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Kaempferide-7-O-(4"-O-acetylrhamnosyl)-3-O-rutinoside reduces myocardial infarction size after coronary artery ligation in rats.

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Kaempferide-7-O-(4"-O-acetylrhamnosyl)-3-O-rutinoside (A-F-B) is a novel flavonoid extracted from the leaves of Actinidia kolomikta. We recently reported that A-F-B administration could improve lipid profiles. A-F-B actions are associated with regulating the activities of PAP and HMG-CoA reductase

Neuroprotective effects of Kaempferide-7-O-(4″-O-acetylrhamnosyl)-3-O-rutinoside on cerebral ischemia-reperfusion injury in rats.

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In the present study, we aim to evaluate the potential neuroprotective effect and the underlying mechanism of Kaempferide-7-O-(4″-O-acetylrhamnosyl)-3-O-rutinoside (A-F-B) against cerebral I/R injury. Adult male rats were pretreated with A-F-B by intragastric administration once a day for 3 days.

Combination of chemical fingerprinting with bioassay, a preferable approach for quality control of Safflower Injection.

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Safflower Injection is one kind of injections derived from traditional Chinese medicine. It is widely applied to treat cerebrovascular diseases such as acute cerebral infarction, stroke, coronary heart disease, and angiitis. However, most adverse reactions of Safflower Injection in clinic are caused

Protective effects of anthocyanins against brain ischemic damage.

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Anthocyanins are considered as bioactive components of plant-based diets that provide protection against ischemic cardiovascular pathologies by mechanisms dependent on their antioxidant and reductive capacities. However, it is not clear whether similar anthocyanin-mediated mechanisms can provide

Neuroprotective effect of kaempferol glycosides against brain injury and neuroinflammation by inhibiting the activation of NF-κB and STAT3 in transient focal stroke.

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BACKGROUND Ischemic brain injury is associated with neuroinflammatory response, which essentially involves glial activation and neutrophil infiltration. Transcription factors nuclear factor-κB (NF-κB) and signal transducer and activator of transcription 3 (STAT3) contribute to ischemic

Inhibition of Protein Disulfide Isomerase in Thrombosis.

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This MiniReview addresses our current understanding of the mechanisms by which protein disulfide isomerase (PDI) mediates thrombus formation and discusses the potential of blocking thrombosis by targeting PDI. Thiol isomerases are ubiquitous oxidoreductases primarily localized to the endoplasmic

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