Über die Entstehung und die Bedeutung der Bogenförmigen ST-Strecke,Sowie der Sog. Zwischenzacke und Ihren Zusammenhang mit der S-Achse

Zusammenfassung Die bogenförmige ST-Strecke kommt häufig, in etwa 12%der Fälle, und die Zwischenzacke selten, in 5der Fälle eines nichtausgewählten Krankenmaterials, vor. Sowohl die Entstehungsursache der bogenförmigen ST-Strecke als der Kischschen Zwischenzacke liegt in der stärkeren oder schwächeren Rechts- oder Linksdeviation der S-Achse. Die Richtung und der Grad der S-Achsendeviation wird es also bestimmen, in wie vielen und welcher Einthovenschen Ableitung die bogenförmige ST-Strecke bzw. die Zwischenzacke notwendigerweise auftreten muß. Bei S-Achsenstellungen zwischen –90°und –30°wird die ST-Strecke in Ableitung I, bei S-Achsenstellungen zwischen –30°und +30°in der I. und II., zwischen +30°und +90°in der I., II., III., zwischen +90°und +150°in der II., III. und bei den Achsenstellungen zwischen +150°und –150°in der III. Einthovenschen Ableitung bogenförmig sein. Die klinische Bedeutung der bogenförmigen ST-Strecke ist gleich mit der klinischen Bedeutung der S-Achsendeviation. Bei dem Vergleich des Herzbefundes der Kranken mit der elektrischen S-Achsenstellung können folgende Feststellungen gemacht werden: Geringergradige Linksdeviation der S-Achse, d. h. bogenförmiges ST _I sowie geringergradige Rechtsdeviation der S-Achse, d. h. ST_III kann praktisch bei pathologischem Herzbefund nicht verwertet werden. Stärkere Links- bzw. Rechtsdeviation der S-Achse, d. h. ST_I und_II bzw. ST_II und_III können im allgemeinen ebenfalls nicht verwertet werden, es ist jedoch wahrscheinlich, daß sie schon einen Übergang zu den pathologischen Befunden bilden. Während jene starken S-Achsendeviationen, wo schon in allen drei Ableitungen bogenförmiges ST besteht, meistens für das Zeichen der myokardialen Läsion betrachtet werden sollen, und zwar in erster Linie dann, wenn die positive S-Zacke in oder neben dem absteigenden Schenkel der R-Zacke gut wahrnehmbar ist.     

Adipose tissue and liver lipid metabolism in obese children: role of the body mass index and the presence of acanthosis nigricans.

AIMS: The aims of our study were to determine if insulin resistance is associated with increased plasma levels of non-esterified fatty acids (NEFA), glycerol, 3-hydroxybutyrate and triglycerides in obese children. We also studied whether the presence of acanthosis nigricans (AN) led to further alterations in the above parameters. METHODS: A total of 101 children were studied on their first visit to the paediatric endocrine clinic. Seventy-four were obese, 30 of them with AN. The remaining 27 were non-obese healthy children (control group). NEFAs, glycerol, triglycerides, 3-hydroxybutyrate, insulin, leptin, adiponectin and glucose were determined in blood samples obtained after overnight fasting. The insulin resistance index (IRI) was calculated following the homeostasis model assessment (HOMA). Data from the three groups were compared using appropriate statistical tests. RESULTS: No differences in age, sex ratio and pubertal stage were observed among the three groups. The group of children with the highest body mass index (BMI) showed higher plasma levels of insulin and leptin, higher IRI and lower plasma levels of adiponectin. As insulin and IRI increased, NEFA and 3-hydroxybutyrate decreased and triglycerides increased. When obese children were categorized by BMI, the presence of AN further exacerbated these differences. CONCLUSIONS: In obese children, insulin resistance is associated with plasma lipid alterations suggestive of both decreased adipose tissue lipolysis and hepatic beta-oxidation and increased hepatic synthesis of triglycerides. Such a metabolic condition may facilitate fat storage and hinder weight loss.     

