manner, with their effectiveness decreasing in the following order: octopamine > dopamine > serotonin > noradrenalin. The effect of biogenic amines on adenylate cyclase was potentiated by guanine nucleotides. It is shown that the effect of biogenic amines on ACSS is implemented via different types of heterotrimeric G proteins: G s proteins in the case of octopamine and dopamine and both G s and G i proteins in the case of serotonin and noradrenalin. The antagonists of α 2 -adrenergic, dopamine, and serotonin receptors decrease the stimulatory effect of octopamine on molluscan ACSS, sometimes even more effectively than the corresponding agonists. Thus, we obtained new convincing evidence showing that the main molecular mechanisms underlying the regulatory effect of hormones and neurotransmitters on ACSS in nervous tissue of higher vertebrates have already been formed in bivalve mollusks, representatives of invertebrate animals. On the basis of the results obtained in this study, it can be assumed that these...

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“…At this stage, as a result of activation of G proteins of different types, the signal path way is selected, which eventually determines cell response to the hormonal effect. In the past years, we and other authors obtained data indicating that G proteins may be activated via a receptor-independent pathway as a result of their interaction with natural polycationic peptides [1,2]; with peptides that are derivatives of the cytoplasmic loops of receptors (for details, see [3]); and with polycationic compounds of an artificial origin that represent synthetic peptides [4][5][6][7][8], derivatives of positively charged amino acids [9,10], or biopolymers containing amino groups [11]. Studying peptide and nonpeptide activators of G proteins mimicking the effect of receptors is a promising approach for the search and development of new-generation drugs that are able to regulate the activity of hormonal signal systems at the stage of functional coupling between receptor and G proteins.…”

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“…Earlier, we showed that the effectiveness with which synthetic peptides interact regulate the functional activity of proteins-the components of the adenylate cyclase signal system (ACSS)-is largely determined by their structural characteristics, such as the number and distribution of positively charged amino acid residues, the ability to form amphipathic helices, the presence in the peptide molecule of hydrophobic radicals, their number, and relative orientation [6][7][8].…”

mentioning

confidence: 99%

Molecular Mechanisms of Interaction of Polycationic Peptides with G Proteins

Guryanov

Vlasov

2005

Dokl Biochem Biophys

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Regulatory Action of Synthetic Cationic Peptides Containing Residues of Glutamic Acid on Functional Activity of Components of the Adenylyl Cyclase Signal System

Cited by 3 publications

References 19 publications

The secondary structure of peptides derived from the third intracellular loop of the serpentine-type receptors and its interrelation with their biological activity

The secondary structure of peptides derived from the third intracellular loop of the serpentine-type receptors and its interrelation with their biological activity

Molecular mechanisms of the regulatory effect of biogenic amines on the functional activity of the adenylate cyclase signal system in nerve ganglia of the mollusk Anodonta cygnea

Molecular Mechanisms of Interaction of Polycationic Peptides with G Proteins

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