PubMed Health⌕ Search

SEARCH · PubMed Health

Results for “Cations, Divalent”

Explore indexed PubMed citations for clinical trials, systematic reviews and public health research. Read source abstracts and follow each citation to its original PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 415 records · Page 23Linked to original sources
PubMed1989

Effects of divalent cations on snake venom cardiotoxin-induced hemolysis and 3H-deoxyglucose-6-phosphate release from human red blood cells.

At a low concentration of Naja naja kaouthia cardiotoxin (3 microM) Ca2+, Sr2+ and Ba2+ (2 mM), had little to no effect on 3H-deoxyglucose-6-phosphate (3H-dGlu-6-p) or hemoglobin release. At higher concentrations of N. n. kaouthia cardiotoxin (greater than or equal to 10 microM), Ca2+ (2 mM), but not Sr2+ or Ba2+, significantly enhanced 3H-dGlu-6-p and hemoglobin release. Mn2+ (2 mM) almost completely inhibited 3H-dGlu-6-p release and hemolysis at both the 3 microM and 10 microM concentrations of cardiotoxin. At a fixed concentration of N. n. kaouthia cardiotoxin (3 microM). Ca2+ at low concentrations (0.5 mM) enhanced 3H-dGlu-6-p and hemoglobin release, but at higher concentrations caused a dose-dependent inhibition of cardiotoxin action. The cardiotoxin from N. n. kaouthia venom (3 microM) induced 3H-dGlu-6-p release and hemolysis release with similar time courses and to similar extents. 3H-dGlu-6-p release induced by cardiotoxin was greatly enhanced as the pH of the medium was increased from 7.0 to 8.5. Similarities between 3H-dGlu-6-p and hemoglobin release do not support opening of pores in the plasmalemma of all red blood cells as the mode of action of cardiotoxins, but suggests that complete lysis of a subpopulation of cells occurs. Cardiotoxins have two components of lysis, only one of which is Ca2+-dependent. The Ca2+-dependent lysis is only evident at higher cardiotoxin concentrations and is likely due to trace phospholipase A2 contamination in the toxin fraction. Mn2+ is an effective antagonist of cardiotoxin action.

Barium↗
PubMed1988

Effects of calcium chelators, divalent cations and sulfhydryl reagents on calcium uptake and motility of bovine spermatozoa.

Addition of 1 mM Ca/EGTA complex (1:1 ratio) to an incubation medium containing 1.5 mM Ca2+ produced a notable increase in the Ca2+ cycling in ejaculated bovine spermatozoa. Similar results were also obtained with the Ca/EDTA and Ca/EDTA complexes or with the heavy metal chelator DTPA (50 microM). Ba2+, Ni2+ or Co2+ added at 0.1 mM concentration abolished the stimulatory effect of the Ca/EGTA complex on Ca2+ cycling, whereas it did not affect the calcium movement in the absence of the calcium chelator complex. It is concluded that small amounts of these cations should be bound to the plasma membrane of bovine spermatozoa and inhibit the cellular calcium influx. 0.1 mM Cd2+ and NEM or 1 mM diamide produced a calcium efflux from the spermatozoa together with an inhibition of cellular motility and an increase in glutamate-oxaloacetate transaminase release. Conversely the impermeant sulfhydryl reagent mersalyl caused a net calcium efflux but did not alter the cellular motility nor the transaminase release. It is suggested that the permeant thiol reagents could decrease the spermatozoal mobility by impairing the mitochondrial ATP-synthesis.

Animals↗
PubMed1984

Divalent cations: do they stabilize the agonist (12S) form of the mu opioid receptor?

In rabbit cerebellum membranes, millimolar concentrations of Mn++ ions while slightly reducing the Kd of 3H-etorphine counteract, to a large extent, sodium inhibition of equilibrium binding of the tritiated agonist to the mu opioid receptor. In digitonin extracts of membranes which have been incubated either with 3H-etorphine or with 3H-diprenorphine in the presence of Mn++ ions, recovery of radioligand bound to the agonist form of the receptor (sedimenting at position 12S) is substantially increased while, at the same time, recovery of radioligand bound to the antagonist form of the receptor (10S) is markedly reduced. Taken together these results suggest that Mn++ ions stabilize the agonist (12S) form of the mu opioid receptor. Mn++ ions may do so by promoting association of the receptor and of a guanine nucleotide regulatory protein.

