Literature DB >> 35816224

A systematic review of recent trends in research on therapeutically significant L-asparaginase and acute lymphoblastic leukemia.

Susan Aishwarya Suresh1, Selvarajan Ethiraj1, K N Rajnish2.   

Abstract

L-asparaginases are mostly obtained from bacterial sources for their application in the therapy and food industry. Bacterial L-asparaginases are employed in the treatment of Acute Lymphoblastic Leukemia (ALL) and its subtypes, a type of blood and bone marrow cancer that results in the overproduction of immature blood cells. It also plays a role in the food industry in reducing the acrylamide formed during baking, roasting, and frying starchy foods. This importance of the enzyme makes it to be of constant interest to the researchers to isolate novel sources. Presently L-asparaginases from E. coli native and PEGylated form, Dickeya chrysanthemi (Erwinia chrysanthemi) are in the treatment regime. In therapy, the intrinsic glutaminase activity of the enzyme is a major drawback as the patients in treatment experience side effects like fever, skin rashes, anaphylaxis, pancreatitis, steatosis in the liver, and many complications. Its significance in the food industry in mitigating acrylamide is also a major reason. Acrylamide, a potent carcinogen was formed when treating starchy foods at higher temperatures. Acrylamide content in food was analyzed and pre-treatment was considered a valuable option. Immobilization of the enzyme is an advancing and promising technique in the effective delivery of the enzyme than in free form. The concept of machine learning by employing the Artificial Network and Genetic Algorithm has paved the way to optimize the production of L-asparaginase from its sources. Gene-editing tools are gaining momentum in the study of several diseases and this review focuses on the CRISPR-Cas9 gene-editing tool in ALL.
© 2022. The Author(s), under exclusive licence to Springer Nature B.V.

Entities:  

Keywords:  Acrylamide; Acute lymphoblastic leukemia; CRISPR-Cas9; Immobilization; L-asparaginase; Machine learning

Year:  2022        PMID: 35816224     DOI: 10.1007/s11033-022-07688-4

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN: 0301-4851            Impact factor:   2.742


  34 in total

1.  Development and catalytic characterization of L-asparaginase nano-bioconjugates.

Authors:  Sarika Agrawal; Naveen Kango
Journal:  Int J Biol Macromol       Date:  2019-06-03       Impact factor: 6.953

2.  Reduction of acrylamide level through blanching with treatment by an extremely thermostable L-asparaginase during French fries processing.

Authors:  Shaohua Zuo; Tao Zhang; Bo Jiang; Wanmeng Mu
Journal:  Extremophiles       Date:  2015-06-16       Impact factor: 2.395

3.  A novel bacterial type II l-asparaginase and evaluation of its enzymatic acrylamide reduction in French fries.

Authors:  Zhibin Sun; Ran Qin; Ding Li; Kai Ji; Ting Wang; Zhongli Cui; Yan Huang
Journal:  Int J Biol Macromol       Date:  2016-07-09       Impact factor: 6.953

4.  Glutaminase free l-asparaginase from Vibrio cholerae: Heterologous expression, purification and biochemical characterization.

Authors:  Remya Radha; Nagarajan Arumugam; Sathyanarayana N Gummadi
Journal:  Int J Biol Macromol       Date:  2018-01-04       Impact factor: 6.953

Review 5.  The 2016 revision to the World Health Organization classification of myeloid neoplasms and acute leukemia.

Authors:  Daniel A Arber; Attilio Orazi; Robert Hasserjian; Jürgen Thiele; Michael J Borowitz; Michelle M Le Beau; Clara D Bloomfield; Mario Cazzola; James W Vardiman
Journal:  Blood       Date:  2016-04-11       Impact factor: 22.113

6.  Outcome of children and adolescents with lymphoblastic lymphoma.

Authors:  Maria Christina Lopes Araújo Oliveira; Keyla Christy Sampaio; Aline Carneiro Oliveira; Aieska Dantas Santos; Lúcia Porto Castro; Marcos Borato Viana
Journal:  Rev Assoc Med Bras (1992)       Date:  2015 Sep-Oct       Impact factor: 1.209

7.  Preparation and nanoencapsulation of l-asparaginase II in chitosan-tripolyphosphate nanoparticles and in vitro release study.

Authors:  Elham Bahreini; Khosrow Aghaiypour; Roghayeh Abbasalipourkabir; Ali Rezaei Mokarram; Mohammad Taghi Goodarzi; Massoud Saidijam
Journal:  Nanoscale Res Lett       Date:  2014-07-09       Impact factor: 4.703

8.  Purification and Characterization of Glutaminase Free Asparaginase from Enterobacter cloacae: In-Vitro Evaluation of Cytotoxic Potential against Human Myeloid Leukemia HL-60 Cells.

Authors:  Islam Husain; Anjana Sharma; Suresh Kumar; Fayaz Malik
Journal:  PLoS One       Date:  2016-02-18       Impact factor: 3.240

9.  Cloning, expression and characterization of L-asparaginase from Pseudomonas fluorescens for large scale production in E. coli BL21.

Authors:  Vijay Kishore; K P Nishita; H K Manonmani
Journal:  3 Biotech       Date:  2015-04-05       Impact factor: 2.406

10.  Recombinant L-Asparaginase from Zymomonas mobilis: A Potential New Antileukemic Agent Produced in Escherichia coli.

Authors:  Karen Einsfeldt; Isis Cavalcante Baptista; Juliana Christina Castanheira Vicente Pereira; Isabele Campos Costa-Amaral; Elaine Sobral da Costa; Maria Cecília Menks Ribeiro; Marcelo Gerardin Poirot Land; Tito Lívio Moitinho Alves; Ariane Leites Larentis; Rodrigo Volcan Almeida
Journal:  PLoS One       Date:  2016-06-02       Impact factor: 3.240

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