Marine Antithrombotics

Dwivedi, Rohini; Pomin, Vitor H.

doi:10.3390/md18100514

Cited by 21 publications

(14 citation statements)

References 99 publications

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“…Consequently, this might indicate the presence of glycans or glycan‐like agents, which could result in minimal bleeding effects (Pomin, 2015). This finding stresses the fact of potent antithrombotic agents within mussels, such as sulphated glycans, protease inhibitors, or galactans, among other agents mentioned in the literature (Brito et al., 2014; Dwivedi & Pomin, 2020; Gomes et al., 2010; Pomin, 2015).…”

Section: Discussionmentioning

confidence: 51%

Antioxidant and antithrombotic effects of green mussels ( Perna canaliculus ) in rats

et al. 2021

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In the past decade, the use of marine mussels as seafood is being more popular. They considered being a rich source of various nutritional bioactive compounds that aroused the scientific community's interest. This study investigated the antioxidant and the antithrombotic consequences on Sprague‐Dawley male rats after adding dried New Zealand mussel Perna canaliculus in their diet. The biochemical, hematological and histopathological changes were also observed. Forty rats were divided into four groups according to the amount of dried mussels in their diet, in addition to a control group that consumed a basal diet only. Group 1 consumed 25% dried mussels in its basal diet; Group 2 consumed 35% dried mussels in its basal diet, and Group 3 was consumed 45% dried mussels in its basal diet. The biochemical parameters showed improvements in liver function. Interestingly, the lipid profile decreased, especially the low‐density lipoprotein cholesterol (LDL‐C) levels which were reduced significantly in Group 3 (p < .01). These observations were accompanied by a decrease in iron levels significantly as the amount of dried mussels increased (p < .01). Furthermore, the noticed changes in the hematological profile prove that there is an increase in antithrombotic activity. Dried mussels had potent antioxidant effects in the liver as shown by increased lipid peroxide (p < .05), reduced glutathione (p < .05), and glutathione peroxidase (GSH‐Px; p < .05). Additionally, antioxidant activity in the kidney was shown to increase through GSH‐Px activity (p < .01). In conclusion, these results indicate that consuming dried mussels resulted in improved biochemical and antioxidants activities and could be used as an antithrombotic agent.

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Section: Discussionmentioning

confidence: 51%

Antioxidant and antithrombotic effects of green mussels ( Perna canaliculus ) in rats

et al. 2021

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“…Moreover, an unexpected fucose (deoxy-hexose) modification was found on the xylose residue of the linkage region of human bikunin and decorin and on two novel human CSPGs; retinoic acid responder protein 1 and meprin A ( Gomez Toledo et al, 2015 ; Nasir et al, 2016 ). This was surprising as fucosylated CS chains have previously only been described in sea cucumbers, a member of the phylum of Echinodermata ( Myron et al, 2014 ; Dwivedi and Pomin, 2020 ). Notably, this fucose modification in human CS was located on xylose (and not on the CS chain), i.e., close to the protein component.…”

Section: Proteoglycan Linkage Region Complexitymentioning

confidence: 95%

Expanding the Chondroitin Sulfate Glycoproteome — But How Far?

Noborn

Nikpour

Persson

et al. 2021

Front. Cell Dev. Biol.

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Chondroitin sulfate proteoglycans (CSPGs) are found at cell surfaces and in connective tissues, where they interact with a multitude of proteins involved in various pathophysiological processes. From a methodological perspective, the identification of CSPGs is challenging, as the identification requires the combined sequencing of specific core proteins, together with the characterization of the CS polysaccharide modification(s). According to the current notion of CSPGs, they are often considered in relation to a functional role in which a given proteoglycan regulates a specific function in cellular physiology. Recent advances in glycoproteomic methods have, however, enabled the identification of numerous novel chondroitin sulfate core proteins, and their glycosaminoglycan attachment sites, in humans and in various animal models. In addition, these methods have revealed unexpected structural complexity even in the linkage regions. These findings indicate that the number and structural complexity of CSPGs are much greater than previously perceived. In light of these findings, the prospect of finding additional CSPGs, using improved methods for structural and functional characterizations, and studying novel sample matrices in humans and in animal models is discussed. Further, as many of the novel CSPGs are found in low abundance and with not yet assigned functions, these findings may challenge the traditional notion of defining proteoglycans. Therefore, the concept of proteoglycans is considered, discussing whether “a proteoglycan” should be defined mainly on the basis of an assigned function or on the structural evidence of its existence.

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“…DD, which contains two crosslinked D fragments of the fibrin protein, is produced from crosslinked fibrin by the plasmin's action. FDP is the degradation product of fibrous protein [34]. t-PA transforms plasminogen into plasmin.…”

Section: Effect Of Clam Heparinoids On Fibrinolysis In Vivomentioning

confidence: 99%

Antithrombotic Activity of Heparinoid G2 and Its Derivatives from the Clam Coelomactra antiquata

et al. 2022

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Clam heparinoid G2 (60.25 kDa) and its depolymerized derivatives DG1 (24.48 kDa) and DG2 (6.75 kDa) prepared from Coelomactra antiquata have been documented to have excellent fibrinolytic and anticoagulant activity. In this study, to further explore the antithrombotic activity of G2, DG1 and DG2, azure A, sheep plasma, and clot lytic rate assays were used to determine their anticoagulant and thrombolytic activity in vitro. The results indicated that the anticoagulant titer of G2 was approximately 70% that of heparin and the thrombolytic activity of DG2 was greater than G2, DG1, and heparin activities. Moreover, in a carrageenan-induced venous thrombosis model, oral administration of G2 and DG1 each at 20 mg/kg and 40 mg/kg for 7 days significantly reduced blacktail thrombus formation, increased tissue-type plasminogen activator, fibrin degradation products, and D-dimer levels, decreased von Willebrand factor and thromboxane B2 levels, and restored phylum and genus abundance changes of intestinal bacteria. DG2 had no antithrombotic effect. At 20 mg/kg, G2, DG1, and heparin had comparable antithrombotic activities, and DG1 at 40 mg/kg had more muscular antithrombotic activity than G2. Thus, DG1 could be an antithrombotic oral agent owing to its more robust antithrombotic activity and lower molecular weight.

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Marine Antithrombotics

Cited by 21 publications

References 99 publications

Antioxidant and antithrombotic effects of green mussels ( Perna canaliculus ) in rats

Antioxidant and antithrombotic effects of green mussels ( Perna canaliculus ) in rats

Expanding the Chondroitin Sulfate Glycoproteome — But How Far?

Antithrombotic Activity of Heparinoid G2 and Its Derivatives from the Clam Coelomactra antiquata

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