We are analyzing https://link.springer.com/article/10.1186/1475-2867-9-9.

Title:
Pegylated derivatives of recombinant human arginase (rhArg1) for sustained in vivo activity in cancer therapy: preparation, characterization and analysis of their pharmacodynamics in vivo and in vitro and action upon hepatocellular carcinoma cell (HCC) | Cancer Cell International
Description:
Background Protein used in medicine, e.g. interferon, are immunogenic and quickly broken down by the body. Pegylation is a recognized way of preserving their integrity and reducing immune reactions, and works well with enzymes used to degrade amino acids, a recent focus of attention in controlling cancer growth. Of the two arginine-degrading enzymes being explored clinically, arginine deiminase is a decidedly foreign mycoplasm-derived enzyme, whereas human arginase 1 is a native liver enzyme. Both have been pegylated, the former with adjuncts of 20 kD, the latter with 5 kD PEG. Pegylation is done by several different methods, not all of which are satisfactory or desirable. Methods The preparation of novel polyethylene glycol (PEG) derivatives for modifying proteins is described, but directed specifically at pegylation of recombinant human arginase 1 (rhArg1). rhArg1 expressed in Escherichia coli was purified and coupled in various ways with 5 different PEG molecules to compare their protective properties and the residual enzyme activity, using hepatocellular cell lines both in vitro and in vivo. Results Methoxypolyethylene glycol-succinimidyl propionate (mPEG-SPA 5,000) coupled with very high affinity under mild conditions. The resulting pegylated enzyme (rhArg1-peg5,000 mw) had up to 6 PEG chains of 5K length which not only protected it from degradation and any residual immunogenicity, but most importantly let it retain >90% of its native catalytic activity. It remained efficacious in depleting arginine in rats after a single ip injection of 1,500 U of the conjugate as the native enzyme, plasma arginine falling to >0.05 μM from ~170 μM within 20 min and lasting 6 days. The conjugate had almost the same efficacy as unpegylated rhArg1 on 2 cultured human liver cancer (HCC) cell lines. It was considerably more effective than 4 other pegylated conjugates prepared. Conclusion Valuable data on the optimization of the pegylation procedure and choice of ligand that best stabilizes the enzyme arginase 1 are presented, a protocol that should equally fit many other enzymes and proteins. It is a long lasting arginine-depleting enzyme in vivo which will greatly improve its use in anti-cancer therapy.
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Keywords {🔍}

rharg, pegylated, arginine, arginase, peg, enzyme, pegylation, native, activity, article, google, scholar, cancer, human, cas, pubmed, mpegspa, rhargpeg, protein, vivo, liver, reaction, table, cell, fig, analysis, adi, ratio, enzymes, proteins, molecules, results, studies, data, hepatocellular, amino, deiminase, size, molecular, lane, recombinant, vitro, rats, treatment, authors, hcc, full, glycol, conditions, levels,

Topics {✒️}

matrix-assisted-laser-desorption-ionization-time granulocyte colony-stimulating factor methoxypolyethylene glycol-n-hydroxy-succinimide paul ning-man cheng & denys arginine-degrading enzymes bio-cancer treatments international yun-chung leung paul ning-man cheng open access article tumor necrosis factor-α wai-hung lo article download pdf methoxypolyethylene glycol-cyanuric chloride maldi-tof mass spectra methoxypolyethylene glycol-succinimidyl propionate methoxypoly-ethylene glycol-maleimide short circulatory half-life singly-charged molecular ion maldi-tof-ms strategic development research treating ass-positive tumors wai-man lam hepatocellular carcinoma cell vitro anti-tumor activity hepatocellular cell lines vivo anti-tumor activity vitro anti-cancer properties circular dichroism spectra full size image chemically modified enzymes privacy choices/manage cookies therapeutic-grade pegylated rharg1 bioconjugate preparations unresectable hepatocellular carcinoma anti-tumor efficacies related subjects sulfhydryl-selective chemistry human hepatocellular carcinoma malignant cell cultures authors’ original file low-range protein marker adi-ss peg5000 mw pegvisomant pfizer/sensus taper liver tumor increasing ph increases bio-informatics centre anti-cancer therapy amino acid analyzer hong kong innovation methoxypolyethylene glycol-propionaldehyde

