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            ‐asparaginase production and enhancement by
            <i>Sarocladium strictum</i>
            :
            <i>In vitro</i>
            evaluation of anti‐cancerous properties

Golbabaie, A.; Nouri, Hoda; Moghimi, Hamid; Khaleghian, Ali

doi:10.1111/jam.14623

Cited by 22 publications

(8 citation statements)

References 27 publications

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“…The role of chemical modifications and protein engineering in improving the effectiveness of medicines is also discussed. Currently, as an alternative to bacterial L-ASNases with chemotherapeutic use, several type II bacterial enzymes are under consideration: Thermus thermophiles , Proteus vulgaris , Pseudomonas fluorescens , Serratia marcescens , Erwinia aroidea , Aspergillus terreus , Mycobacterium tuberculosis , Yersinia pseudotuberculosis , recombinant Saccharomyces cerevisiae , Halomonas elongata , Sarocladium strictum , Streptomyces rochei , Aspergillus terreus , Fusarium culmorum and Zymomonas mobilis [ 62 , 138 , 139 , 140 , 141 , 142 ]. They all have antiproliferative activities toward cancer cells.…”

Section: Alternative Approaches To the Development Of Antitumor L-asn...mentioning

confidence: 99%

Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions

et al. 2022

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L-asparaginases (EC 3.5.1.1) are a family of enzymes that catalyze the hydrolysis of L-asparagine to L-aspartic acid and ammonia. These proteins with different biochemical, physicochemical and pharmacological properties are found in many organisms, including bacteria, fungi, algae, plants and mammals. To date, asparaginases from E. coli and Dickeya dadantii (formerly known as Erwinia chrysanthemi) are widely used in hematology for the treatment of lymphoblastic leukemias. However, their medical use is limited by side effects associated with the ability of these enzymes to hydrolyze L-glutamine, as well as the development of immune reactions. To solve these issues, gene-editing methods to introduce amino-acid substitutions of the enzyme are implemented. In this review, we focused on molecular analysis of the mechanism of enzyme action and to optimize the antitumor activity.

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Section: Alternative Approaches To the Development Of Antitumor L-asn...mentioning

confidence: 99%

Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions

et al. 2022

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“…The incorporation of this enzyme in the treatment of Acute Lymphocytic Leukemia (ALL) increased the complete remission of the disease from 20 to 80-90%, configuring, therefore, as an indispensable medicine to face the respective neoplasia (Costa-Silva et al 2020). Besides, it is emphasized the role of L-ASNase in therapeutic protocols for acute myelocytic leukemia, lymphosarcoma, acute myelomonocytic leukemia, reticulosarcoma, and melanosarcoma (Golbabaie et al 2020).…”

Section: L-asparaginasementioning

confidence: 99%

“…The antineoplastic mechanism of L-ASNase comes from the inherent ability to catalyze the conversion of the amino acid L-asparagine (L-Asn) to L-aspartate (L-Asp) and ammonia (Golbabaie et al 2020). In contrast to healthy cells, the expression of asparagine synthase, an enzyme responsible for producing L-Asn in the intracellular medium, is low in neoplastic cells.…”

Section: L-asparaginasementioning

confidence: 99%

Antarctic environments as a source of bacterial and fungal therapeutic enzymes

LIMA

Bispo

AGOSTINHO

et al. 2022

An. Acad. Bras. Ciênc.

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Microbial therapeutic enzymes are the protagonists in the pharmacological treatment of different human diseases. The intrinsic enzymatic characteristics, such as high affinity and specificity to the corresponding substrate, enable effective therapies, with minimal adverse effects and complete remission. However, immunogenicity, short half-life, low enzymatic yield, and low selectivity regarding available enzyme drugs are currently the main obstacles to their development and the broad adherence to therapeutic protocols. By harboring adapted and still unexplored microbial life, environments of extreme conditions, such as Antarctica, become especially important in the prospecting and development of new enzymatic compounds that present higher yields and the possibility of genetic improvement. Antarctic microorganisms have adaptation mechanisms, such as more fluid cell membranes, production of antifreeze proteins and enzymes with more malleable structures, more robust, stable, selective catalytic sites for their respective substrates, and high antioxidant capacity. In this context, this review aims to explore enzymes synthesized by bacteria and fungi from Antarctica as potential drug producers, capable of providing therapeutic efficacy, less adverse effects, and lower production costs with highlight to L-Asparaginase, collagenase, superoxide dismutase and ribonucleases. In addition, this review highlights the unique biotechnological profile of these Antarctic extremophile microorganisms.

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“…Thereafter, 5 µl of the 4 mM of pNA conjugated specific substrates (200 µM of final concentration) was added to each tube individually and incubated at 37 °C for 2 hours. At the end, a MultiSkan plate reader (LabSystems Diagnostic OY, Helsinki, Finland) was used to measure the absorbance of samples at 400 nm [34] .…”

Section: Caspases Activity Assaymentioning

confidence: 99%

Biochemical and Biological Evaluation of an L-Asparaginase from Isolated Escherichia coli MF-107 as an Anti-Tumor Enzyme on MCF7 Cell Line

Shahnazari¹,

Bigdeli²,

Dashbolaghi³

et al. 2022

IBJ

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Background: One of the most widely used anticancer agents is microbial L-ASNase. Herein, we assessed the biochemical and biological properties of an isolated L-ASNase from a Gram-negative bacteria strain, Escherichia coli MF-107. Methods: Using garden asparagus, we obtained several bacterial isolates. These strains were further screened for L-ASNase activity. A promising bacterial isolate was selected for L-ASNase production and subsequent purification. The molecular weight of purified L-ASNase was determined. The MTT assay was applied to assess the cytotoxic effect of the purified enzyme. Also, for caspase activity determination and the apoptotic effect of purified enzyme on in cells, we conducted a real-time PCR method. Results: The molecular weight of the enzyme was approximately 37 kDa. In the pH range of 7.5 to 8, the enzyme had considerable stability. At 35 °C, the purified L-ASNase optimum activity was recorded. The cytotoxic effect of the enzyme on treated cells was dose-dependent with an IC 50 value of 5.7 IU/ml. The Bax gene expression considerably raised by 5.75-fold ( p < 0.001) upon L-ASNase treatment. On the other hand, the anti-apoptotic Bcl-2 gene expression showed a 2.63-fold increase compared to the control ( p < 0.05). It was detected that the mRNA levels of caspase-3 and p53 were considerably upregulated (5.93 and 1.85-fold, respectively). We did not find any alternation in the caspase-8 activity of the treated cells compared to untreated cells. Conclusion: In this research, the proliferation of the breast cancer cells remarkably inhibited via the cytotoxic effect of isolated L-ASNase from microbial sources.

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l ‐asparaginase production and enhancement by Sarocladium strictum : In vitro evaluation of anti‐cancerous properties

Cited by 22 publications

References 27 publications

Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions

Molecular Analysis of L-Asparaginases for Clarification of the Mechanism of Action and Optimization of Pharmacological Functions

Antarctic environments as a source of bacterial and fungal therapeutic enzymes

Biochemical and Biological Evaluation of an L-Asparaginase from Isolated Escherichia coli MF-107 as an Anti-Tumor Enzyme on MCF7 Cell Line

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