Special Issue "Marine Anticoagulants and Antithrombotics"

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (31 March 2016).

Special Issue Editors

Dr. Paulo A.S. Mourão
E-Mail Website
Guest Editor
Program of Glycobiology, Institute of Medical Biochemistry Leopoldo de Meis, University Hospital Clementino Fraga Filho, Federal University of Rio de Janeiro, Brazil
Tel. 55.21.2562.2090; Fax: +61 21 39382090
Interests: glycobiology; glycosaminoglycans; NMR spectroscopy; anticoagulation; antithrombosis; marine sulfated glycans
Dr. Vitor H. Pomin
E-Mail Website
Guest Editor
Program of Glycobiology, Institute of Medical Biochemistry Leopoldo de Meis, University Hospital Clementino Fraga Filho, Federal University of Rio de Janeiro, Brazil
Fax: +55 21 39382090
Interests: glycobiology; glycosaminoglycans; NMR spectroscopy; structural glycobiology; anticoagulation; antithrombosis; marine sulfated glycans
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Special Issue Information

Dear Colleagues,

Cardiovascular diseases are unquestionably the main cause of death in the world. For example, the World Health Organization stated that in 2011 alone, approximately 7 and 6.2 million people have died, respectively, from ischemic heart disease and stroke - the two top causes of mortality reported for that year. Curiously, the third leading cause is lower respiratory infection, which have caused 3.2 million deaths that same year. This figure comprises a little less than 4 times the rate of the first two causes of death, combined. Considering that 55 million is the estimated number of deaths in world in the year of 2011, the two first causes, combined, comprise something close to 25% of the total deaths worldwide. Based on these numbers, it is evident that there is a high demand for anticoagulant/antithrombotic agents in the global pharmaceutical market.

The naturally occurring sulfated polysaccharide heparin is the most frequently employed anticoagulant/antithrombotic agent used so far. However, clinically speaking, the therapy based on heparin presents several side-effects, such as a propensity for developing thrombocytopenia, hemorrhagic consequences; ineffectiveness in congenital or acquired antithrombin deficiencies, incapacity to inhibit thrombin bound to fibrin, extremely variable bioavailability, and inherent structural complexity and heterogeneity. Hence, the research for new, potential anticoagulant/antithrombotic agents is highly required, especially nowadays, considering the great number of cardiovascular-associated deaths and diseases.

We believe that marine-sourced compounds are promising alternatives for new anticoagulant/antithrombotic agents, because they may present unique structures that are rarely seen, or perhaps even nonexistent, in terrestrial sources. Marine compounds can also present mechanisms of action in anticoagulation and antithrombosis that are different from those of heparin. These distinct activities can either compensate for the downsides of heparin therapy or even present new routes for anticoagulant and antithrombotic therapy. We have therefore decided to develop this Special Issue entitled “Marine Anticoagulants and Antithrombotics”. As guest editors, we invite you to contribute a paper from your research to this Special Issue of Marine Drugs. We believe that your contribution is highly important for launching future new anticoagulant/antithrombotic agents that may serve as alternatives to heparin, or at least as co-adjuvants to heparin treatment.

Dr. Paulo A.S. Mourão
Dr. Vitor H. Pomin
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Marine Drugs is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2000 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


Keywords

  • anticoagulant
  • antithrombin
  • antithrombotic
  • biomacromolecules
  • blood coagulation (co)factors
  • drug development
  • drug discovery
  • drug research
  • heparin
  • heparin cofactor II
  • marine algae
  • marine invertebrate
  • marine anticoagulant
  • marine antithrombotic
  • organic molecules
  • seaweed
  • serpin-dependent anticoagulation
  • serpin-independent anticoagulation
  • synthetic molecules
  • thrombin

Published Papers (2 papers)

