rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5
|
pubmed:dateCreated |
1988-4-7
|
pubmed:abstractText |
The possibility of a short-term cAMP-dependent regulation of mixed-function oxidation and of glucuronide formation was investigated in isolated mouse hepatocytes and in mouse liver microsomal membranes. N6, O2-dibutyryl cAMP (in accordance with its increasing effect on gluconeogenesis) decreased aminopyrine oxidation and p-nitrophenol conjugation in isolated hepatocytes, while the phenolphthalein conjugation remained unaltered. Similar to dibutyryl cAMP the Ca2+ ionophore A 23187 also decreased aminopyrine oxidation. In cell-free systems the phosphorylation of isolated microsomal membranes by the exogenous cAMP-dependent protein kinase was inhibitory on aminopyrine oxidation and p-nitrophenol glucuronide formation but aniline oxidation and phenolphthalein glucuronidation were not affected. The correlation between the negative cAMP-dependent control of certain processes of biotransformation and the positive cAMP-dependent regulation of gluconeogenesis is discussed.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aminopyrine,
http://linkedlifedata.com/resource/pubmed/chemical/Bucladesine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Glucuronates,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrophenols,
http://linkedlifedata.com/resource/pubmed/chemical/Phenolphthalein,
http://linkedlifedata.com/resource/pubmed/chemical/Phenolphthaleins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/p-nitrophenol glucuronide
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0006-2952
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
37
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
849-54
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:2830884-Aminopyrine,
pubmed-meshheading:2830884-Animals,
pubmed-meshheading:2830884-Biotransformation,
pubmed-meshheading:2830884-Bucladesine,
pubmed-meshheading:2830884-Calcimycin,
pubmed-meshheading:2830884-Cyclic AMP,
pubmed-meshheading:2830884-Galactosamine,
pubmed-meshheading:2830884-Gluconeogenesis,
pubmed-meshheading:2830884-Glucuronates,
pubmed-meshheading:2830884-Liver,
pubmed-meshheading:2830884-Mice,
pubmed-meshheading:2830884-Nitrophenols,
pubmed-meshheading:2830884-Phenolphthalein,
pubmed-meshheading:2830884-Phenolphthaleins,
pubmed-meshheading:2830884-Protein Kinases
|
pubmed:year |
1988
|
pubmed:articleTitle |
Cyclic AMP-dependent phosphorylation in the control of biotransformation in the liver.
|
pubmed:affiliation |
1st Institute of Biochemistry, Semmelweis University, Medical School, Budapest, Hungary.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|