Concentration of copper and zinc in blood of psoriatic patients treated topically with ointment containing 2-chloroethyl-3-chloropropyl sulfide.

Copper and zinc concentration in plasma, erythrocytes and whole blood was determined in a group of psoriatic patients (n = 80 ) before and after treatment with an ointment (in accordance with recommendations of the Helsinki Declaration) in which 2-chloroethyl-3-chloropropyl sulfide (CLEPS) is an active compound and in a comparative group (n = 99) of clinically healthy volunteers. The performed examinations revealed a significantly lower (by 19.1%) plasma copper concentration in patients before treatment in comparison with the control group. After treatment (CLEPS) plasma copper concentration increased significantly (p < 0.001). In comparison with the control group, in erythrocytes of psoriatic patients copper concentration was higher both before and after treatment. Plasma zinc concentration in psoriatic patients was lower before treatment, whereas in erythrocytes, compared with the control group, it was higher both before and after treatment.

[Disturbances of oxidative metabolism in congestive heart failure. Possibility of pharmacologic protection]. / Zaburzenia metabolizmu tlenowego w zastoinowej niewydolnosci serca. Mozliwosci ochrony farmakologicznej.

In 20 patients with congestive heart failure, a significant increase in malonyldialdehyde (MDA) plasma concentration, decrease in GSH-Px plasma activity and decrease in selenium (Se) concentration in plasma and whole blood were found. We discussed possibility of pharmacological protection in observed oxidative metabolism disturbances.

Adenosine deaminase activity in blood of patients with stable angina pectoris.

The activity of adenosine deaminases (EC.3.5.4.4) in granulocytes and lymphocytes of patients with stable angina pectoris was lower by about 27% and 24%, respectively as compared with control group, whereas these values in erythrocytes and blood plasma were at the normal level.

5'-nucleotidase and adenosine deaminase activities in blood of patients with unstable angina pectoris.

During ischaemia and hypoxia adenosine is released from cardiac cells. Adenosine is the end product of 5'-nucleotidase activity. We were interested in how this enzyme activity in plasma of patients with unstable angina pectoris, causes short-term ischaemia. 5'-Nucleotidase activity in plasma was determined using a standard diagnostic kit from Sigma. Furthermore, we studied the activity of adenosine deaminase in plasma, granulocytes, lymphocytes and erythrocytes by the methods of Hopkinson [1]. It was found that 5'-nucleotidase activity was increased by about 43% in plasma. The activity of adenosine deaminase (ADA) in plasma increased by 6%, but in granulocytes, lymphocytes and erythrocytes decreased by about 24, 19 and 10.6%, respectively. We concluded that a large increase in 5'-nucleotidase activity may be caused by activation of 5'-ectonucleotidase in blood cells by ischaemia. However, the decrease in ADA activity in blood cells may be associate with the adenosine metabolism.

[High energy substance and late complications of diabetes]. / Zwiazki bogatoenergetyczne a pózne powiklania cukrzycy.

All the vital processes in cels are dependent on its energetic metabolism. The substances of most importance are adenine phosphates. We present update knowledge about their metabolism. We noted also importance of enzymes involved in these processes. In diabetes disturbance in energetic state of the cell are obvious. We tried to find up theoretically what is the influence of diabetes on metabolism of high energetic adenine phosphates. We present probable role of these substances in development of late complications of diabetes.

[Adenosine deaminase: isoenzymes ADA1 and ADA2]. / Deaminaza adenozyny: izoenzymy ADA1 i ADA2.

The isoenzymes ADA1 and ADA2 of the enzyme adenosine deaminase (ADA 3.5.4.4) deaminate mainly two nucleotides: adenosine and 2'-deoxyadenosine, molecules with many effects on human cells. Thus, the ADA1 and ADA2 in human cells are of extreme importance. Biochemical and biological properties of the isoenzymes ADA1 and ADA2 as well as their usefulness in diagnostic of many diseases were described.

Red blood cell superoxide dismutase and catalase activities in patients suffering from multiple sclerosis treated with adrenocorticotropic hormone.