Hepatic encephalopathy secondary to porto-systemic shunt satisfactorily treated with interventionist radiology

Hepatic encephalopathy is a reversible state of altered cognition that may occur in patients with acute or chronic liver disease or porto-systemic shunt, and in which known neurological or psychiatric signs may develop. Nitrogenated substances from intestinal digestion reach the brain without being cleared by their passage through the liver due to the presence of porto-systemic shunt. We report two cases of patients with porto-systemic shunt diagnosed with recurrent chronic hepatic encephalopathy refractory to conventional medical treatment. They were satisfactorily treated with shunt embolization using interventionist radiology techniques.     

Histamine and tryptase modulate asthmatic airway smooth muscle GM-CSF and RANTES release.

Degranulating mast cells are increased in the airway smooth muscle (ASM) of asthmatics, where they may influence ASM function. The aim of the present study was to determine whether histamine and tryptase modulate ASM cell granulocyte-macrophage colony-stimulating factor (GM-CSF) and RANTES (regulated on activation, normal T-cell expressed and secreted) release and also to examine which receptors are involved in this release. Confluent, quiescent ASM cells from asthmatic and nonasthmatic donors were treated with histamine (1 microM-100 microM) with and without histamine receptor antagonist pre-treatment, or the protease-activated receptor (PAR)-2 agonists tryptase (0.5-5 nM) and SLIGKV (100 and 400 microM). The cells were then stimulated with interleukin (IL)-1beta and/or tumour necrosis factor (TNF)-alpha (10 ng.mL(-1)) or left unstimulated for 24 h. Release of GM-CSF and RANTES was determined by ELISA and prostaglandin (PG)E(2) measured by enzyme immunoassay. Neither histamine nor tryptase induced ASM GM-CSF or RANTES secretion. However, histamine increased IL-1beta-induced GM-CSF release and markedly reduced TNF-alpha-induced RANTES release by both asthmatic and nonasthmatic cells to a similar extent, but did not modulate PGE(2) release. All changes involved activation of the histamine H1 receptor as they were partially or fully blocked by chlorpheniramine, but not ranitidine. Tryptase, via its proteolytic activity, also potentiated GM-CSF, but not RANTES, release from asthmatic and nonasthmatic ASM cells induced by both cytokines. PAR-2 involvement in the tryptase potentiation was unlikely because SLIGKV had no effect. In conclusion, mast cells, through histamine and tryptase, may locally modulate airway smooth muscle-induced inflammation in asthma.     

The R7 subfamily of RGS proteins assists tachyphylaxis and acute tolerance at mu-opioid receptors.

Members of the R7 subfamily of regulators of G-protein signaling (RGS) proteins (RGS6, RGS7, RGS9-2, and RGS11) are found in the mouse CNS. The expression of these proteins was effectively reduced in different neural structures by blocking their mRNA with antisense oligodeoxynucleotides (ODNs). This was achieved without noticeable changes in the binding characteristics of labeled beta-endorphin to opioid receptors. Knockdown of R7 proteins enhanced the potency of antinociception promoted by morphine and [D-Ala(2), N-MePhe(4), Gly-ol(5)]-enkephalin (DAMGO)-both agonists at mu-opioid receptors. The duration of morphine analgesia was greatly increased in RGS9-2 and in RGS11 knockdown mice. The impairment of R7 proteins brought about different changes in the analgesic activity of selective delta agonists. Knockdown of RGS11 reduced [D-Ala(2)]deltorphin II analgesic effects. Those of RGS6 and RGS9-2 proteins caused [D-Ala(2)]deltorphin II to produce a smoothened time-course curve-the peak effect blunted and analgesia extended during the declining phase. RGS9-2 impairment also promoted a similar pattern of change for [D-Pen(2,5)]-enkephalin (DPDPE). RGS7-deficient mice showed an increased response to both [D-Ala(2)]deltorphin II and DPDPE analgesic effects. A single intracerebroventricular (i.c.v.) ED(80) analgesic dose of morphine gave rise to acute tolerance in control mice, but did not promote tolerance in RGS6, RGS7, RGS9-2, or RGS11 knockdown animals. Thus, R7 proteins play a critical role in agonist tachyphylaxis and acute tolerance at mu-opioid receptors, and show differences in their modulation of delta-opioid receptors.