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Titolo:
HEPATIC MERCAPTURIC ACID FORMATION - INVOLVEMENT OF CYTOSOLIC CYSTEINYLGLYCINE S-CONJUGATE DIPEPTIDASE ACTIVITY
Autore:
JOSCH C; SIES H; AKERBOOM TPM;
Indirizzi:
UNIV DUSSELDORF,INST PHYSIOL CHEM 1,POSTFACH 101007 D-40001 DUSSELDORF GERMANY UNIV DUSSELDORF,INST PHYSIOL CHEM 1 D-40001 DUSSELDORF GERMANY
Titolo Testata:
Biochemical pharmacology
fascicolo: 6, volume: 56, anno: 1998,
pagine: 763 - 771
SICI:
0006-2952(1998)56:6<763:HMAF-I>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA-MEMBRANE VESICLES; PERFUSED-RAT-LIVER; MULTIDRUG-RESISTANCE PROTEIN; GLUTATHIONE CONJUGATE; DEHYDROPEPTIDASE-I; RENAL DIPEPTIDASE; TRANSPORT; ENZYMES; KIDNEY; 1-CHLORO-2,4-DINITROBENZENE;
Keywords:
CYSTEINYLGLYCINE S-CONJUGATE; DIPEPTIDASE; GLUTATHIONE; MERCAPTURIC ACID; MONOCHLOROBIMANE; RAT LIVER PERFUSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
43
Recensione:
Indirizzi per estratti:
Citazione:
C. Josch et al., "HEPATIC MERCAPTURIC ACID FORMATION - INVOLVEMENT OF CYTOSOLIC CYSTEINYLGLYCINE S-CONJUGATE DIPEPTIDASE ACTIVITY", Biochemical pharmacology, 56(6), 1998, pp. 763-771

Abstract

The role of cysteinylglycine S-conjugate dipeptidases in the intrahepatic mercapturic acid pathway was investigated in rat liver. Subcellular compartmentation studies and liver perfusions were performed risingmonochlorobimane and bimane S-conjugates as model compounds. The major parr (over 95%) of total hepatic cysteinylglycine S-conjugate dipeptidase activity was Located in the cytosol. Lower specific activity appeared in the canalicular plasma membrane fraction. Similar hepatic localization of dipeptidase activity was seen in the guinea pig. In intact rat liver perfused with monochlorobimane, the major products were the glutathione S-conjugate (mBSG) and the cysteinylglycine S-conjugate (mBCG) in bile. Minor amounts of the cysteine S-conjugate (mBCys) and the mercapturic acid (mBNAc) were formed, indicating a limitation in further metabolism of the dipeptide S-conjugate in the biliary space. However, when the dipeptide S-conjugate was offered to the sinusoidal space in liver perfusions, substantial uptake and conversion to mBNAc was observed, and only trace amounts of the infused dipeptide appeared in bile. The data suggest that cytosolic cysteinylglycine S-conjugate dipeptidase as identified here is involved in hepatic mercapturic acidformation from sinusoidal cysteinylglycine S-conjugates. This is especially of significance for species such as guinea pig and human, in which dipeptide S-conjugates are generated in the sinusoidal domain of the liver due to the presence of high gamma-glutamyltranspeptidase activity. (C) 1998 Elsevier Science Inc.

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Documento generato il 04/12/20 alle ore 05:54:58