Comparison of anticoagulant effects of regulatory proline-containing oligopeptides. Specificity of glyprolines, semax, and selank and potential for their practical application

La, Liapina; Ve, Pastorova; Оберган, Т.Ю.; Ge, Samonina; Ip, Ashmarin; Nf, Miasoedov

doi:10.1134/s1062359006020099

Cited by 10 publications

(7 citation statements)

References 27 publications

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“…Apart from proinflammatory activity, numerous beneficial effects of proline-containing short sequences were observed. For example, glyprolines regulate the endothelial permeability 34,35 , hemostasis 36,37 , carbohydrate and lipid metabolism 38 as well as protect gastric mucosa 9 .…”

Section: Biological Activity Of the Collagen-derived Glyprolinesmentioning

confidence: 99%

Proline‐containing peptides—New insight and implications: A Review

Misiura

Miltyk

2019

BioFactors

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The family of regulatory proline‐containing peptides (PCPs), also known as glyprolines, exhibit significant biological activity. The group of glyprolines includes Gly‐Pro (GP), Pro‐Gly‐Pro (PGP), cyclic Gly‐Pro (cGP), as well as PGP derivatives, for example, N‐acetylated PGP (N‐a‐PGP) and N‐methylated PGP (N‐m‐PGP). PCPs are engaged in various biological processes including the proinflammatory neutrophil chemoattraction in lung diseases, inflammatory bowel diseases or ischemic stroke. Glyprolines have been also postulated to play an important role as atheroprotective and anticoagulant agents, exhibit neuroprotective effects in Parkinson's disease, as well as regulate insulin‐like growth factor (IGF) homeostasis. It was also noticed that PCPs inhibit proliferation and migration of keratinocytes in wound healing, protection of the gastric mucosa and stimulation of its regeneration. The regulatory glyprolines are derived from endogenous and exogenous sources. Most PCPs are derived from collagen or diet protein degradation. Recently, great interest is concentrated on short proline‐rich oligopeptides derived from IGF‐1 degradation. The mechanism of PCPs biological activity is not fully explained. It involves receptor‐mediated mechanisms, for example, N‐a‐PGP acts as CXCR1/2 receptor ligand, whereas cGP regulates IGF‐1 bioavailability by modifying the IGF‐1 binding to the IGF‐1 binding protein‐3. PGP has been observed to interact with collagen‐specific receptors. The data suggest a promising role of PGP as a target of various diseases therapy. This review is focused on the effect of PCPs on metabolic processes in different tissues and the molecular mechanism of their action as an approach to pharmacotherapy of PCPs‐dependent diseases.

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Section: Biological Activity Of the Collagen-derived Glyprolinesmentioning

confidence: 99%

Proline‐containing peptides—New insight and implications: A Review

Misiura

Miltyk

2019

BioFactors

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“…72 Gly-Pro-Arg-Pro peptides are not directly involved with the binding of fibrinogen to platelets, the peptide is perhaps an antagonist which binds to the ligand, preventing its interaction with receptors. 72,80,81 A decapeptide, LGGAKQAGDV, which corresponds to the residues 402 to 411 of the fibrinogen γ-chain, inhibits the binding of fibrinogen to the thrombin-stimulated platelets. Fibrinogen binding of the peptide depended on the applied dosage, where the optimal dose has IC 50 of 50 to 100 μM and maximum inhibition above 90%.…”

Section: Endogenous Proteins and Peptides As Platelet Inhibitorsmentioning

confidence: 99%

“…71,76,82 Bradykinin is a short-lived vasoactive peptide that has been reported to promote vasodilation, exerts antiproliferative effects and inhibits thrombin-induced platelet activation in vitro. 72,80,81 The stable metabolic endproduct of bradykinin, is a pentapeptide, known as bradykinin (1-5) which is formed by the proteolytic action of angiotensin-converting enzyme. The study carried by Murphey et al 72 have demonstrated that Bradykinin (1-5) has the ability to inhibit platelet aggregation in humans through a novel mechanism without causing vasodilation Apelin peptide is the endogenous ligand of APJ, a G protein-coupled receptor.…”

Section: Endogenous Proteins and Peptides As Platelet Inhibitorsmentioning

confidence: 99%

Bioactive peptides and proteins as alternative antiplatelet drugs

Rengasamy

Khan

Ahmad

et al. 2019

Medicinal Research Reviews

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Antiplatelet drugs reduce the risks associated with atherothrombotic events and show various applications in diverse cardiovascular diseases including myocardial infarctions. Efficacy of the current antiplatelet medicines including aspirin, clopidogrel, prasugrel and ticagrelor, and the glycoprotein IIb/IIIa antagonists, are limited due to their increased risks of bleeding, and antiplatelet drug resistance. Hence, it is important to develop new effective antiplatelet drugs, with fewer side‐effects. The vast repertoire of natural peptides can be explored towards this goal. Proteins and peptides derived from snake venoms and plants represent exciting candidates for the development of novel and potent antiplatelet agents. Consequently, this review discusses multiple peptides that have displayed antiplatelet aggregation activity in preclinical drug development stages. This review also describes the antiplatelet mechanisms of the peptides, emphasizing the signaling pathways intervened by them. Also, the hurdles encountered during the development of peptides into antiplatelet drugs have been listed. Finally, hitherto unexplored peptides with the potential to prevent platelet aggregation are explored.

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“…Glyproline peptides are abundant in collagen and gelatine hydrolysates and cause significant inhibition of some factors involved in blood coagulation and platelet aggregation [99,113]. Some collagen-derived peptides may also suppress thrombocyte aggregation [114][115][116], as observed in vitro and also in vivo. The peptides PGP, PG, GP, and Gly-Pro-Gly-Gly have been found to show ability to increase fibrinolytic, anticoagulant, and antithrombotic activities in rat plasma [99,113].…”

Section: Other Interesting Activitiesmentioning

confidence: 99%

Marine Collagen as a Source of Bioactive Molecules: A Review

Alemán¹,

Martínez-Álvarez

2013

NPJ

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Skins, scales and bones are the major by-products of the fish-processing industry. These by-products are not regarded as ordinary saleable products and are usually discarded causing a heavy environmental impact. However, they are a good source of collagen. This collagen could be extracted and further enzymatically hydrolysed to liberate physiologically active peptides. Specifically, some collagen-derived peptides may exhibit interesting antioxidant activity, potent antihypertensive activity, antimicrobial activity against different strains of bacteria, protective effect on cartilage, or capacity to stimulate bone formation. Collagen hydrolysates from fish disposals may also exhibit other interesting activities (e.g., satiety, calciotropic, or opioid). The bioactive properties of collagen-derived peptides, and also their resistance to protein digestion, make them potential ingredients of health promoting foods.

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Comparison of anticoagulant effects of regulatory proline-containing oligopeptides. Specificity of glyprolines, semax, and selank and potential for their practical application

Cited by 10 publications

References 27 publications

Proline‐containing peptides—New insight and implications: A Review

Proline‐containing peptides—New insight and implications: A Review

Bioactive peptides and proteins as alternative antiplatelet drugs

Marine Collagen as a Source of Bioactive Molecules: A Review

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