Pharmacodynamic parameters of anticoagulants based on sulfated polysaccharides from marine algae

Дрозд, Н. Н.; Tolstenkov, A. S.; Makarov, V. A.; Кузнецова, Т. А.; Беседнова, Н. Н.; Шевченко, Н. М.; Zvyagintseva, T. N.

doi:10.1007/s10517-006-0426-3

Cited by 21 publications

(13 citation statements)

References 10 publications

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“…Rajapakse and colleagues [57] characterized a 12.01 kDa single-chain monomeric protein from the marine yellowfin sole ( Limanda aspera ) which inhibited the blood coagulation serine endopeptidase factor XII (IC 50 <1 μM) by forming an inactive complex, and also triggered platelet aggregation by binding to a membrane glycoprotein integrin. Drozd and colleagues [58] extended the pharmacology of the fucoidans (24) from the marine algae Fucus evanescens and Laminaria cichorioides, showing that these sulfated polysaccharides inhibited both thrombin and factor Xa with potency comparable to non-fractioned and low-molecular weight heparins, although with considerable variability attributed to the “degree of sulfation and various types of glycoside bonds”. Luppi and colleagues [59] reported the purification and structural characterization of an unusual low-sulfated heparin (25) from the marine Italian bivalve mollusk Callista chione that decreased anti-factor Xa and activated partial thromboplastin time activity (IC 50 =52–97 IU/mg), probably as the result of a specific decrease in sulfation at position 2 of the uronic acid units.…”

Section: Marine Compounds With Anthelmintic Antibacterial Anticomentioning

confidence: 99%

Marine pharmacology in 2005–6: Marine compounds with anthelmintic, antibacterial, anticoagulant, antifungal, anti-inflammatory, antimalarial, antiprotozoal, antituberculosis, and antiviral activities; affecting the cardiovascular, immune and nervous systems, and other miscellaneous mechanisms of action

Mayer

Rodrı́guez

Berlinck

et al. 2009

Biochimica et Biophysica Acta (BBA) - General Subjects

277

141

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BACKGROUND-The review presents the 2005-2006 peer-reviewed marine pharmacology literature, and follows a similar format to the authors' 1998-2004 reviews. The preclinical pharmacology of chemically characterized marine compounds isolated from marine animals, algae, fungi and bacteria is systematically presented.RESULTS-Anthelminthic, antibacterial, anticoagulant, antifungal, antimalarial, antiprotozoal, antituberculosis and antiviral activities were reported for 78 marine chemicals. Additionally 47 marine compounds were reported to affect the cardiovascular, immune and nervous system as well as possess anti-inflammatory effects. Finally, 58 marine compounds were shown to bind to a variety of molecular targets, and thus could potentially contribute to several pharmacological classes. SIGNIFICANCE-Continued preclinical and clinical research with marine natural products demonstrating a broad spectrum of pharmacological activity and will probably result in novel therapeutic agents for the treatment of multiple disease categories. CONCLUSIONS-Marine

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Section: Marine Compounds With Anthelmintic Antibacterial Anticomentioning

confidence: 99%

Marine pharmacology in 2005–6: Marine compounds with anthelmintic, antibacterial, anticoagulant, antifungal, anti-inflammatory, antimalarial, antiprotozoal, antituberculosis, and antiviral activities; affecting the cardiovascular, immune and nervous systems, and other miscellaneous mechanisms of action

Mayer

Rodrı́guez

Berlinck

et al. 2009

Biochimica et Biophysica Acta (BBA) - General Subjects

277

141

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“…Commercial lyophilized human plasma (Renam) was used. Specific antithrombin (antifactor IIa; aIIa) and antifactor Xa (aXa) activities were calculated from calibration curves of International Reference Specimens of nonfractionated/low molecular weight heparins 5 and 1 [2].…”

Section: Methodsmentioning

confidence: 99%

“…Rocket biospecific electrophoresis of the test solutions was carried out at voltage gradient of 10 V/cm on glass plates in 1% agarose gel containing protamine sulfate [2]. Specimens of the studied preparations were put into 3-4 mm wells (0.31-5.00 µg).…”

Section: Methodsmentioning

confidence: 99%

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Inhibition of thrombin and factor Xa by Fucus evanescens fucoidan and its modified analogs

et al. 2008

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Specimens of fucoidan extracted from Fucus evanescens were purified from protein and polyphenols, deacetylated and depolymerized by fucoidanase for evaluation of their biological activity. Deacetylation did not modify the capacity of fucoidan to inhibit thrombin and factor Xa, while purification from protein and polyphenols reduced this capacity. Depolymerization of fucoidan increased its capacity to inhibit thrombin mainly through heparin cofactor II. All the studied specimens formed complexes with protamine sulfate.

