Ewa Ochwanowska

The Jan Kochanowski University in Kielce, Kielce, Swietokrzyskie, Poland

Are you Ewa Ochwanowska?

Claim your profile

Publications (11)5.59 Total impact

  • Source
    Ewa Ochwanowska, Bożena Witek, Adam Kołątaj
    [Show abstract] [Hide abstract]
    ABSTRACT: The experiment was carried out on 20 Swiss male mice divided into experimental (E, n=10) and control (C, n=10) group. E mice were intraperitoneally injected with glucagon (15 μg/kg b.w.) twice daily for eight days, while mice C with 250 μl 0.9% NaCl/mouse (to exclude the injection effect only). In the lysosomal fraction of the liver the activities of acid phosphatase, β-N-acetyl-hexosaminidase, β-glucuronidase, β-glucosidase, lysosomal arylesterase, lysosomal lipase, leucine aminopeptidase and alanine aminopeptidase were determined. Glucagon caused an increase of activity of all studied enzymes except β-glucuronidase and β-glucosidase, where reduced activities were observed. KEY WORDS: adaptation / glucagon / glucose / lysosomal enzymes / mice Endocrine pancreatic functions in the course of diabetes were a subject of numerous studies [Cryer 2008, Henkel et al. 2005]. The lysosomal enzymes are important in the cell degradation processes [Beaujouin and Liaudet-Coopman 2008, Minazaki et al. 2008, Witek et al. 2007, 2008]. The participation of lysosomal enzymes in glucagon-induced autophagocytosis was first suggested by Ashford and Porter [1962]. It has been found that the formation of autophagic vacuoles after glucagon treatment in vivo was accompanied by an increase in fragility and osmotic sensitivity of lysosome membranes [De Duve and Wattiaux 1966, Deter and De Duve 1967].
    Animal Science Papers and Reports Institute of Genetics and Animal Breeding. 01/2009; 27:371-375.
  • Source
    Bożena Witek, Ewa Ochwanowska, Adam Kołątaj
    [Show abstract] [Hide abstract]
    ABSTRACT: The investigations were conducted on 20 Swiss male mice, fed a feed containing 16% (control group, n=10) or 10% protein (experimental group, n=10). After 14 days of feeding, sections of liver and kidneys were obtained from all animals and homogenized in order to obtain the lysosomal fraction, in which the activity of the following enzymes was determined: acid phosphatase, lysosomal esterase, lysosomal lipase, β-glucuronidase, β-galactosidase, β-glucosidase, β-N-acetyl-hexosaminidase, leucine aminopeptidase, alanine aminopeptidase and cathepsins D and L. Feed with the protein level reduced to 10% had, compared to the control, a significant and differentiated effect on the activity of enzymes examined, depending on the enzyme type and organ.
    Animal Science Papers and Reports Institute of Genetics and Animal Breeding. 01/2008; 26:153-159.
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Observing the changes of activity of some lysosomal enzymes in blood serum of female rabbits subjected to injection of 10 microg of ghrelin/kg of body weight. In the blood serum the activity of cathepsins D and L, alanine aminopeptidase, acid phosphatase, lysosomal lipase and lysosomal esterase was determined. As a result of ghrelin injection the activity of all the enzymes examined in blood serum increased markedly. Changes of lysosomal enzymes activities in the blood serum caused by the effects of ghrelin should be regarded as the response of the lysosomal system.
    Neuro endocrinology letters 09/2005; 26(4):397-400. · 0.93 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: MALDI-TOF mass spectrometry, 1H NMR spectrometry, the continuous variation method and molecular modeling by MM3 calculation confirmed our earlier studies showing that gonadotropin-releasing hormone (GnRH) forms complex with copper(II) ion with the binding ratio 1:1. The copper(II) complex formed at physiological pH has a square planar configuration and GnRH complexes with nickel(II) and cobalt(II) ions are less stable than that of copper(II).
    Neuro endocrinology letters 07/2005; 26(3):247-52. · 0.93 Impact Factor
  • Neuroendocrinology Letters. 02/2004;
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Changes in the activity of alanine aminopeptidase, leucine aminopeptidase and cathepsins D and L in the liver and kidney of male and female of mice, injected with 0.4 IU/kg b.w. insulin for 4 and 8 days. The homogenates of the liver and kidney were taken for examination. The activity of alanine aminopeptidase, leucine aminopeptidase and cathepsins D and L has been determined according to [1] method. The activity of alanine aminopeptidase, leucine aminopeptidase, cathepsins D and L in the liver and kidney of male and female of mice decreased in effect of insulin injections for 4 and 8 days. The changes of enzyme activities showed a stimulating effect of the insulin injection on the labilization of lysosomal membranes. The range of the reaction remained in a relationship with the kind of the organ, the type of enzyme, time over which insulin introduced operates in the organism, and with the sex.
