Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019829 (Hodgkin's disease)
 30,247 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The kinetic properties of the if channel in shortened sheep Purkinje fibres were investigated using a two-micro-electrode voltage-clamp technique in the presence of Ba2+, Mn2+ and tetrodotoxin (TTX). The time course of the hyperpolarization-activated if currents (DiFrancesco, 1981 b) at potentials within the activation range was found to depend on whether the channel was switching 'on' or 'off'. At potentials positive to the half-activation point if decay was faster than if onset; at potentials negative to the half-activation point if onset was faster than if decay. The time courses of if onset and decay become similar only at potentials close to the centre of the activation range. If a single exponential was fitted to the time course of if switching, the time constant (tau y) was found to vary as a function of potential from approximately 50 msec to several seconds. The tau y - voltage relation is an extremely steep bell-shaped distribution. Reducing external Na+ (range 140-17.5 mM) did not alter the voltage dependence of the if time course. Increasing external K+ (range 5-60 mM) shifted the if time constants and activation curve by similar amounts in a depolarizing direction. The temperature dependence of if was investigated over the range 27.5-41 degrees C. Cooling reversibly slowed the time course of if activation with a Q10 of 3.13 (S.D. +/- 0.85, n = 62). A reversible reduction in the slope of the fully-activated current-voltage relation was observed on cooling, the Q10 being 1.35 (S.D. +/- 0.07), and was usually accompanied by a small depolarizing shift of the half-activation point and the reversal potential Ef. It is concluded that the if time course shows a marked potential dependence and does not obey Hodgkin-Huxley kinetics. Its temperature dependence resembles that of if in the sino-atrial node (DiFrancesco & Ojeda, 1980).
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PMID:The kinetics and temperature dependence of the pace-maker current if in sheep Purkinje fibres. 687 38

The levels of copper, zinc, calcium, manganese and magnesium have been monitored in the sera of patients suffering from various types of cancer. Only serum copper appeared to be of any diagnostic significance, its levels being above the normal reported range in the breast cancer, leukaemia and Hodgkin's lymphoma patients. In the case of breast cancer, serum copper is progressively elevated according to the stage of the disease. Serum calcium levels were also significantly lower in patients with tumours of the breast, gastrointestinal tract and cervix. The results suggest that serum copper levels could be of prognostic significance in breast cancer patients receiving radiotherapy.
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PMID:The serum levels of some trace and bulk elements in cancer patients. 705 45

The activation marker CD30 is expressed on the cell surface of the malignant cells in Hodgkin's disease and a few non-Hodgkin lymphomas. We have analyzed the regulation of membrane-bound CD30 and found that the binding of a variety of anti-CD30 antibodies induced down-regulation of CD30 on cell lines. In addition, such down-modulation was also observed after treatment of the cell surface proteins with the sulfhydryl reagent iodoacetamide or after stimulation of the second messenger pathway with phorbol ester or calcium ionophore. This modulation was abolished at 4 degrees C and strongly inhibited by chelators like EDTA or 1,10-phenanthroline, whereas EGTA, a selective inhibitor of Ca(2+)-dependent proteinases and other inhibitors of serine, thiol and acid proteinases, showed no effect. The down-modulation was strengthened by Zn2+ or Cd2+, but not by other divalent cations such as Fe2+, Mn2+, Mg2+, Ca2+ or Co2+, thus indicating the involvement of a zinc metalloproteinase in CD30 modulation which can be activated by protein kinase C and by alkylation of sulfhydryl groups. Pulse-chase experiments, analysis of the CD30 glycosylation and specific measurement of the 90-kDa soluble form of CD30 (sCD30) with a sandwich radioimmunoassay revealed that CD30 down-modulation results from enhanced release of 90-kDa sCD30 by the site-specific cleavage of CD30 accomplished by a zinc metalloproteinase. This release occurs at the cell membrane without prior endocytosis.
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PMID:A zinc metalloproteinase is responsible for the release of CD30 on human tumor cell lines. 759 Dec 96


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