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“…They have been found in many types of organisms from sponges [43,44], to algae [45,46], to sea cucumbers [47,48], fish [49] and clams [50]. It should be noted that all these marine natural products are sulfates.…”

Section: Marine Derived Protease Inhibitorsmentioning

confidence: 99%

Proteases: Nature’s Destroyers and the Drugs that Stop Them

Veltri¹

2015

PPIJ

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Proteases are found in all life forms and regulate many cellular pathways. Proteases have been proven as viable drug targets. This paper reviews the mechanism of hydrolysis of the amino acid based aspartic, cysteine, serine and threonine proteases and will also highlight the current anti protease therapeutics in the clinic. the oxygen of the carbonyl drive the cleavage of the peptide bond, which abstracts hydrogen from the general base. Water then releases the second half of the product from the active site residue. The oxyanion hole generated during the transition state is stabilized through hydrogen bonding with amino groups of the backbone. The role of the oxyanion hole is not fully understood [18]. While the chemistry of the mechanism of hydrolysis is similar for serine, aspartic, cysteine and threonine proteases, the amino acids involved in catalysis are what define the various classes. The different classes of proteases are discussed below. Serine ProteasesSerine proteases [19][20][21] use an active site serine to hydrolyze a peptide bond. The other amino acids involved in catalysis vary between the different serine protease groups. The Ser-His-Asp triad can be replaced with Ser-His-Glu, Ser-His-His or Ser-Lys depending on the family of serine protease [20,21]. The serine proteases are categorized by tertiary structures into the super families of the trypsin-like or subtilisin-like [2,19,20]. Examples of the trypsin-like serine proteases, the larger of the super families, are trypsin, chymotrypsin, thrombin, factor IX a, and factor Xa [2,19,20]. Interestingly, some cysteine proteases adopt the trypsin-like structure [22]. Examples of the subtilisin-like serine proteases are proteinase K and thermitase [2,19,20]. Proteases: Nature's Destroyers and the Drugs that Stop Them 3/11Copyright: ©2015 Veltri Citation: Veltri CA (2015) Proteases: Nature's Destroyers and the Drugs that Stop Them. Pharm Pharmacol Int J 2(6): 00044. DOI: 10.15406/ ppij.2015.02.00044Along with tertiary structure, serine proteases are designed against the nature of the P 1 residue recognized by the protease types. The trypsin-like proteases cleave positively charged residues (Lys or Arg are preferred at P 1 ), elastase-like proteases prefer small hydrophobic residues (Ala or Val are preferred at P 1 ) while chymotrypsin-like proteases prefer large hydrophobic residues (Phe, Tyr, or Leu) [2,19,20]. Aspartic ProteasesAspartic proteases [19,[23][24][25][26] use two aspartic acid residues to hydrolyze a peptide bond. These proteases are categorized into the super families of pepsin-like or viral retropepsin-like due to the tertiary structure [23,24,26,27]. The pepsin-like include pepsin, cathepsin D and chymosin [23,27]. The viral retropepsinlike include the retro pepsins of the immune viruses HIV, FIV and SIV [24,26].Aspartic proteases are unique in the fact they do not have a His residue in their active site. The general acid-base mechanism proposed for peptide hydrolysis involves two Asp residues and uses water to attack the targe...

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Pharmacodynamic parameters of anticoagulants based on sulfated polysaccharides from marine algae

Cited by 21 publications

References 10 publications

Inhibition of thrombin and factor Xa by Fucus evanescens fucoidan and its modified analogs

Proteases: Nature’s Destroyers and the Drugs that Stop Them

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