Preventive role of gallic acid on alcohol dependent and cysteine protease-mediated pancreas injury.
In order to investigate an association between alcohol consumption and lysosomal cysteine protease induced pancreatic injury and preventive effect of gallic acid as dose-dependent, we determined myeloperoxidase and malondialdehyde levels, serum amylase activities and cathepsin B and L activities in the cytosolic and lysosomal fractions of pancreatic tissue in the ethanol (8 g/kg) and ethanol plus gallic acid (at different doses 50, 100 and 200 mg/kg) given rats. Absolute ethanol (8 g/kg) was given by oral gavage. Gallic acid was dissolved in the saline (2 ml/kg) and administered before 30 min the oral administration of ethanol. Pancreatic myeloperoxidase and also malondialdehyde levels and serum amylase activities were measured. Besides, histological investigations were made. Cathepsin B activities in the cytosolic fraction were decreased by gallic acid (200 mg/kg) and increased in ethanol given rats. Cytosolic/lysosomal ratio of cathepsin B and L were found to be low in the all doses of gallic acid as compared to ethanol group. Serum amylase, pancreatic myeloperoxidase activities and malondialdehyde levels in the ethanol group were higher than in the control group. These were not statistically significant for myeloperoxidase and malondialdehyde. Also, our histopathologic results indicated that ethanol administration increased pancreatic tissue injury. Gallic acid especially at 200 mg/kg improved ethanol-mediated pancreatic tissue damage.In conclusion, gallic acid treatments were decreased release of lysosomal cathepsin B and L enzymes into cytoplasmic fraction and prevented alcohol mediated pancreatic tissue injury. Preventive effect of gallic acid might be dose-dependent.
Department of Biochemistry, Faculty of Medicine, Osmangazi University, Eskisehir 26480, Turkey.
Güngör
G
Kanbak
Mediha
M
Canbek
Ayşegül
A
Oğlakçı
Kazim
K
Kartkaya
Hakan
H
Sentürk
Gökhan
G
Bayramoğlu
Cengiz
C
Bal
Burak
B
Göl
Ayşe
A
Ozmen
D061354:Acinar Cells / Q000187:drug effects / Q000378:metabolism / Q000473:pathology; D000681:Amylases / Q000097:blood; D000818:Animals; D002401:Cathepsin B / Q000378:metabolism*; D056668:Cathepsin L / Q000378:metabolism*; D003600:Cytosol / Q000201:enzymology; D000431:Ethanol; D005260:Female; D016166:Free Radical Scavengers / Q000008:administration & dosage* / Q000494:pharmacology; D005707:Gallic Acid / Q000008:administration & dosage* / Q000494:pharmacology; D008247:Lysosomes / Q000201:enzymology; D008315:Malondialdehyde / Q000378:metabolism; D010179:Pancreas / Q000187:drug effects / Q000201:enzymology / Q000473:pathology; D019512:Pancreatitis, Alcoholic / Q000097:blood / Q000139:chemically induced / Q000201:enzymology / Q000517:prevention & control*; D009195:Peroxidase / Q000378:metabolism; D051381:Rats; D017207:Rats, Sprague-Dawley
D016166:Free Radical Scavengers; D000431:Ethanol; D008315:Malondialdehyde; D005707:Gallic Acid; D009195:Peroxidase; D000681:Amylases; D002401:Cathepsin B; C533916:Ctsb protein, rat; D056668:Cathepsin L; C534280:Ctsl protein, rat