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WebPage:
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         headline:Pegylated derivatives of recombinant human arginase (rhArg1) for sustained in vivo activity in cancer therapy: preparation, characterization and analysis of their pharmacodynamics in vivo and in vitro and action upon hepatocellular carcinoma cell (HCC)
         description:Protein used in medicine, e.g. interferon, are immunogenic and quickly broken down by the body. Pegylation is a recognized way of preserving their integrity and reducing immune reactions, and works well with enzymes used to degrade amino acids, a recent focus of attention in controlling cancer growth. Of the two arginine-degrading enzymes being explored clinically, arginine deiminase is a decidedly foreign mycoplasm-derived enzyme, whereas human arginase 1 is a native liver enzyme. Both have been pegylated, the former with adjuncts of 20 kD, the latter with 5 kD PEG. Pegylation is done by several different methods, not all of which are satisfactory or desirable. The preparation of novel polyethylene glycol (PEG) derivatives for modifying proteins is described, but directed specifically at pegylation of recombinant human arginase 1 (rhArg1). rhArg1 expressed in Escherichia coli was purified and coupled in various ways with 5 different PEG molecules to compare their protective properties and the residual enzyme activity, using hepatocellular cell lines both in vitro and in vivo. Methoxypolyethylene glycol-succinimidyl propionate (mPEG-SPA 5,000) coupled with very high affinity under mild conditions. The resulting pegylated enzyme (rhArg1-peg5,000 mw) had up to 6 PEG chains of 5K length which not only protected it from degradation and any residual immunogenicity, but most importantly let it retain >90% of its native catalytic activity. It remained efficacious in depleting arginine in rats after a single ip injection of 1,500 U of the conjugate as the native enzyme, plasma arginine falling to >0.05 μM from ~170 μM within 20 min and lasting 6 days. The conjugate had almost the same efficacy as unpegylated rhArg1 on 2 cultured human liver cancer (HCC) cell lines. It was considerably more effective than 4 other pegylated conjugates prepared. Valuable data on the optimization of the pegylation procedure and choice of ligand that best stabilizes the enzyme arginase 1 are presented, a protocol that should equally fit many other enzymes and proteins. It is a long lasting arginine-depleting enzyme in vivo which will greatly improve its use in anti-cancer therapy.
         datePublished:2009-04-17T00:00:00Z
         dateModified:2009-04-17T00:00:00Z
         pageStart:1
         pageEnd:13
         license:https://creativecommons.org/licenses/by/2.0
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            Hepatocellular Carcinoma Cell
            Arginase
            Pegvisomant
            Arginine Deiminase
            Arginine Level
            Cancer Research
            Cell Biology
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      headline:Pegylated derivatives of recombinant human arginase (rhArg1) for sustained in vivo activity in cancer therapy: preparation, characterization and analysis of their pharmacodynamics in vivo and in vitro and action upon hepatocellular carcinoma cell (HCC)
      description:Protein used in medicine, e.g. interferon, are immunogenic and quickly broken down by the body. Pegylation is a recognized way of preserving their integrity and reducing immune reactions, and works well with enzymes used to degrade amino acids, a recent focus of attention in controlling cancer growth. Of the two arginine-degrading enzymes being explored clinically, arginine deiminase is a decidedly foreign mycoplasm-derived enzyme, whereas human arginase 1 is a native liver enzyme. Both have been pegylated, the former with adjuncts of 20 kD, the latter with 5 kD PEG. Pegylation is done by several different methods, not all of which are satisfactory or desirable. The preparation of novel polyethylene glycol (PEG) derivatives for modifying proteins is described, but directed specifically at pegylation of recombinant human arginase 1 (rhArg1). rhArg1 expressed in Escherichia coli was purified and coupled in various ways with 5 different PEG molecules to compare their protective properties and the residual enzyme activity, using hepatocellular cell lines both in vitro and in vivo. Methoxypolyethylene glycol-succinimidyl propionate (mPEG-SPA 5,000) coupled with very high affinity under mild conditions. The resulting pegylated enzyme (rhArg1-peg5,000 mw) had up to 6 PEG chains of 5K length which not only protected it from degradation and any residual immunogenicity, but most importantly let it retain >90% of its native catalytic activity. It remained efficacious in depleting arginine in rats after a single ip injection of 1,500 U of the conjugate as the native enzyme, plasma arginine falling to >0.05 μM from ~170 μM within 20 min and lasting 6 days. The conjugate had almost the same efficacy as unpegylated rhArg1 on 2 cultured human liver cancer (HCC) cell lines. It was considerably more effective than 4 other pegylated conjugates prepared. Valuable data on the optimization of the pegylation procedure and choice of ligand that best stabilizes the enzyme arginase 1 are presented, a protocol that should equally fit many other enzymes and proteins. It is a long lasting arginine-depleting enzyme in vivo which will greatly improve its use in anti-cancer therapy.
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      keywords:
         Hepatocellular Carcinoma Cell
         Arginase
         Pegvisomant
         Arginine Deiminase
         Arginine Level
         Cancer Research
         Cell Biology
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      name:Bio-Cancer Treatment International Limited, Bio-Informatics Centre, Hong Kong Science Park, Shatin, Hong Kong
      name:Department of Applied Biology and Chemical Technology and Lo Ka Chung Centre for Natural Anti-Cancer Drug Development, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong
      name:Bio-Cancer Treatment International Limited, Bio-Informatics Centre, Hong Kong Science Park, Shatin, Hong Kong
      name:Bio-Cancer Treatment International Limited, Bio-Informatics Centre, Hong Kong Science Park, Shatin, Hong Kong
      name:Department of Applied Biology and Chemical Technology and Lo Ka Chung Centre for Natural Anti-Cancer Drug Development, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong
      name:Department of Applied Biology and Chemical Technology and Lo Ka Chung Centre for Natural Anti-Cancer Drug Development, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong
      name:Bio-Cancer Treatment International Limited, Bio-Informatics Centre, Hong Kong Science Park, Shatin, Hong Kong
      name:Bio-Cancer Treatment International Limited, Bio-Informatics Centre, Hong Kong Science Park, Shatin, Hong Kong
      name:Bio-Cancer Treatment International Limited, Bio-Informatics Centre, Hong Kong Science Park, Shatin, Hong Kong
      name:BioMedES, Leggat House, Keithhall, Inverurie, Aberdeen, UK
      name:Department of Applied Biology and Chemical Technology and Lo Ka Chung Centre for Natural Anti-Cancer Drug Development, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong
      name:Department of Applied Biology and Chemical Technology and Lo Ka Chung Centre for Natural Anti-Cancer Drug Development, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong

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