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l asparaginase/neoplasms
Länken sparas på Urklipp
Sida 1 från 263 resultat
Therapy of refractory adult acute lymphoblastic leukemia with vincristine and prednisone plus tandem methotrexate and L-asparaginase. Results of a Cancer and Leukemia Group B Study.
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Methotrexate (MTX) and L-asparaginase (ASP) are effective agents in the treatment of acute lymphoblastic leukemia (ALL). The effects of combining MTX and ASP are schedule dependent. To investigate this schedule dependency, the Cancer and Leukemia Group B (CALGB) employed vincristine and prednisone
Effects of L-asparaginase on plasma amino acid profiles and tumor burden in cats with lymphoma.
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BACKGROUND
L-Asparaginase (Elspar(a)), is an Escherichia coli-derived enzyme that depletes lymphoma cells of asparagine, inhibiting protein synthesis and resulting in cell death. The single agent response rate in cats with lymphoma and impact of L-asparaginase on plasma amino acid concentrations is
A phase II clinical trial of polyethylene glycol-conjugated L-asparaginase in patients with advanced ovarian cancer: Early closure for safety.
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The anti-angiogenic activity of L-asparaginase (L-ASP) and the sensitivity of ovarian cancer cell lines to L-ASP has been previously demonstrated by preclinical findings. The aim of this clinical trial was to translate those findings and evaluate the activity of polyethylene glycol-conjugated
A pharmacoeconomic analysis of pegaspargase versus native Escherichia coli L-asparaginase for the treatment of children with standard-risk, acute lymphoblastic leukemia: the Children's Cancer Group study (CCG-1962).
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OBJECTIVE
The purpose of this pharmacoeconomic analysis was to compare pegaspargase. a newer chemotherapeutic agent used for treating acute lymphoblastic leukemia, with native Escherichia coli L-asparaginase in induction, delayed intensification 1 and delayed intensification 2.
METHODS
A subset of
L-Asparaginase as a single agent in acute lymphocytic leukemia: survey of studies form Childrens Cancer Study Group.
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A series of studies were undertaken by the Childrens Cancer Study Group between 1968 and 1972 to evaluate the optimum schedule and dosage of L-asparaginase as a single agent in induction and maintenance of children with previously treated acute lymphocytic leukemia. Six different dosages of enzyme
L-Asparaginase: human toxicology and single agent activity in nonleukemic neoplasms.
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The early hope that L-asparaginase would be a breakthrough in medical treatment, with selective toxic effects based on the qualitative presence or absence of a specific enzyme (asparagine synthetase), has not been realized. Despite its failure to live up to early hopes, L-asparaginase is now
[Progress in researches on anti-tumor agent L-asparaginase for treatment of leukemia].
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L-asparaginase is a very effective anti-tumor agent. To take the most advantage of enzyme treatment method, the natural L-asparaginase could be chemically modified, entrapped or immobilized into/onto other carriers. The extracorporeal shunt system with immobilized enzyme reactor deserves to receive
Phase II study with sequential L-asparaginase and methotrexate in advanced refractory breast cancer.
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The combination of sequential L-asparaginase and methotrexate (MTX) was evaluated in 33 patients with advanced refractory breast cancer. There were nine partial responses and one complete response, giving an overall response rate of 30% and a median duration of response of 8 months. Five of 17
Selective reduction in glutaminase activity of l‑Asparaginase by asparagine 248 to serine mutation: A combined computational and experimental effort in blood cancer treatment.
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Type II l‑asparaginase (l‑ASNase) is an FDA approved enzyme drug with extensive applications for treatment of certain blood cancers. However, the therapeutic efficiency of this enzyme is hampered by its undesirable glutaminase activity. Given the pivotal role of this enzyme against cancer, designing
Assessment of l-Asparaginase Pharmacodynamics in Mouse Models of Cancer.
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l-asparaginase (ASNase) is a metabolism-targeted anti-neoplastic agent used to treat acute lymphoblastic leukemia (ALL). ASNase's anticancer activity results from the enzymatic depletion of asparagine (Asn) and glutamine (Gln), which are converted to aspartic acid (Asp) and glutamic acid (Glu),
Bacterial l-asparaginases for cancer therapy: Current knowledge and future perspectives.
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l-Asparaginases hydrolyzing plasma l-asparagine and l-glutamine has attracted tremendous attention in recent years owing to remarkable anticancer properties. This enzyme is efficiently used for acute lymphoblastic leukemia (ALL) and lymphosarcoma and emerged against ALL in children, neoplasia, and
A phase I and pharmacodynamic evaluation of polyethylene glycol-conjugated L-asparaginase in patients with advanced solid tumors.
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OBJECTIVE
To evaluate the in vitro activity of polyethylene glycol-conjugated L-asparaginase (PEG-Lasparaginase) against fresh human tumor specimens, using the human tumor clonogenic assay (HTCA), and to perform a phase I dose-escalation clinical trial of PEG-L-asparaginase. The goal of the clinical
l-asparaginase induces intrinsic mitochondrial-mediated apoptosis in human gastric adenocarcinoma cells and impedes tumor progression.
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l-asparagine essentially regulates growth and proliferation of cancer cells. l-asparaginase is an anti-cancer enzyme that deprives the cancer cells of l-asparagine. The purpose of this study was to explore the mechanism of a novel l-asparaginase from Pseudomonas fluorescens on l-asparagine
Optimizing the dosing schedule of l-asparaginase improves its anti-tumor activity in breast tumor-bearing mice.
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Proliferation of acute lymphoblastic leukemic cells is nutritionally dependent on the external supply of asparagine. l-asparaginase, an enzyme hydrolyzing l-asparagine in blood, is used for treatment of acute lymphoblastic leukemic and other related blood cancers. Although previous studies
[Antitumor activity of L-asparaginase from Erwinia carotovora from against different leukemic and solid tumours cell lines].
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We have studied dose- and time-dependent antitumor and cytotoxic effects of Erwinia carotovora L-asparaginase (ECAR LANS) and Escherichia coli L-asparaginase (MEDAC) on human leukemic cells and human and animal solid tumor cells. We determined the sensitivity of tumor cells to L-asparaginases, as
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