Human Paraoxonase 1 as a Pharmacologic Agent: Limitations and Perspectives

Human PON1 (h-PON1) is a multifaceted enzyme and can hydrolyze (and inactivate) a wide range of substrates. The enzyme shows anti-inflammatory, antioxidative, antiatherogenic, ant-diabetic, antimicrobial, and organophosphate (OP)-detoxifying properties. However, there are certain limitations regardi...

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Published in:TheScientificWorld 2014, Vol.2014 (2014), p.1-6
Main Authors: Pande, Abhay H., Aggarwal, Geetika, Tripathy, Rajan K., Bajaj, Priyanka
Format: Article
Language:English
Subjects:
Amino acids
Animals
Aqueous solutions
Aryldialkylphosphatase - biosynthesis
Aryldialkylphosphatase - genetics
Aryldialkylphosphatase - pharmacology
Bacteriology
Crystal structure
Disease
E coli
Enzyme kinetics
Enzymes
Escherichia coli - genetics
Health education
Humans
Hydrolysis
Inflammation - drug therapy
Inflammation - genetics
Mice
Molecular Targeted Therapy
Organophosphate Poisoning - blood
Organophosphate Poisoning - drug therapy
Organophosphates
Pharmaceutical sciences
Pharmaceuticals
Poisoning
Proteins
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Review
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description Human PON1 (h-PON1) is a multifaceted enzyme and can hydrolyze (and inactivate) a wide range of substrates. The enzyme shows anti-inflammatory, antioxidative, antiatherogenic, ant-diabetic, antimicrobial, and organophosphate (OP)-detoxifying properties. However, there are certain limitations regarding large-scale production and use of h-PON1 as a therapeutic candidate. These include difficulties in producing recombinant h-PON1 (rh-PON1) using microbial expression system, low hydrolytic activity of wild-type h-PON1 towards certain substrates, and low storage stability of the purified enzyme. This review summarizes the work done in our laboratory to address these limitations. Our results show that (a) optimized polynucleotide sequence encoding rh-PON1 can express the protein in an active form in E. coli and can be used to generate variant of the enzyme having enhanced hydrolytic activity, (b) in vitro refolding of rh-PON1 enzyme can dramatically increase the yield of an active enzyme, (c) common excipients can be used to stabilize purified rh-PON1 enzyme when stored under different storage conditions, and (d) variants of rh-PON1 enzyme impart significant protection against OP-poisoning in human blood (ex vivo) and mouse (in vivo) model of OP-poisoning. The rh-PON1 variants and their process of production discussed here will help to develop h-PON1 as a therapeutic candidate.
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The enzyme shows anti-inflammatory, antioxidative, antiatherogenic, ant-diabetic, antimicrobial, and organophosphate (OP)-detoxifying properties. However, there are certain limitations regarding large-scale production and use of h-PON1 as a therapeutic candidate. These include difficulties in producing recombinant h-PON1 (rh-PON1) using microbial expression system, low hydrolytic activity of wild-type h-PON1 towards certain substrates, and low storage stability of the purified enzyme. This review summarizes the work done in our laboratory to address these limitations. Our results show that (a) optimized polynucleotide sequence encoding rh-PON1 can express the protein in an active form in E. coli and can be used to generate variant of the enzyme having enhanced hydrolytic activity, (b) in vitro refolding of rh-PON1 enzyme can dramatically increase the yield of an active enzyme, (c) common excipients can be used to stabilize purified rh-PON1 enzyme when stored under different storage conditions, and (d) variants of rh-PON1 enzyme impart significant protection against OP-poisoning in human blood (ex vivo) and mouse (in vivo) model of OP-poisoning. 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subjects Amino acids
Animals
Aqueous solutions
Aryldialkylphosphatase - biosynthesis
Aryldialkylphosphatase - genetics
Aryldialkylphosphatase - pharmacology
Bacteriology
Crystal structure
Disease
E coli
Enzyme kinetics
Enzymes
Escherichia coli - genetics
Health education
Humans
Hydrolysis
Inflammation - drug therapy
Inflammation - genetics
Mice
Molecular Targeted Therapy
Organophosphate Poisoning - blood
Organophosphate Poisoning - drug therapy
Organophosphates
Pharmaceutical sciences
Pharmaceuticals
Poisoning
Proteins
Recombinant Proteins - biosynthesis
Recombinant Proteins - genetics
Review
title Human Paraoxonase 1 as a Pharmacologic Agent: Limitations and Perspectives
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