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Research

Open AccessArticle
Determination of FVIIa-sTF Inhibitors in Toxic Microcystis Cyanobacteria by LC-MS Technique
Mar. Drugs 2016, 14(1), 7; https://doi.org/10.3390/md14010007 - 30 Dec 2015
Cited by 3
Abstract
The blood coagulation cascade involves the human coagulation factors thrombin and an activated factor VII (fVIIa). Thrombin and fVIIa are vitamin-K-dependent clotting factors associated with bleeding, bleeding complications and disorders. Thrombin and fVIIa cause excessive bleeding when treated with vitamin-K antagonists. In this [...] Read more.
The blood coagulation cascade involves the human coagulation factors thrombin and an activated factor VII (fVIIa). Thrombin and fVIIa are vitamin-K-dependent clotting factors associated with bleeding, bleeding complications and disorders. Thrombin and fVIIa cause excessive bleeding when treated with vitamin-K antagonists. In this research, we explored different strains of toxic Microcystis aeruginosa and cyanobacteria blooms for the probable fVIIa-soluble Tissue Factor (fVIIa-sTF) inhibitors. The algal cells were subjected to acidification, and reverse phase (ODS) chromatography-solid phase extraction eluted by water to 100% MeOH with 20%-MeOH increments except for M. aeruginosa NIES-89, from the National Institute for Environmental Studies (NIES), which was eluted with 5%-MeOH increments as an isolation procedure to separate aeruginosins 89A and B from co-eluting microcystins. The 40%–80% MeOH fractions of the cyanobacterial extract are active against fVIIa-sTF. The fVIIa-sTF active fractions from cultured cyanobacteria and cyanobacteria blooms were subjected to liquid chromatography-mass spectrometry (LC-MS). The 60% MeOH fraction of M. aeruginosa K139 exhibited an m/z 603 [M + H]+ attributed to aeruginosin K139, and the 40% MeOH fraction of M. aeruginosa NIES-89 displayed ions with m/z 617 [M − SO3 + H]+ and m/z [M + H]+ 717, which attributed to aeruginosin 89. Aeruginosins 102A/B and 298A/B were also observed from other toxic strains of M. aeruginosa with positive fVIIa-sTF inhibitory activity. The active fractions contained cyanobacterial peptides of the aeruginosin class as fVIIa-sTF inhibitors detected by LC-MS. Full article
(This article belongs to the Special Issue Marine Anticoagulants and Antithrombotics)
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Open AccessArticle
The Marine-Derived Kinase Inhibitor Fascaplysin Exerts Anti-Thrombotic Activity
Mar. Drugs 2015, 13(11), 6774-6791; https://doi.org/10.3390/md13116774 - 09 Nov 2015
Cited by 7
Abstract
Background: The marine-derived kinase inhibitor fascaplysin down-regulates the PI3K pathway in cancer cells. Since this pathway also plays an essential role in platelet signaling, we herein investigated the effect of fascaplysin on thrombosis. Methods: Fascaplysin effects on platelet activation, platelet aggregation and platelet-leukocyte [...] Read more.
Background: The marine-derived kinase inhibitor fascaplysin down-regulates the PI3K pathway in cancer cells. Since this pathway also plays an essential role in platelet signaling, we herein investigated the effect of fascaplysin on thrombosis. Methods: Fascaplysin effects on platelet activation, platelet aggregation and platelet-leukocyte aggregates (PLA) formation were analyzed by flow cytometry. Mouse dorsal skinfold chambers were used to determine in vivo the effect of fascaplysin on photochemically induced thrombus formation and tail-vein bleeding time. Results: Pre-treatment of platelets with fascaplysin reduced the activation of glycoprotein (GP)IIb/IIIa after protease-activated receptor-1-activating peptide (PAR-1-AP), adenosine diphosphate (ADP) and phorbol-12-myristate-13-acetate (PMA) stimulation, but did not markedly affect the expression of P-selectin. This was associated with a decreased platelet aggregation. Fascaplysin also decreased PLA formation after PMA but not PAR-1-AP and ADP stimulation. This may be explained by an increased expression of CD11b on leukocytes in PAR-1-AP- and ADP-treated whole blood. In the dorsal skinfold chamber model of photochemically induced thrombus formation, fascaplysin-treated mice revealed a significantly extended complete vessel occlusion time when compared to controls. Furthermore, fascaplysin increased the tail-vein bleeding time. Conclusion: Fascaplysin exerts anti-thrombotic activity, which represents a novel mode of action in the pleiotropic activity spectrum of this compound. Full article
(This article belongs to the Special Issue Marine Anticoagulants and Antithrombotics)
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