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1
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Does chronic ethanol administration have influence on pancreatic regeneration in the course of caerulein induced acute pancreatitis in rats

100%
Rydzewska G., Jurkowska G., Dzieciol J., Faszczewska A., Wroblewski E., Gabryelewicz A.
Journal of Physiology and Pharmacology
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2001
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tom 52
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nr 4,2
This study was undertaken in order to determine the influence of chronic ethanol administration on pancreatic regeneration during acute pancreatitis (AP). Rats were pair fed with isocaloric diet containing or not ethanol. After 8 weeks of such feeding AP was induced by sc injection of caerulein (Cae). 6 h, 24 h and 5 days after first Cae dose pancreatic weight, amylase, chymotrypsin, protein, RNA, DNA contents were determined and phosphatidic acid (PA) production in isolated pancreatic acini was measured. Proliferating cells were quantified by immunochemical staining of cells incorporating bromodeoxyuridine (BrdU). Results: Pancreatic weight was significantly higher at 6 h after first Cae injection in both, ethanol fed (EF) and control groups (C), however at 24 h pancreatic weight did not differ from prior to AP induction in EF rats. Ethanol feeding (EF) did not influence significantly protein, chymotrypsin and amylase content in pancreatic tissue in groups with AP. In EF rats RNA content after 5 days of AP was higher than in control animals. Total DNA content in EF rats with AP was lower 6 h after AP induction, earlier than in control animals with AP. Immunochemistry showed higher labelling index for BrdU after 6 h, 24 h and 5 days of AP in EF rats. In contrast to this findings, in EF animals, AP induction was not able to stimulate further PA accumulation. Conclusion: We conclude that chronic ethanol feeding, while inhibiting PA accumulation in comparison to control group, does not impair pancreatic tissue regeneration during the early phase of Cae-induced AP. Stimulation of regenerative/reparative processes in EF rats during Cae-induced AP seems to be even more pronounced than in the control group.
2

The effect of alloxydim on phospholipase activity in root tips of wheat cv Kadett

84%
Banas W., Stenlid G., Klocek J., Banas A., Stymne S.
Biological Bulletin of Poznań. Supplement
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1997
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tom 34
3
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Phospholipase D mediated transphospatidylation as a possible new pathway of ethanol metabolism in isolated rat pancreatic acini

67%
Rydzewska G., Jurkowska G., Gabryelewicz A.
Journal of Physiology and Pharmacology
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1996
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tom 47
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nr 2
4
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Pancreatic regeneration after chronic ethanol feeding in rats

67%
Rydzewska G., Jurkowska G., Wroblewski E., Faszczewska A., Gabryelewicz A.
Journal of Physiology and Pharmacology
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1999
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tom 50
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nr 2
5

Prostaglandin E [dmPGE2] action in vitro on the activity of rat liver Golgi apparatus galactosyltransferase

67%
Kordowiak A. M., Tomecki J., Procyk K., Kapusta P.
Acta Biochimica Polonica
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1993
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tom 40
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nr 4
In vitro addition of 16,16'-dimethyl prostaglandin E2 to Golgi-rich membrane fraction in final concentration of 0.1 ng/1 mg of protein increased generally the activity of galactosyltransferase in comparison with control. The percentage of phospholipids in the whole fraction was similar in both investigated groups, only the sum of phosphatidylethanolamine + phosphatide acid was significantly lower after addition of dmPGE2 than in the control (0.001
6

Regulation of wound-responsive calcium-dependent protein kinase from maize (ZmCPK11) by phosphatidic acid

59%
Klimecka M., Szczegielniak J., Godecka L., Lewandowska-Gnatowska E., Dobrowolska G., Muszynska G.
Acta Biochimica Polonica
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2011
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tom 58
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nr 4
In plant cells, phospholipids are not only membrane components but also act as second messengers interacting with various proteins and regulating diverse cellular processes, including stress signal transduction. Here, we report studies on the effects of various phospholipids on the activity and expression of maize wound-responsive calcium-dependent protein kinase (ZmCPK11). Our results revealed that in leaves treated with n-butanol, a potent inhibitor of phosphatidic acid (PA) synthesis catalyzed by phospholipase D, a significant decrease of ZmCPK11 activity was observed, indicating contribution of PA in the kinase activation. Using lipid binding assays, we demonstrate that among various phospholipids only saturated acyl species (16 : 0 and 18 : 0) of phosphatidic acid are able to bind to ZmCPK11. Saturated acyl species of PA are also able to stimulate phosphorylation of exogenous substrates by ZmCPK11 and autophosphorylation of the kinase. The level of ZmCPK11 autophosphorylation is correlated with its enzymatic activity. RT-PCR analysis showed that transcript level of ZmCPK11 in maize leaves increased in response to PA treatment. The influence of PA on the activity and transcript level of ZmCPK11 suggests an involvement of this kinase in a PA-mediated wound signal transduction pathway.
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