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: EC:3.2.1.26 (
invertase
)
4,927
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The release by glycyl-L-phenylalanine 2-naphthylamide (Gly-L-Phe-2-NNap) of endocytosed
invertase
associated with the MLP fraction (sum of the M, L and P fractions [de Duve, Pressman, Gianetto, Wattiaux & Appelmans (1955) Biochem. J. 63, 604-617]) of rat liver was investigated and compared with the release of
cathepsin C
. The percentage of
invertase
released increases with time after the enzyme injection, whereas the release of
cathepsin C
is not influenced by this treatment and corresponds to 85-90% of the total activity of the enzyme. It takes about 2h to attain a similar release of both enzymes. The quantity of
invertase
releasable or not by Gly-L-Phe-2-NNap was plotted against the time after the injection. Results agree well with the hypothesis that unreleasable
invertase
is associated with a pre-lysosomal compartment, whereas releasable
invertase
is present in lysosomes. A kinetic analysis indicates that
invertase
enters the pre-lysosomal compartment with a zero-order rate constant of 0.48 unit/min per g fresh wt., and leaves this compartment with a first-order rate constant of 0.042 min-1.
...
PMID:Effect of glycyl-L-phenylalanine 2-naphthylamide on invertase endocytosed by rat liver. 397 51
The oligomeric structure and the residual propeptide are distinct characteristics of
cathepsin C
from other members in the papain superfamily. In this study, we examined the physiological role of the
cathepsin C
propeptide. The stable overexpression of
cathepsin C
propeptide significantly decreased the activities of intestinal alkaline phosphatase (IAP) and
sucrase
in human Caco-2 intestinal epithelial cells, whereas it did not change the proliferation and
cathepsin C
activity. The overexpression of
cathepsin C
propeptide significantly decreased the amounts of IAP protein in differentiated Caco-2 cells, compared with the transfection of mock vector, whereas the amounts of IAP transcripts were not changed. Pulse-chase analysis confirmed that the reduction in IAP activity was due to an increase in IAP degradation, but not a decrease in IAP expression. For the mechanism of the enhanced IAP degradation, we identified proteins interacting with
cathepsin C
propeptide in Caco-2 cells by immunoprecipitation and mass spectrometry. Cathepsin C propeptide interacted with proteins with a molecular mass of approximately 70 kDa, including IAP and heat shock cognate protein 70. Our present results suggest that the propeptide of
cathepsin C
may stimulate the sorting to the lysosome, at least in part, contributing to the degradation of IAP in Caco-2 cells.
...
PMID:Cathepsin C propeptide interacts with intestinal alkaline phosphatase and heat shock cognate protein 70 in human Caco-2 cells. 1830 34
