DMSO inhibits human platelet activation through cyclooxygenase-1 inhibition. A novel agent for drug eluting stents?

Asmis, Lars M.; Tanner, Felix C.; Sudano, Isabella; Lüscher, Thomas F.; Camici, Giovanni G.

doi:10.1016/j.bbrc.2009.12.102

Cited by 31 publications

(21 citation statements)

References 38 publications

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“…Dimethyl sulfoxide (DMSO) of 1% was chosen as the positive control. It presumably prevents platelet activation as an inhibitor of cyclooxygenase-1 (17). …”

Section: Resultsmentioning

confidence: 99%

Antiplatelet and anti-proliferative action of disintegrin from Echis multisquamatis snake venom

et al. 2017

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AimTo purify the platelet aggregation inhibitor from Echis multisquamatis snake venom (PAIEM) and characterize its effect on platelet aggregation and HeLa cell proliferation.MethodsSodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and matrix assisted laser desorption/ionization time-of-flight (MALDI-TOF) were used for PAIEM identification. Platelet aggregation in the presence of PAIEM was studied on aggregometer Solar-AP2110. The changes of shape and granularity of platelets in the presence of PAIEM were studied on flow cytometer COULTER EPICS XL, and degranulation of platelets was estimated using spectrofluorimetry. Indirect enzyme-linked immunosorbent assay was used for the determination of target of PAIEM on platelet surface. An assay based on 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide was used to evaluate the effect of PAIEM on the proliferation of HeLa cells in cell culture.ResultsThe molecular weight of the protein purified from Echis multisquamatis venom was 14.9 kDa. Half-maximal inhibitory concentration (IC50) of PAIEM needed to inhibit adenosine diphosphate (ADP)-induced platelet aggregation was 7 μM. PAIEM did not affect thrombin- or ADP-induced platelet activation, but it did prevent binding of the anti-IIb antibody to glycoprotein IIb/IIIa (GPIIbIIIa)-receptor of adhered platelets and inhibited the viability of HeLa cells by 54%.ConclusionAs a member of the disintegrin family, PAIEM inhibited platelet aggregation and cell proliferation possibly by blocking integrin-mediated interactions. However, it did not impair cellular signaling causing any changes in platelet shape and granularity and did not affect ADP-induced platelet degranulation. This disintegrin was shown to be a potent inhibitor of integrin-mediated cellular interactions including platelet aggregation or cancer cell proliferation.

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“…Dimethyl sulfoxide (DMSO) of 1% was chosen as the positive control. It presumably prevents platelet activation as an inhibitor of cyclooxygenase-1 (17). …”

Section: Resultsmentioning

confidence: 99%

Antiplatelet and anti-proliferative action of disintegrin from Echis multisquamatis snake venom

et al. 2017

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“…Moreover, the inhibitory effect of silybin on thrombin was significantly weaker than the effect of cyanidin and quercetin. Asmis et al (2010) suggest that 0.5 % DMSO inhibits platelet response to arachidonate, but aggregation in response to other agonists (ADP, collagen, ristocentin, epinephrine, U46619) was not affected by DMSO. We also checked the effect of 0.77 % DMSO on blood platelet activity and did not observe any changes in thrombin-induced aggregation between control and DMSO treatment platelets.…”

Section: Discussionmentioning

confidence: 99%

Thrombin inhibitory activity of some polyphenolic compounds

et al. 2013

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Thrombin, also known as an active plasma coagulation factor II, belongs to the family of serine proteases and plays a crucial role in blood coagulation process. The process of thrombin generation is the central event of the hemostatic process and regulates blood coagulant activity. For this reason, thrombin inhibition is key to successful novel antithrombotic pharmacotherapy. The aim of our present study was to examine the effects of the well-known polyphenolic compounds on the activity of thrombin, by characterization of its interaction with selected polyphenols using different biochemical methods and biosensor BIAcore analyses. Only six compounds, cyanidin, quercetin, silybin, cyanin, (+)-catechin and (−)-epicatechin, of all examined in this study polyphenols caused the inhibition of thrombin amidolytic activity. But only three of the six compounds (cyanidin, quercetin and silybin) changed thrombin proteolytic activity. BIAcore analyses demonstrated that cyanidin and quercetin caused a strong response in the interaction with immobilized thrombin, while cyanin and (−)-epicatechin induced a low response. Lineweaver–Burk curves show that used polyphenol aglycones act as competitive thrombin inhibitors. Our results suggest that polyphenolic compounds might be potential structural bases and source to find and project nature-based, safe, orally bioavailable direct thrombin inhibitors.

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“…In case of ADPinduced aggregation, SSE 150 (8.0 ± 2.77%, data not shown) and 200 g/ml showed similar effects with nitroprusside 30 g/ml (6.3 ± 0.96%). Because DMSO, which we used for dissolving SSE as stock solution (100 mg/ml), was reported to have anti-aggregating effects, especially via inhibiting thromboxane production (Saeed et al, 1988;Asmis et al, 2010), it needed to be investigated whether the DMSO vehicle could show the anti-aggregating effects. Thus, we compared the effect of DMSO 0.05%, 0.1%, 0.2% and 0.4% with PBStreated control and found that there were no differences between groups (data not shown).…”

Section: Discussionmentioning

confidence: 99%

Antiplatelet effects of Spatholobus suberectus via inhibition of the glycoprotein IIb/IIIa receptor

Lee

et al. 2011

Journal of Ethnopharmacology

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DMSO inhibits human platelet activation through cyclooxygenase-1 inhibition. A novel agent for drug eluting stents?

Cited by 31 publications

References 38 publications

Antiplatelet and anti-proliferative action of disintegrin from Echis multisquamatis snake venom

Antiplatelet and anti-proliferative action of disintegrin from Echis multisquamatis snake venom

Thrombin inhibitory activity of some polyphenolic compounds

Antiplatelet effects of Spatholobus suberectus via inhibition of the glycoprotein IIb/IIIa receptor

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