Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
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Target Concepts:
Gene/Protein
Disease
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Enzyme
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Query: UNIPROT:P01034 (
cystatin C
)
3,397
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The concentration of
cystatin C
, a cysteine proteinase inhibitor, was measured during the treatment of murine LS lymphosarcoma with cyclophosphamide and
HA-1
murine hepatoma with the antitumor drug Ukrain. It was shown that concentrations of
cystatin C
were very low in both the tumor tissues studied (
HA-1
hepatoma cells and LS lymphosarcoma); increased
cystatin C
concentrations were found only in Ukrain-treated murine hepatoma, suggesting the mechanism of antitumor effect of this drug. Cyclophosphamide treatment in LS lymphosarcoma did not influence the concentration of
cystatin C
in tumor cells. At the same time, a marked increase in cathepsin B and cathepsin L activity in LS lymphosarcoma was found, indicating the involvement of apoptosis in the mechanism of antitumor action of cyclophosphamide. While the DNA from untreated LS lymphosarcoma was very homogenous and its molecular weight was high, the DNA from tumors of treated mice broke down, giving rise to the ladder figure characteristically produced by cells dying from apoptosis. Evidence was obtained that cyclophosphamide-induced tumor regression was effected by apoptosis.
...
PMID:Cystatin C in LS lymphosarcoma and HA-1 hepatoma treated with Ukrain and cyclophosphamide and involvement of apoptosis. 1134 40
Cystatin C is the best known extracellular endogenous cysteine proteinase inhibitor and has been studied as a possible index of tumor growth and as a marker of the effectiveness of antitumor therapy. The aim of this study was to evaluate
cystatin C
concentrations in murine tumor tissues (compared with other organs not directly involved with tumor development, such as the liver and spleen) during treatment with several antitumor drugs (Ukrain and/or cyclophosphane). Cystatin C concentrations in murine tissues and biological fluids was determined by enzyme-linked immunosorbent (ELISA) assay. The
cystatin C
ELISA test is a sandwich immunoassay, which uses immobilized rabbit antihuman
cystatin C
Pab and mouse antihuman
cystatin C
Mab-HRP (monoclonal antibodies, conjugated with horseradish peroxidase). We observed decreased serum
cystatin C
concentrations compared with controls in all nontreated tumor models:
HA-1
hepatoma (solid and ascitic forms), lung adenocarcinoma (solid and ascitic forms) and LS lymphosarcoma. In the ascitic fluid of mice with
HA-1
hepatoma the
cystatin C
concentration was much lower than in the serum of the same mice (about 20-fold lower). In the
HA-1
model of hepatoma cells
cystatin C
concentration decreased about 2-3-fold compared with the control (intact liver) and Ukrain significantly increased the
cystatin C
concentration. Cyclophosphane treatment of LS lymphosarcoma significantly increased the
cystatin C
concentration in serum. Cyclophosphane treatment (50 mg/kg, single injection) increased
cystatin C
by up to 8-fold more in tumor issue. Ukrain treatment of LS lymphosarcoma was also followed by increased levels of
cystatin C
in tumor tissue (4-fold); cyclophosphane plus Ukrain had a similar positive effect. In the group with LS lymphosarcoma Ukrain or cyclophosphane plus Ukrain treatment induced a significant increase in
cystatin C
concentration in liver. Liver
cystatin C
concentration decreased in the
HA-1
hepatoma group and treatment with Ukrain or carboxymethylated beta-1, 3-glucan (CMG) increased this index in both groups. Spleen
cystatin C
concentrations decreased about 5-fold in LS lymphosarcoma compared with controls and combined treatment with cyclophosphane plus Ukrain restored the index to the normal value. We can conclude that both murine tumors studied were characterized by low
cystatin C
concentrations in tumor tissues and decreased
cystatin C
concentrations (to a lesser degree) were also observed in liver and spleen as a result of the "toxic" effect of tumor bearing. Effective treatment in all cases (especially with Ukrain or a combination of cyclophosphane plus Ukrain) induced a significant increase in
cystatin C
. Obviously, the decrease in
cystatin C
concentration predominantly in tumor tissue was connected with tumor development and restoration of
cystatin C
level may be used as a marker of efficacy of antitumor therapy.
...
PMID:Cysteine proteinase inhibitor level in tumor and normal tissues in control and cured mice. 1134 42
The concentration of stefin A (cystatin A in mice) was measured in animals with experimental tumors (LS lymphosarcoma,
HA-1
-hepatoma, and Lewis lung carcinoma) during effective antitumor therapy. In mice with these tumors serum concentrations of stefin A increased, while the concentration of
cystatin C
(extracellular cystein proteinase inhibitor) decreased. The concentration of stefin A in tumor tissue in Lewis lung carcinoma was higher than in LS lymphosarcoma and
HA-1
-hepatoma ascitic cells, which can be explained by the degree of their malignancy. The content of stefin A in tumor tissue was similar to that in the liver and spleen of tumor-bearing animals, while its concentration in the liver and spleen of tumor-bearing animals was lower than in intact mice. The level of stefin A is an important marker of malignancy and an indicator of the efficiency of antitumor therapy.
...
PMID:Cystein proteinase inhibitor stefin A as an indicator of efficiency of tumor treatment in mice. 1453 8
Intact peritoneal macrophages in vitro secreted the cysteine proteinase inhibitor
cystatin C
. Polysaccharides stimulated
cystatin C
secretion: lipopolysaccharide < carboxymethylated beta-D-glucan < sulfoethylated beta-D-glucan. Human plasma low-density- (LDL) and high-density lipoproteins (HDL) are still more potent inducers of
cystatin C
secretion by macrophages. Peritoneal macrophages from mice with experimental
HA-1
hepatoma compared to those from intact mice secreted more
cystatin C
with maximum polysaccharide-stimulated secretion after 30 min of incubation. LDL and HDL induced
cystatin C
secretion by tumor macrophages also.
...
PMID:Effect of polysaccharides and human plasma lipoproteins on the secretion of cystatin C by peritoneal macrophages from normal and tumor bearing mice. 1506 96
Development of murine
HA-1
hepatoma was accompanied by increased activity of cathepsin B (in ascitic cells), cathepsin D (in ascitic fluid) and increased activity of procathepsin B. There were some changes of cysteine proteinases in liver and spleen, not involved directly into tumor growth. The most prominent changes included the decreased level of cysteine proteinase inhibitors
cystatin C
and stefin A in ascitic cells (and to a lesser degree in liver tissue). During tumor development serum
cystatin C
concentration decreased by 3-times compared to intact mice. Treatment by antitumor drug Ukraine increased life span of mice with
HA-1
hepatoma (transplanted intravenously), decreased the increment of tumor weight. In ascite such treatment caused a decrease of number of tumor cells and an increase of number of macrophages. Ukraie (administered once or 5-times in a dose of 0.5 mg per mice) increased
cystatin C
level, revealing protective mechanism of action.
...
PMID:[Cysteine proteinases and their inhibitors in the development of mouse HA-1 hepatoma and antineoplastic therapy]. 1517 24