arginase/karcinóm prsníka

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The Involvement of Arginase and Nitric Oxide Synthase in Breast Cancer Development: Arginase and NO Synthase as Therapeutic Targets in Cancer.

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It is well established that, during development of malignancies, metabolic changes occur, including alterations of enzyme activities and isoenzyme expression. Arginase and nitric oxide (NO) synthase (NOS) are two of those enzymes considered to be involved in tumorigenesis. The goal of this article

Arginase activity in patients with breast cancer: an analysis of plasma, tumors, and its relationship with the presence of the estrogen receptor.

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BACKGROUND Breast cancer is an important cause of cancerrelated death in women. In this pathological condition, arginase plays a role by providing ornithine as a substrate for the biosynthesis of polyamines which are important in tumor progression. The aim of this work was to determine the arginase

Protective role of carnitine in breast cancer via decreasing arginase activity and increasing nitric oxide.

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Breast cancer remains one of the most common types of cancer. High levels of arginase and ornithine in different carcinomas may indicate their relation to cancer. Carnitine is a cofactor required for the transformation of free long-chain fatty acids into acetyl-carnitines. We have examined the

[The supernatant of 4T1 breast cancer cell culture increases arginase 1 content in ANA-1 macrophages].

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OBJECTIVE To explore the effect of the supernatant of 4T1 murine breast cancer cell culture on arginase 1 (Arg-1) in ANA-1 macrophages in vitro by simulating the microenvironment of breast cancer. METHODS The experimental ANA-1 macrophages were treated with the supernatant of 4T1 culture, and

[Usefulness of postoperative assay of arginase activity in blood serum of women after breast cancer resection].

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The usefulness of arginase test was evaluated in follow-up of patients after breast cancer resection. The arginase activity was measured in blood serum of 970 patients from January 1996 to December 2000. The arginase activity above the normal value was detected in serum of 539 (55.6%) women. Only

Proteomic identification of mitochondrial targets of arginase in human breast cancer.

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We have previously reported arginase expression in human breast cancer cells and demonstrated that the inhibition of arginase by N(ω) hydroxy L-arginine (NOHA) in MDA-MB-468 cells induces apoptosis. However, arginase expression and its possible molecular targets in human breast tumor samples and

Combined use of arginase and dichloroacetate exhibits anti-proliferative effects in triple negative breast cancer cells.

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OBJECTIVE Drug combination in cancer therapy aims to achieve synergistic therapeutic effect, reduced drug dosage, reduced drug toxicity and minimizes or delays the induction of drug resistance. In the present study, we investigated the anticancer effects of the combination of two metabolic

Effect of rosuvastatin on arginase enzyme activity and polyamine production in experimental breast cancer.

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BACKGROUND Breast cancer is the most common malignant tumour of women around the world. As a key enzyme of the urea cycle, arginase leads to the formation of urea and ornithine from L-arginine. In the patients with several different cancers, arginase has been found to be higher and reported to be a

Blocking autophagy enhanced cytotoxicity induced by recombinant human arginase in triple-negative breast cancer cells.

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Depletion of arginine by recombinant human arginase (rhArg) has proven to be an effective cancer therapeutic approach for a variety of malignant tumors. Triple-negative breast cancers (TNBCs) lack of specific therapeutic targets, resulting in poor prognosis and limited therapeutic efficacy. To

Elevated serum arginase activity levels in patients with breast cancer.

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OBJECTIVE Recently, the high activity of arginase enzyme has been observed in the sera of malignant neoplasms. In this pathogenic condition, it is said that arginase strongly inhibits lymphocyte proliferation and plays a role in providing ornithine as a substrate for biosynthesis of polyamines,

Arginase in patients with breast cancer.

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The mean arginase activity in breast cancers (n = 80) was significantly higher than in control tissues and it accounted for 0.31 +/- 0.23 U/g wet tissue and 0.083 +/- 0.061 U/g (P < 0.05), respectively. With the cutoff value of 0.1 U/g wet tissue, raised arginase activity was observed in 74% of

Arginase inhibition suppresses lung metastasis in the 4T1 breast cancer model independently of the immunomodulatory and anti-metastatic effects of VEGFR-2 blockade.

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Tumor angiogenesis promotes tumor growth and metastasis. Anti-angiogenic therapy in combination with chemotherapy is used for the treatment of metastatic cancers, including breast cancer but therapeutic benefits are limited. Mobilization and accumulation of myeloid-derived suppressor cells (MDSC)

Expression patterns of the immunomodulatory enzyme arginase 1 in blood, lymph nodes and tumor tissue of early-stage breast cancer patients.

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Arginase 1 (ARG1) is an important enzyme in amino acid metabolism that also exerts immunoregulatory function. High ARG1 expression, which is associated with cell cycle arrest and functional unresponsiveness in T cells, has been observed after trauma, infections and in cancer patients. We studied

Arginase activity in human breast cancer cell lines: N(omega)-hydroxy-L-arginine selectively inhibits cell proliferation and induces apoptosis in MDA-MB-468 cells.

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L-Arginine is the common substrate for two enzymes, arginase and nitric oxide synthase (NOS). Arginase converts L-arginine to L-ornithine, which is the precursor of polyamines, which are essential components of cell proliferation. NOS converts L-arginine to produce NO, which inhibits proliferation

Statin-induced breast cancer cell death: role of inducible nitric oxide and arginase-dependent pathways.

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Statins are widely used cholesterol-lowering drugs that selectively inhibit the enzyme 3-hydroxy-3-methylglutaryl CoA reductase, leading to decreased cholesterol biosynthesis. Emerging data indicate that statins stimulate apoptotic cell death in several types of proliferating tumor cells, including

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