[How to approach the patient with supraventricular tachycardia in the EP lab: A systematic overview]. / Diagnostik bei supraventrikulären Tachykardien : Wie ist das Vorgehen im elektrophysiologischen Labor?

The term supraventricular tachycardia (SVT) summarizes those tachycardias involving the atrial myocardium along with the atrioventricular (AV) node. The prevalence is about 2.25 per 1000 (without atrial fibrillation and atrial flutter) and, therefore, SVT represents one of the most common group of arrhythmias besides atrial fibrillation encountered in the emergency department especially since they tend to recur until definite therapy. The clinical symptoms may include palpitations, anxiety, presyncope, angina, and dyspnea. Pharmacological therapy of these arrhythmias often fails. The present article deals with the differential diagnosis of SVT and also introduces a series of manuscripts that provide detailed insight into the differential diagnosis and treatment of these arrhythmias.

In vitro function of S rnases in Lycopersicon peruvianum.

S RNases are products of the S locus that are expressed in the stylar tissue of Lycopersicon peruvianum with the gametophytic self-incompatibility (SI) system. Two S RNases (S12 and Sa) with RNase activity from the S12Sa genotype of L. peruvianum were purified using gel filtration and cation-exchange chromatography. The molecular masses of the two RNases, S12 and Sa, were 21 and 23.1 kDa, respectively. The specific activities of S12 and Sa for torula yeast rRNA as a substrate were 8,500 and 6,000 units/ml, respectively. Of various reagents tested for RNase activities, ZnSO4 and CuSO4 were found to remarkably reduce its activity. The growth of S12Sa pollen was inhibited when it was cultured in a pollen germination medium that contained the purified S12 RNase. The result suggested that the S RNase was either a probable inhibitor of pollen growth or controlled pollen growth. Additionally, 512Sa pollens germinated well in vitro in a germination medium that contained S12 RNase in the presence of ZnSO4 and CuSO4. Our finding suggests that the treatment of S RNase with its inhibitor destroys the SI ability on an in vitro self-pollen growth test.

Inhibition of phospholipase C gamma 1 activity by amentoflavone isolated from Selaginella tamariscina.

Amentoflavone was isolated as an inhibitor of phospholipase C gamma 1 (PLC gamma 1) and phosphoinositides (PI)-turnover in PLC gamma 1 overexpressing NIH3T3 fibroblasts (NIH3T3 gamma 1) from Selaginella tamariscina (Selaginellaceae) together with other related biflavonoids, isocryptomerin and cryptomerin B. Only amentoflavone inhibited the PLC gamma 1 activity with an IC50 of 29 microM and the formation of total inositol phosphates (IPt) in PDGF-stimulated NIH3T3 gamma 1 with an IC50 of 9.2 microM but did not show inhibitor activity against protein kinase C. Isocryptomerin and cryptomerin B did not show inhibitor activity against PLC gamma 1 at the concentration of 150 microM, and did not inhibit IPt production in PDGF-induced NIH3T3 gamma 1 at the concentration of 180 microM.

Antihepatotoxic activity of icariin, a major constituent of Epimedium koreanum.

In an attempt to identify compounds with antihepatotoxic activity, carbon tetrachloride-induced cytotoxicity in primary cultured rat hepatocytes has been adopted as a screening system. Using this screening system, an antihepatotoxic compound from the aerial parts of Epimedium koreanum has been isolated. This compound, icariin, is a flavonol glycoside. Its antihepatotoxic activity was first evaluated by measuring the release of glutamic pyruvic transaminase and sorbitol dehydrogenase from CCl4-intoxicated rat hepatocytes into the culture medium. Icariin significantly reduced the level of glutamic pyruvic transaminase and sorbitol dehydrogenase released resulting in a 76% protection from toxicity at concentration ranges from 1 microM to 20 microM. The antihepatotoxic activity of icariin was also estimated by the determination of total cytochrome P-450 content and glutathione-S-transferase activity in the CCl4-intoxicated hepatocytes.