Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Isolated perfused liver and cultures of rat hepatocytes were assessed for the quantitative evaluation of hepatotoxicity. Release of de novo biosynthesized plasma proteins and acid hydrolases into perfusion or culture media was taken as an indication of the integrity of hepatocytes in both systems. The activities of six acid hydrolases, alpha-L-fucosidase, alpha-D-galactosidase, beta-D-galactosidase, beta-D-N-acetylgalactosaminidase, beta-D-N-acetylglucosaminidase, and cathepsin D, were assayed in collagenase-segregated hepatocytes and in monolayer cultures of rat liver cells obtained via collagenase perfusion of rat liver. In situ, liver perfusion with collagenase led to a loss of 45 +/- 5% of the total acid hydrolase activity in the mitochondrial-lysosomal pellet of the liver cells with concomitant increase of these enzymes in the cytosol. In monolayer cultures over a period of 30 h, increased activity of cathepsin D, beta-D-galactosidase, and beta-D-N-acetylglucosaminidase in the mitochondrial-lysosomal pellet and the cytosol fraction was evident with concurrent biosynthesis of plasma proteins. The use of radioactive tracing techniques with the isolated perfused liver revealed that the rate of catabolism of intracellular protein was approximately 5 times that of plasma protein synthesis. Both methods described here are suitable for the study of the effects of toxins on the function of hepatocytes.
 ...
PMID:Study of hepatotoxicity in isolated perfused liver versus cultures of rat hepatocytes. 291 36

Germanium complexes (IV) with succinic (H2Suc), oxyethyliminodiacetic (H2Oeida) and iminodisuccinic (H4Ids) acids as well as homo- and heteroligand germanium complexes (IV)--products of interaction of triammonium salt of oxyethylidendiphosphonic acid ((NH4)3HL) and oxyacids: tartaric (H4Tart), citric (H4Citr), trioxyglutaric (H4Toglut) acids have been synthesized. Composition of the obtained complexes: [Ge(OH)2(NaSuc)2].2H2O (I); [Ge(OH) (Oeida).H2O].H2O (II); [Ge(OH)2(NaHIds)2] (III); [Ge(OH)2(NH4)3HL) (H2Tart)] (IV); [Ge(OH)2(NH4)3HL) (H2Citr)] (V); [Ge(OH)2(NH4)3HL) (H2Toglut)] (VI); [Ge(OH)2((NH4)2HL)2] (VII); [Ge (OH)2((NH4)2HL)2] (VII); [Ge(OH)2 (H2O)2(NH4) HL] (VIII) has been determined. The capability of the synthesized compounds has been studied to affect synthesis and activity of the following enzymes: collagenase, alpha-N-acetylgalactosaminidase (alpha-GalNAc-ase) and alpha-galactosidase (alpha-Gal-ase). It has been established that the complexes II-VIII activate biosynthesis of alpha-Gal-ase and alpha-GalNAc-ase, while germanium dioxide (IX) and complex I possess considerable inhibiting effect on synthesis of the above enzymes. It has been also established that all the compounds except for IV increased the activity of both alpha-Gal-ase and alpha-GalNAc-ase. All the considered complexes demonstrated similar reaction with respect to collagenase: they inhibited both synthesis and activity.
 ...
PMID:[Effect of coordinational germanium compounds on enzyme synthesis and activity]. 1243 65