The purpose of this study was to determine superoxide dismutase (SOD) and catalase (CAT) activities in erythrocytes of patients with multiple sclerosis treated with ACTH. SOD activity in hemolysates was determined according to the method of Misra and Fridovich and calculated as units per gram of hemoglobin (Hb). CAT activity in hemolysates was determined with Beers and Sizer's method and expressed in IU/g Hb. SOD activity in control group was (1.61 +/- 0.45) x 10(3) U/g Hb whereas, the activity of CAT amounted to (5.88 +/- 1.36) x 10(4) U/g Hb. Before the treatment, SOD activity was decreased by approximately 20% ((1.25 +/- 0.25) x 10(3) U/g Hb) while that of CAT-by about 7.7% ((5.43 +/- 0.68) x 10(4) U/g Hb) in comparison to the normal control. After treatment with ACTH, activity of both enzymes increased: SOD-by about 34.4% to (1.68 +/- 0.38) x 10(3) U/g Hb and CAT-by about 7% to (6.29 +/- 0.55) x 10(4) U/g Hb. Results of investigations showed that ACTH caused an increase in CAT and SOD activities in erythrocytes of patients after three-week treatment.

Activity of adenosine deaminase in red blood cells of patients suffering from multiple sclerosis treated with adrenocorticotropic hormone.

Adenosine deaminase (ADA) activity was studied in red blood cells of patients suffering from multiple sclerosis treated with adrenocorticotropic hormone (ACTH). ADA activity in hemolysates was determined according to the method of Hopkinson and calculated as units per g of hemoglobin. Activity of adenosine deaminase in healthy subjects was 0.871 +/- 0.251 U/g Hb. In patients with multiple sclerosis, before treatment ADA activity was 0.765 +/- 0.131 U/g Hb and was about 15.2% lower than in the control group (p < 0.02). After treatment with ACTH, ADA activity increased to 1.005 +/- 0.211 U/g Hb (p < 0.001). We have suggested that increased activity of adenosine deaminase in red blood cells of patients suffering from multiple sclerosis after treatment with ACTH is caused by diminution of superoxide generation, and therefore its sparing effect on cell membrane and enzyme is connected with membranes.

Superoxide dismutase and catalase activity in psoriatic patients treated topically with ointment containing 2-chloroethyl-3-chloropropyl sulfide.

The purpose of this study was to determine dismutase and catalase activities in erythrocytes of psoriatic patients with psoriasis vulgaris topically treated with an ointment (in accordance with recommendations of the Helsinki Declaration), in which 2-chloroethyl-3-chloropropyl sulfide (CLEPS) is an active compound. SOD activity in hemolysates was determined according to the method of Misra and Fridovich [12] and calculated as units per g of hemoglobin. CAT activity in hemolysates was determined by Beers and Sizer method [2] and expressed in U/g Hb. SOD activity in the control group was 1.61 +/- 0.48 U/g Hb x 10(3). However, the activity of CAT was 5.72 +/- 1.17 U/g Hb x 10(4). Before treatment SOD activity was decreased by ca. 22.5% (1.25 +/- 0.53 U/g Hb x 10(3)) while that of CAT by about 7% (5.30 +/- 1.41 U/g Hb x 10(4)), in comparison with the normal control. After treatment with the ointment, activity of both enzymes increased by about 18% to 1.55 x 10(3) U/g Hb and by about 16.5% to 6.25 x 10(4) U/g Hb, respectively. The results of our investigations showed that the ointment (containing mustard gas derivative) applied on psoriatic skin, causes increased of SOD and CAT activity in erythrocytes after regression of psoriatic lesions and treatment termination.

Effect of dipyridamole on inosine triphosphate pyrophosphohydrolase activity and inosine triphosphate content in fresh human erythrocytes incubated with adenosine.

The activity of inosine triphosphate pyrophosphohydrolase (ITPH) in human erythrocytes was found to be 1.50 +/- 0.39 mumol of inosine triphosphate (ITP) hydrolysed x min-1 per g Hb, and no measurable amount of ITP was detected. When dipyridamole was added to the medium composed of adenosine, pyruvate and inorganic phosphate, ITPH activity was 1.18 +/- 0.41, and at the same time ITP accumulation was 0.61 +/- 0.31 mumol/g Hb. The negative correlation between ITPH activity and accumulation of ITP was r = -0.87 at P less than 0.001.

Relationship between adenosine deaminase activity (ADA) and inosinemonophosphate (IMP) accumulation in fresh erythrocytes incubated with adenosine and dipyridamole.

Fresh human erythrocytes were incubated in two media: a) adenosine (10 mM), pyruvate (10 mM), phosphate (50 mM) (APP medium); b) APP medium enriched with 100 mumol/l dipyridamole (APPD) medium. The amount of IMP in fresh erythrocytes was 0.18 +/- 0.09 mumol/g Hb, after incubation in APP medium it was 1.52 +/- 0.78 mumol/g Hb, and after incubation in APP medium it was 1.52 +/- 0.78 mumol/g Hb, and after incubation in APPD the amount was 5.28 +/- 0.94 mumol/g Hb. ADA activity was measured simultaneously. The mean activity (+/- SD) of ADA fresh red cells was 1.29 +/- 0.36 U/g Hb, after 2 h incubation in APP medium it was 1.71 +/- 0.38 U/g Hb, and after 2 h incubation in APPD medium an activity of 2.68 +/- 0.95 U/g Hb was found. A highly significant correlation between the accumulation of IMP and the activity of ADA in fresh erythrocytes (r = 0.93; p = less than 0.001) and in erythrocytes incubated in APPD medium (r = 0.97; p = less than 0.001) was found.

