ribonuclease/krebs

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Ribonuclease binase inhibits primary tumor growth and metastases via apoptosis induction in tumor cells.

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Exogenous ribonucleases are known to inhibit tumor growth via apoptosis induction in tumor cells, allowing to consider them as promising anticancer drugs for clinical application. In this work the antitumor potential of binase was evaluated in vivo and the mechanism of cytotoxic effect of binase on

Sensitivity and specificity of serum ribonuclease in the diagnosis of pancreatic cancer.

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The serum levels of a poly-[C]-specific acid ribonuclease (RNase) found in the pancreas was measured in 40 normal persons and 137 patients with pancreatic cancer, other cancers, obstructive jaundice, acute pancreatitis or chronic pancreatitis. Serum RNase increased by as much as 800 percent above

A multifunctional ribonuclease A-conjugated carbon dot cluster nanosystem for synchronous cancer imaging and therapy.

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Carbon dots exhibit great potential in applications such as molecular imaging and in vivo molecular tracking. However, how to enhance fluorescence intensity of carbon dots has become a great challenge. Herein, we report for the first time a new strategy to synthesize fluorescent carbon dots (C-dots)

Induction of 2'-5' oligoadenylate synthetase and activation of ribonuclease in tamoxifen treated human breast cancer cell lines.

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In the present study the intracellular activity of oligoadenylate synthetase and ribonuclease have been evaluated in two human breast cancer cell lines treated with tamoxifen, a well known antiestrogenic drug. Increased levels of oligoadenylate synthetase and enhanced ribonuclease activity have been

A Human Ribonuclease Variant and ERK-Pathway Inhibitors Exhibit Highly Synergistic Toxicity for Cancer Cells.

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Pancreatic-type ribonucleases (ptRNases) are prevalent secretory enzymes that catalyze the cleavage of RNA. Ribonuclease inhibitor (RI) is a cytosolic protein that has femtomolar affinity for ptRNases, affording protection from the toxic catalytic activity of ptRNases, which can invade human cells.

Elevated ribonuclease activity in the thymus and white blood cells of genetically cancer prone mice.

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Ribonuclease activity in cell-free thymus homogenates was elevated for five strains of mice genetically predisposed toward leukemia or reticulum cell neoplasms (AKR, C58, PL, RF, and SJL). Such increased activity was directed against polyuridylic acid and was observed in 8-wk old mice, well before

Ribonuclease-Activated Cancer Prodrug.

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Cancer chemotherapeutic agents often have a narrow therapeutic index that challenges the maintenance of a safe and effective dose. Consistent plasma concentrations of a drug can be obtained by using a timed-release prodrug strategy. We reasoned that a ribonucleoside 3'-phosphate could serve as a

Plant ribonucleases and nucleases as antiproliferative agens targeting human tumors growing in mice.

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The antiproliferative and antitumor effect of leaf ribonuclease was tested in vitro on the human ML-2 tumor cell line and in vivo on athymic nude mice bearing human melanoma tumors. The antiproliferative activity of this plant ribonuclease in vitro studies was negligible. In the experiments in vivo

[Why ribonucleases cause death of cancer cells].

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Molecular properties and possible mechanisms of action of cytotoxic ribonucleases (RNases), potential antitumor therapeutics, are characterized. The analysis of recent publications and own experimental results have allowed the authors, on the one hand, to distinguish cellular components that are

Bovine seminal ribonuclease induces in vitro concentration dependent apoptosis in stimulated human lymphocytes and cells from human tumor cell lines.

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Bovine seminal ribonuclease (BS RNase), a dimeric homolog of bovine pancreatic ribonuclease has been proven to have important biological properties as aspermatogenic, antitumor, embryotoxic and immunosuppressive activities. Recently we published preliminary results concerning the ability of bovine

Epidermal growth factor receptor-dependent cytotoxic effect by an EGF-ribonuclease conjugate on human cancer cell lines--a trial for less immunogenic chimeric toxin.

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Mammalian pancreatic ribonuclease (RNase) was conjugated chemically via a disulfide bond to human or murine epidermal growth factor (EGF). The conjugation between EGF and RNase was ascertained by SDS-PAGE using reduced and nonreduced conjugates. The EGF-RNase conjugate retained potent RNase activity

Ribonuclease H: a ubiquitous activity in virions of ribonucleic acid tumor viruses.

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Ten ribonucleic acid (RNA) tumor viruses grown in five different host cell species and three non-oncogenic viruses from three different virus groups have been examined for ribonuclease H content. Three different substrates were used to assay ribonuclease H: calf thymus [(3)H]RNA-deoxyribonucleic

Separation of ribonuclease H and RNA directed DNA polymerase (reverse transcriptase) of murine type-C RNA tumor viruses.

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Ribonuclease H (RNA.DNA-hybrid ribonucleotidohydrolase, EC 3.1.4.34) has been reported to copurify with reverse transcriptase (RNA directed DNA polymerase) of RNA tumor viruses. In addition, viral specific ribonuclease H and reverse transcriptase of avian type-C viruses are thought to be part of the

[Analysis of gene expression of ribonuclease inhibitor in human breast cancer tissue].

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OBJECTIVE Ribonuclease inhibitor (RI), which is rich in human placenta, is a multi-functional acidic glycoprotein. Our previous studies showed that the growth of some solid tumors (S180 sarcoma, Ca761 breast cancer, and H22 hepatoma) could be significantly inhibited by RI extracted and purified from

Effect of wheat leaf ribonuclease on tumor cells and tissues.

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The antiproliferative and antitumor effect of wheat leaf ribonuclease was tested in vitro on the human ML-2 cell line and in vivo on athymic nude mice bearing human melanoma tumors. The antiproliferative activity of this plant ribonuclease was negligible in comparison with bovine seminal

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