    Neuro endocrinology letters 01/2004; 25(1-2):83-6. · 0.93 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Changes in the activity of cathepsin D and L, alanine aminopeptidase, leucine aminopeptidase, N-acetyl-beta-glucosaminidase, lysosomal arylesterase and lysosomal lipase in the liver and kidney of unselected and selected mice, subjected to 7.5 mg/kg b.w. of hydrocortisone injection for 4 and 8 days. The homogenates of the liver and kidney were subjected to differentiated centrifuging and determination of studied enzymes. Injection of hydrocortisone caused an increase in the activity of all investigated lysosomal enzymes in the liver and kidney of mice. The reactions of selected mice were stronger in comparison with unselected ones. The highest increase in the activity investigated enzymes was observed after 8 days of hydrocortisone injection.
    Neuro endocrinology letters 05/2002; 23(2):105-8. · 0.93 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: The study was carried out on fifty male rabbits of the New Zealand White breed. Diabetes was caused by a single, intravenous alloxan injection. Rabbits which had glycaemia 7th day after the alloxan administration higher than 11 millimol/litre were selected for the studies. They were divided into 5 groups: I - control (without diabetes); II - 3-week diabetes; III - 6-week diabetes; IV - 3-month diabetes; V - 6-month diabetes. In control and experimental rabbits the activity of beta-glucuronidase, N-acetyl-beta-glucosaminidase, lysosomal acid phosphatase, leucine aminopeptidase, cathepsin D, and lysosomal arylesterase was determined in lysosomal fractions of the liver and kidney. Alloxan caused lowering of the activity of all the investigated enzymes in the kidney and liver except lysosomal arylesterase. Alloxan injection caused a significant increase in the activity of all the investigated enzymes. The advisable lysosomal enzymes may be useful for the monitoring of the course and effectiveness of diabetes therapy.
    Neuro endocrinology letters 09/2001; 22(4):238-42. · 0.93 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Changes in the activity of beta-glucuronidase, N-acetyl-beta-glucosaminidase, cathepsin D and L, alanine aminopeptidase and lysosomal acid lipase in lysosomal fractions of the liver and kidneys of mice, which were administered 20 mg/kg b.w. of exogenous melatonin (N-acetyl-5-methoxytryptamine) for 7 and 14 days were investigated. The slices of the liver and kidney were homogenized in 0.1M phosphate buffer, pH 7.0. Homogenates were subjected to differentiated centrifuging and determination of studied enzymes. Melatonin caused lowering of the activity of all the investigated lysosomal enzymes in the liver and kidney. Administration of melatonin was caused the lowering of the activity of the investigated lysosomal enzymes in comparison with values in control groups.
    Neuro endocrinology letters 07/2001; 22(3):181-5. · 0.93 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: OBJECTIVES: Changes in the activity of β-glucuronidase, N-acetyl-β- glucosaminidase, cathepsin D and L, alanine aminopeptidase and lysosomal acid lipase in lysosomal fractions of the liver and kidneys of mice, which were administered 20 mg/kg b.w. of exogenous melatonin (N-acetyl-5-methoxy- tryptamine) for 7 and 14 days were investigated. METHODS: The slices of the liver and kidney were homogenized in 0. 1M phosphate buffer, pH 7.0. Homogenates were subjected to differentiated centrifuging and determination of studied enzymes. RESULTS: Melatonin caused lowering of the activity of all the investigated lysosomal enzymes in the liver and kidney. CONCLUSION: Administration of melatonin was caused the lowering of the activity of the investigated lysosomal enzymes in comparison with values in control groups.
  • AGATA GRANICZKA, EWA OCHWANOWSKA, ADAM KO
    [Show abstract] [Hide abstract]
    ABSTRACT: Witek B., Graniczka A., Ochwanowska E., Ko‡"taj A. Changes of the lysosomal enzyme activity in the liver and kidney of mice after glucagon injections Summary Changes in the activity of b-glucuronidase, N-acetyl-b-glucosaminidase, cathepsin D and cathepsin L in the liver and kidney of mice, injected intraperitonealy with 15 µg/kg b.w. of glucagon were investigated. The experiment was carried out on 24 8-week-old mice, whose parents were chosen from random match. The homogenates of the liver and kidney were subjected to differentiate centrifuging, and in the lysosomal fractions of the liver and kidney the activities of b-glucuronidase (b-GlcUr), N-acetyl-b-glucosaminidase (NAG), cathepsin D (Cath. D), and cathepsin L (Cath. L) were estimated. Injection of glucagon caused a decrease in the activity of b-glucuronidase in the liver and kidney, cathepsin L in the liver, N-acetyl-b-glucosaminidase in the kidney, and an increase cathepsin D and cathepsin L in the kidney of mice. The results suggest that exogenous glucagon had a significant influence on the activity investigated lysosomal enzymes. The range of the reaction remained in a relationship with the kind of the organ and type of enzyme.