Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UMLS:C0019204 (
hepatocellular carcinoma
)
71,386
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
To determine the cause of the increased content of carbohydrate-bound phosphate in tumour lysosomal hydrolases, the activity and kinetics in human
hepatocellular carcinoma
of two enzymes involved in the formation of mannose-6-phosphate in lysosomal hydrolases UDP-GlcNAc: lysosomal enzyme GlcNAc alpha l-phosphotransferase (GlcNAc-phosphotransferase) and
phosphodiester glycosidase
were studied. The activity level of the phosphotransferase with artificial and natural substrates was elevated (P less than 0.025 and P less than 0.001, respectively) in
hepatoma
compared to that in uninvolved tissue, while the
phosphodiester glycosidase
of
hepatoma
was at a level similar to that of the uninvolved tissue. To verify a previous observation that cathepsin D of human
hepatoma
contained increased GlcNAc-phosphomannose, the protease was examined for carbohydrate phosphorylation by the GlcNAc-phosphotransferase. The protease from normal human liver was much more phosphorylated than
hepatoma
protease, confirming the previous observation. The predominant phosphorylation of the protease occurred in one of two major heavy subunits, with some phosphorylation in one of two minor light subunits.
...
PMID:Elevated carbohydrate phosphotransferase activity in human hepatoma and phosphorylation of cathepsin D. 164 48
Two enzymes (N-acetylglucosamine-1-phosphotransferase and
phosphodiester glycosidase
) involved in formation of mannose-6-phosphate at lysosomal hydrolases were studied for the activity and kinetics in human
hepatocellular carcinoma
. The activity level of the phosphotransferase with an artificial substrate was elevated (p less than 0.025) in
hepatoma
compared to that in normal liver, while the
phosphodiester glycosidase
of
hepatoma
was in a similar level with that of control. The elevation was more remarkable with a physiological substrate, cathepsin D. (P less than 0.001). Since cathepsin D from normal liver was previously demonstrated to contain less phosphomannose compared to the
hepatoma
protease, the protease was investigated for carbohydrate phosphorylation by the phosphotransferase. The liver protease was much more phosphorylated than the
hepatoma
protease, endorsing the previous observation. The predominant phosphorylation of the protease occurred in heavy subunit.
...
PMID:[Carbohydrate phosphotransferase in human hepatoma and phosphorylation of cathepsin D]. 217 73