Incorporation of adenosine and adenine into hypoxanthine nucleotides of fresh red blood cells.

Incorporation of adenosine and adenine into hypoxanthine nucleotides of fresh red blood cells was monitored using 8-14C-adenosine and 8-14C-adenine added to the incubation medium containing adenosine, pyruvate and inorganic phosphate (APP medium). Using 8-14C-adenosine it was shown that 21.7% of the isotope contained in the incubation medium penetrated red blood cells. Of that quantity about 50% becomes incorporated into nucleotides. Of the isotope 5.3% was found in hypoxanthine nucleotides (1.3% in ITP and 4.0% in IMP). During incubation of red blood cells in APP medium fortified with the 8-14C-adenine about 95% of isotope penetrated into cells and 60% of that quantity became incorporated into nucleotides. In hypoxanthine nucleotides only trace amounts of isotope were found (0.12% in IMP and 0.13% in ITP).

Effect of dipyridamole on adenosine incorporation into hypoxanthine nucleotides of fresh human red cells.

Fresh human red cells were incubated for 2 hours in a medium containing adenosine, pyruvate and inorganic phosphate (APP medium), or in APP medium supplemented with 10(-4) M dipyridamole (APPD medium). No measureable amount of ITP was found in fresh red cells, and the average IMP content in these cells was 0.18 +/- 0.09 mumol/g Hb. After 2 hours incubation in APP medium, the IMP content increased almost 8.5-fold to 1.52 +/- 0.78 mumol/g Hb. Under these conditions the ITP level also increased to 1.40 +/- 0.84 mumol/g Hb. After 2 hours incubation of red cells in APPD medium, the average IMP content increased to 5.30 +/- 2.33 mumol/g Hb, about 3.5 times that found in APP medium. At the same time ITP content was about 53.6% lower, that is 0.65 mumol/g Hb. In red cells incubated in APPD medium, penetration of 8-14C-adenosine decreased by 50%, and incorporation of this nucleotide into the pool of all free nucleotides also decreased by 18.2% as compared to red cells incubated in APP medium. It is concluded that IMP is probably formed directly from AMP gained by the phosphorylation of adenosine during its penetration.

Effect of dipyridamole on adenine incorporation into hypoxanthine nucleotides of fresh red blood cells.

An investigation was carried out on the penetration of [8-14C]adenine into fresh human red blood cells and of adenine incorporation into hypoxanthine nucleotides of red blood cells incubated in: 1) a medium containing adenosine, pyruvate, inorganic phosphate and NaCl, and 2) APP medium containing 1 X 10(-4) M dipyridamole (APPD medium). It was found that dipyridamole inhibits by about 45% the penetration of adenine into the red blood cells, and by 18% the incorporation of the isotope into the nucleotides of the cells under study. The inhibition of nucleotide synthesis and incorporation of the isotope into them did not apply to IMP, whose content--following erythrocyte incubation in APPD medium--increased 3.5 times, i.e. from 1.52 to 5.30 mumole/g Hb. At the same time there was an increase of the isotope count from 0.12% in IMP isolated from APP incubated erythrocytes to 0.34% in IMP synthesized in APPD incubated erythrocytes. Erythrocyte incubation in APPD medium reduced ITP synthesis by about 53% relative to its synthesis observed after erythrocyte incubation in APP medium equal to 1.40 mumole per g Hb.

Activity of inosine triphosphate pyrophosphohydrolase in fresh and stored human erythrocytes.

The accumulation of inosine triphosphate (ITP) in human erythrocytes incubated with inosine depends on the activity of inosine triphosphate pyrophosphohydrolase (ITPH). High activity of this enzyme is accompanied by a low concentration of ITP and conversely. We showed that ITPH activity decreases with the prolongation of blood preservation time. As a consequence there is a lower accumulation of ITP in fresh erythrocytes incubated in a medium containing high concentrations of inosine, pyruvate and phosphate (IPP) than in red blood cells preserved at 4 degrees C. Synthesis of ITP in erythrocytes incubated in IPP medium being so intensive, it seems possible that during incubation an intermediate accumulates which decreases ITPH activity.