Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-7-9
pubmed:abstractText
The oxidative metabolism of xenobiotics is effected mainly by cytochrome P450 enzymes (CYP), which are expressed as a family of genetically related enzymes primarily in hepatocytes. The pancreas is among the extrahepatic tissues expressing CYP, and it has been suggested that intermediates generated by them might be of pathogenetic significance for diseases of the pancreas such as chronic pancreatitis. We studied 10 surgical resection specimens by immunohistochemistry with polyclonal antibodies against recombinant human CYP 1A1, 1A2, 2C9, 2E1, and 3A and used tissues from 11 normal pancreata as controls. In addition, we assayed microsomal preparations for their capacity to metabolize verapamil. In normal pancreata weak to moderate expression of all enzymes was demonstrated immunohistochemically in up to 50% of duct epithelia, acinar cells, and islet cells. In contrast, in chronic pancreatitis an up-regulation was observed, with immunohistochemical positivity in some cases in up to 100% of duct epithelia and acinar cells. The oxidative capacity of microsomal preparations from chronic pancreatitis was higher than that of preparations obtained from control tissues; compared to liver microsomes, however, it was low. The up-regulation of CYP may have pathogenetic significance for chronic pancreatitis. Yet considering the pancreas' capacity for conjugation reactions, conceivably low levels of reactive intermediates could effectively undergo inactivation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0885-3177
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
521-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9598815-Adult, pubmed-meshheading:9598815-Aged, pubmed-meshheading:9598815-Aryl Hydrocarbon Hydroxylases, pubmed-meshheading:9598815-Chronic Disease, pubmed-meshheading:9598815-Cytochrome P-450 CYP1A2, pubmed-meshheading:9598815-Cytochrome P-450 CYP2E1, pubmed-meshheading:9598815-Cytochrome P-450 Enzyme System, pubmed-meshheading:9598815-Female, pubmed-meshheading:9598815-Humans, pubmed-meshheading:9598815-Immunohistochemistry, pubmed-meshheading:9598815-Male, pubmed-meshheading:9598815-Microsomes, pubmed-meshheading:9598815-Middle Aged, pubmed-meshheading:9598815-Oxidation-Reduction, pubmed-meshheading:9598815-Pancreas, pubmed-meshheading:9598815-Pancreatitis, pubmed-meshheading:9598815-Steroid 16-alpha-Hydroxylase, pubmed-meshheading:9598815-Steroid Hydroxylases, pubmed-meshheading:9598815-Up-Regulation, pubmed-meshheading:9598815-Verapamil
pubmed:year
1998
pubmed:articleTitle
Up-regulation of cytochrome P450 1A2, 2C9, and 2E1 in chronic pancreatitis.
pubmed:affiliation
Department of Clinical Pharmacology, Institute of Pharmacology and Toxicology, University of Rostock, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't