Animals↗
PubMed1985

Hyaluronic acid-complement interactions--II. Role of divalent cations and gelatin.

Native hyaluronic acid (HA) is reported to be a weak anticomplementary agent. However, the normal buffer systems used for complement tests incorporate gelatin, Ca2+ and Mg2+, which may bind to HA, influence its conformation and interfere with its anticomplementary reactions with complement components such as Cl. In this study, metal ions (Ca2+ and Mg2+), gelatin and fibronectin appeared to react with native HA preparations and block their anticomplementary effects on Cl. In previous studies, we obtained evidence for a relationship between reversible heat-induced HA conformational changes and a subsequent reversible increase in anticomplementary activity. The anticomplementary activity of heat-treated HA preparations was also reduced by gelatin.

Binding Sites↗
PubMed1985

An unexpected effect of divalent cations on the adenovirus endogenous protein kinase: alteration in the specificity of phosphorylation.

The adenovirus endogenous protein kinase specifically phosphorylates capsid protein IIIa in the presence of Mg2+, utilizing either ATP or GTP as a phosphate donor. When Mn2+ is substituted for Mg2+, in the presence of ATP, phosphorylation of IIIa is enhanced by 2-3 fold. However, in addition to IIIa phosphorylation, the core proteins V and VII are now phosphorylated. A similar finding is made when Co2+ is used instead of Mg2+. Further, when Mn2+ or Co2+ is substituted for Mg2+, the phosphoamino acid residue profile is changed, viz., instead of only phosphoserine being labeled, phosphothreonine is now extensively labeled. These results are specific for the above endogenous viral proteins, since when the viral protein kinase is used to phosphorylate added exogenous substrates such as casein, no enhancement of phosphorylation nor any change in phosphoamino acid profile is achieved by substituting Mn2+ for Mg2+. It is thus likely that MnATP or CoATP somehow interacts differently with adenovirus structural proteins than does MgATP and this facilitates their accessibility to the enzyme.

Adenosine Triphosphate↗
PubMed1983

The effect of divalent cations on Cloudman melanoma cells.

The effect of Ca2+, Cd2+, Cu2+, Mg2+ and Zn2+ as acetates (10(-3) - 10(-5)M) and of 2% DMSO on the proliferation and differentiation of clone M3 of the Cloudman S91 mouse melanoma was studied and compared with the behaviour of GPK (keratocyte) and MRC5 (fibroblast) cell lines. Whereas neither calcium nor magnesium ions influenced the proliferation of the cells as measured by [3H]-thymidine incorporation, absorbance at 280 nm of NaOH cell digests and cell counts, cadmium, zinc and copper ions selectively inhibited the melanoma line. Cd2+ (10(-5)M) and Zn2+ (10(-4)M) were selectively cytotoxic to melanoma cells in contrast to keratocytes and fibroblasts. No direct effect of the cations on melanogenesis, as estimated from the ratio of absorbance at 350 nm and 280 nm and by tyrosinase assays, was demonstrated. DMSO stimulated melanogenesis in melanoma cells but inhibited their growth. Experiments with ouabain indicate that active transport is involved in the uptake of zinc by melanoma cells.

Animals↗
PubMed1990

Divalent cations effectively replace Ca2+ and support bradykinin induced noradrenaline release.

Bradykinin (BK), a nonapeptide acting at the B2-type BK-receptor, and depolarization with high KCl (50 mM), induce catecholamine secretion in pheochromocytoma cells (PC-12). The mechanism underlying the BK-induced release, which is absolutely Ca2(+)-dependent, is not yet understood. Alkaline metals, barium (Ba2+), strontium (Sr2+) and other metal cations, manganese (Mn2+) or lanthanum (La3+), support BK-induced [3H]noradrenaline ([3H]NA) release. The extent of supporting transmitter release is dependent upon the specificity of the extracellular cation, with rank order potency of: Ba2+ greater than Sr2+ greater than Ca2+ greater than Mn2+La3+. The same rank order potency was observed for supporting both BK- and K(+)-induced release. [3H]NA release in the presence of Ba2+ or Sr2+ was much greater than in the presence of Ca2+, and unlike with Ca2+ was not saturable at the highest concentration measured. La3+ and Mn2+ were significantly less effective than Ca2+ at supporting release. These results strongly suggest that extracellular Ca2+ entry is essential for release, and that BK mediates release via a receptor-operated Ca2+ channel.

Adrenal Gland Neoplasms↗