The effects of various statins on platelet aggregation in blood samples from normal and diabetic rabbits were measured. All of the statins used in our study inhibited platelet aggregation by about 20% at 1 microM. Our results show that diabetes increased the rate of platelet aggregation from 48 +/- 5% to 72 +/- 8%, however, statins inhibited the rate of platelet aggregation by about 60% (p < 0.01). The addition of leptin (125 ng/ml) to blood samples from healthy rabbits increased the aggregation rate to about 64%, but statins decreased this rate to about 26%. Our results indicate that diabetes increases the rate of platelet aggregation in rabbits and increases antiplatelet efficacy of statins due to interactions with leptin.
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http://dx.doi.org/10.1016/s1734-1140(10)70282-6 | DOI Listing |
Vopr Pitan
January 2025
Ufa University of Science and Technology, 450076, Ufa, Russian Federation.
The most common mechanism of the development of cardiovascular diseases is atherosclerosis, caused by genetic predisposition, hyperlipidemia, inflammation and metabolic disorders. Statins used in medicine inhibit endogenous cholesterol synthesis, but are characterized by diabetogenic effect, development of intolerance in 9.1%, and muscle symptoms in 10-25% of patients.
View Article and Find Full Text PDFJ Cardiothorac Surg
January 2025
School of Medicine, American University of the Caribbean, Cupecoy, Sint Maarten.
Myocardial Injury after Noncardiac Surgery (MINS) is an increasingly recognized complication that significantly impacts postoperative morbidity and mortality. Characterized by elevated cardiac troponin levels without overt ischemic symptoms, MINS presents a challenge in perioperative care. This review article explores the epidemiology, etiology, and management of MINS, with a particular focus on prevention and the latest management strategies.
View Article and Find Full Text PDFJ Neurosurg Anesthesiol
January 2025
Department of Neurology, Neurocritical Care Division, University of Pennsylvania, Philadelphia, PA.
Minimally invasive, image-guided endovascular procedures are becoming increasingly prevalent as techniques and technologies have advanced, particularly within the realm of neurovascular interventions. Endovascular approaches ubiquitously result in endothelial injury with subsequent risk of thromboembolic complications. Periprocedural antiplatelet agent use is an integral component of the management of patients undergoing endovascular neurointerventional procedures.
View Article and Find Full Text PDFPlatelets
December 2025
Cyrus Tang Medical Institute, The Fourth Affiliated Hospital of Soochow University, Collaborative Innovation Center of Hematology, State Key Laboratory of Radiation Medicine and Prevention, Soochow University, Suzhou, China.
Recent studies have shown that anti-ERp5 antibodies inhibit platelet activation and thrombus formation; Moreover, ERp5-deficient platelets exhibit enhanced platelet reactivity via regulation of endoplasmic reticulum (ER) stress. In this study, we used a new ERp5-knockout mouse model as well as recombinant ERp5 (rERp5) protein, to examine the role of ERp5 in platelet function and thrombosis. Although platelet-specific ERp5-deficient mice had decreased platelet count, the mice had shortened tail-bleeding times and enhanced platelet accumulation in FeCl-induced mesenteric artery injury, compared with wild-type mice.
View Article and Find Full Text PDFBiochimie
January 2025
Laboratory of Applied Toxinology, Center of Toxins, Immune-Response and Cell Signaling (CeTICS), Butantan Institute, São Paulo, Brazil. Electronic address:
PA-BJ is a serine protease present in Bothrops jararaca venom that triggers platelet aggregation and granule secretion by activating the protease-activated receptors PAR-1 and PAR-4, without clotting fibrinogen. These receptors also have a relevant role in endothelial cells, however, the interaction of PA-BJ with other membrane-bound or soluble targets is not known. Here we explored the activity of PA-BJ on endothelial cell receptor, cytoskeleton, and coagulation proteins in vitro, and show the degradation of fibrinogen and protein C, and the limited proteolysis of actin, EPCR, PAR-1, and thrombomodulin.
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