Induction of leukotriene production by bleomycin and asparaginase in mast cells in vitro and in patients in vivo

Geuenich, S.; Haberl, C.; Egger, Dietmar; Kaspers, Uwe; Hültner, Lothar; Wilmanns, W.; Denzlinger, Claudio

doi:10.1016/s0006-2952(97)00481-4

Cited by 15 publications

(10 citation statements)

References 18 publications

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“…These conditions result from direct release of inflammatory mediators, such as leukotrienes and prostaglandins [9]. Leukotriene release from mast cell degranulation has been previously observed in patients treated with other chemotherapeutic agents, such as bleomycin and asparaginase [10]. In our case, eosinophil counts remained within normal ranges, and specific IgE levels or other markers of an acute allergic reaction were not measured.…”

Section: Discussionmentioning

confidence: 47%

Acute Cardiogenic Shock Induced by Infusional 5-Fluorouracil

Sulpher

Dattilo

Dent

et al. 2014

Case Reports in Oncological Medicine

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A 49-year-old patient with metastatic carcinoma of the bladder and no prior history of heart disease presented with diffuse ST elevation, elevated troponins, and biventricular dysfunction requiring intensive care unit admission and inotropic support after receiving her first course of infusional 5-fluorouracil (5-FU). Over the course of several days, the patient's cardiac function and clinical status returned to baseline. A follow-up echocardiogram performed 5 days after initial presentation revealed an ejection fraction of 59 percent, with no evidence of wall motion abnormalities. Subsequent 5-FU chemotherapy was discontinued, and the patient went on to receive second-line chemotherapy.

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Section: Discussionmentioning

confidence: 47%

Acute Cardiogenic Shock Induced by Infusional 5-Fluorouracil

Sulpher

Dattilo

Dent

et al. 2014

Case Reports in Oncological Medicine

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“…E. coli type II l-asparaginase (EcA-II) was found to be localized in the periplasm and to have higher af®nity for l-asparagine than the type I isozyme (EcA-I) (Cedar & Schwartz, 1967). The EcA-II exhibits antitumour activity (Mashburn & Wriston, 1964;Schwartz et al, 1966) and has been used as a drug in the treatment of acute childhood lymphoblastic leukaemia, although the treatment is restricted owing to its multiple in¯ammatory or allergic side effects (Geuenich et al, 1998). The mechanism of the antitumour activity of EcA-II has not yet been completely elucidated.…”

Section: Introductionmentioning

confidence: 99%

Structure of the type IL-asparaginase from the hyperthermophilic archaeonPyrococcus horikoshiiat 2.16 Å resolution

Yao

Yasutake

Morita

et al. 2005

Acta Crystallogr D Biol Cryst

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The crystal structure of the L-asparaginase from the hyperthermophilic archaeon Pyrococcus horikoshii (PhA) was determined by the multiwavelength anomalous diffraction (MAD) method and was refined to a resolution of 2.16 angstroms with a crystallographic R factor and free R factor of 21.1 and 25.3%, respectively. This is the first report of the three-dimensional structure of a type I L-asparaginase. These enyzmes are known as cytosolic L-asparaginases with lower affinities for substrate than the type II L-asparaginases. Although the overall fold of PhA was closely related to the structure of the well characterized type II L-asparaginase, structural differences were also detected. PhA forms a homodimer that corresponds to half the homotetramer of type II L-asparaginases. Structure comparison at the active site reveals that most catalytic residues are conserved except for two residues that recognize the amino group of the substrate. Additionally, a remarkable structural difference is found in the so-called 'active-site flexible loop'. In PhA this loop is stabilized by beta-hairpin formation and by elaborate interactions with the type-I-specific alpha-helical region derived from the other subunit forming the PhA dimer. The flexible loop of the type II enzyme is considered to serve as a mobile gate to the active site. Therefore, the loop stabilization observed in the PhA structure may cause limitation of the access of the substrate to the active site.

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“…However, these L-asparaginases can also have undesirable side effects, including anaphylaxis, pancreatitis, diabetes, leucopoenia, neurological seizures, and coagulation abnormalities that may lead to intracranial thrombosis or hemorrhage (7,10). These side effects are considered to arise from allergic responses, and the use of L-asparaginases from different organisms might alleviate the problem (11).…”

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confidence: 99%

Biochemical Characterization of a Novel l -Asparaginase with Low Glutaminase Activity from Rhizomucor miehei and Its Application in Food Safety and Leukemia Treatment

Huang

Liu

Sun

et al. 2014

Appl Environ Microbiol

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A novel fungal gene encoding the Rhizomucor miehei L-asparaginase (RmAsnase) was cloned and expressed in Escherichia coli. Its deduced amino acid sequence shared only 57% identity with the amino acid sequences of other reported L-asparaginases. The purified L-asparaginase homodimer had a molecular mass of 133.7 kDa, a high specific activity of 1,985 U/mg, and very low glutaminase activity. RmAsnase was optimally active at pH 7.0 and 45°C and was stable at this temperature for 30 min. The final level of acrylamide in biscuits and bread was decreased by about 81.6% and 94.2%, respectively, upon treatment with 10 U RmAsnase per mg flour. Moreover, this L-asparaginase was found to potentiate a lectin's induction of leukemic K562 cell apoptosis, allowing lowering of the drug dosage and shortening of the incubation time. Overall, our findings suggest that RmAsnase possesses a remarkable potential for the food industry and in chemotherapeutics for leukemia.

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Induction of leukotriene production by bleomycin and asparaginase in mast cells in vitro and in patients in vivo

Cited by 15 publications

References 18 publications

Acute Cardiogenic Shock Induced by Infusional 5-Fluorouracil

Acute Cardiogenic Shock Induced by Infusional 5-Fluorouracil

Structure of the type IL-asparaginase from the hyperthermophilic archaeonPyrococcus horikoshiiat 2.16 Å resolution

Biochemical Characterization of a Novel l -Asparaginase with Low Glutaminase Activity from Rhizomucor miehei and Its Application in Food Safety and Leukemia Treatment

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