Polyethylene Glycol Conjugation of Recombinant Methioninase for Cancer Therapy

Tan, Yuying; Sun, Xin; Xu, Mingxu; An, Zili; Tan, Xuezhong; Tan, Xiuying; Han, Qinghong; Miljković, D.; Yang, Meng; Hoffman, Robert M.

doi:10.1006/prep.1997.0805

Cited by 72 publications

(32 citation statements)

References 15 publications

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“…The reduction of the enzyme activity upon modification might due to the direct interaction with the catalytic sites causing slight hindrance to binding of substrates, as reported for modified enzymes by PEGylation [1,3,16,26,27]. Practically, the colorimetric activity was correlated with the modification of surface primary and ε-amino groups of lysine residues, ensuring the little interaction with surface amino groups [27]. However, there is no notable modification of free surface thiols upon modification by PEG moieties, that could by justified by the strict selectivity for amino groups modification or absence of surface thiols.…”

Section: Discussionmentioning

confidence: 82%

Biochemical and Pharmacokinetic Properties of Aspergillus flavipes Glutathione-Homocystine Transhydrogenase of Unique Affinity for Homocystine Reduction using GSH as Hydrogen Donor

Elsayed¹

2015

Med chem

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Section: Discussionmentioning

confidence: 82%

Biochemical and Pharmacokinetic Properties of Aspergillus flavipes Glutathione-Homocystine Transhydrogenase of Unique Affinity for Homocystine Reduction using GSH as Hydrogen Donor

Elsayed¹

2015

Med chem

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“…Interestingly, methionine/ valine depleted, tyrosine lowered and arginine enriched was the most rationalized form for inhibition of tumor growth (Chen et al, 2001, He et al, 2003. L-Methioninase was extensively tested a potent anti-proliferative enzyme towards Lewis lung (Yoshioka et al, 1998), human colon (Tan et al, 1998), glioblastoma (Kokkinakis et al, 2001), neuroblastoma (Hu and Cheung, 2009) as reviewed by Nozaki (2009) andEl-Sayed (2010). Recently, Parenteral nutrition is a common cosupportive strategy for various aspects of tumor therapy (Buchman et al, 2006).…”

Section: Rationality Of Plp Dependent Enzymes As Antitumor and Anticamentioning

confidence: 99%

“…PEGylated forms of therapeutic enzymes as Escherichia coli asparaginase (Abuchowski et al, 1979), arginine deiminase (Izzo et al, 2007), Bacillus subtilis arginase (Cheng et al, 2005), Aspergillus flavus uricase (Bayol et al, 2002) displays affordable therapeutic potentialities comparing to corresponding free enzymes, as declared by FDA. PEGylation of Pseudomonas putida L-methioninase was extensively studied (Tan et al, 1998 andSun et al, 2003). The half-life time of PEG-L-methioninase was increased to 160 min, comparing to 80 min to the unmodified enzyme.…”

Section: Pegylation Of L-methioninasementioning

confidence: 99%

“…The half-life time of PEG-L-methioninase was increased to 160 min, comparing to 80 min to the unmodified enzyme. However, the activity of L-methioninase was relatively not inhibited by PEGylation as appeared from the IC 50 values against human lung and kidney tumors (Tan et al, 1998). In addition, PEGylation enhance the half-life times of the recombinant L-methioninase by about 20 fold and rate of serum methionine depletion by about 12 fold (Sun et al, 2003).…”

Section: Pegylation Of L-methioninasementioning

confidence: 99%

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PLP-Dependent Enzymes: a Potent Therapeutic Approach for Cancer and Cardiovascular Diseases

El-Sayed¹,

Shindia²

2011

Targets in Gene Therapy

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“…42,43 The cell lysate (200 L) was first precipitated by acetonitrile (800 L). A total of 10 L of supernatant was then mixed with 5 L of OPA.…”

Section: Methionine Levels Of Tumor Cellsmentioning

confidence: 99%

Survival efficacy of the combination of the methioninase gene and methioninase in a lung cancer orthotopic model

Miki

et al. 2000

Cancer Gene Ther

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We have previously demonstrated the antitumor efficacy of recombinant methioninase (rMETase) derived from Pseudomonas putida. To enhance the efficacy of rMETase, we have constructed the pLGFP-METSN retrovirus encoding the P. putida methioninase (MET) gene fused with the green fluorescent protein (GFP) gene. pLGFP-METSN or control vector pLGFPSN was introduced into the human lung cancer cell line H460. The methionine level of H460-GFP-MET cells was reduced to 33% of that of H460-GFP cells. rMETase (0.08 U/mL) in the medium resulted in 10% survival of H460-GFP-MET cells compared with untreated cells in vitro. In contrast, rMETase-treated H460-GFP cells survived at 90% of control. Tissue fragments harvested from subcutaneous tumors of H460-GFP-MET or H460-MET were implanted by surgical orthotopic implantation into the lungs of nude mice. A suboptimal dose of rMETase was administered intraperitoneally daily to mice in each group. Overall survival of rMETase-treated animals with H460-GFP-MET tumors was significantly longer than either rMETase-treated or -untreated animals with H460-GFP tumors (P Ͻ .05 in log-rank test). In two repeat experiments, rMETase-treated animals with H460-GFP-MET tumors had a 30-day survival of 80% and 83%, respectively. Untreated animals with H460-GFP-MET tumors had a 30-day survival of 40% and 58%, respectively. rMETase-treated animals with H460-GFP tumors had a 30-day survival of 0% and 33%, respectively. Untreated animals with H460-GFP tumors had a 30-day survival of 0% and 33%, respectively.

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Polyethylene Glycol Conjugation of Recombinant Methioninase for Cancer Therapy

Cited by 72 publications

References 15 publications

Biochemical and Pharmacokinetic Properties of Aspergillus flavipes Glutathione-Homocystine Transhydrogenase of Unique Affinity for Homocystine Reduction using GSH as Hydrogen Donor

Biochemical and Pharmacokinetic Properties of Aspergillus flavipes Glutathione-Homocystine Transhydrogenase of Unique Affinity for Homocystine Reduction using GSH as Hydrogen Donor

PLP-Dependent Enzymes: a Potent Therapeutic Approach for Cancer and Cardiovascular Diseases

Survival efficacy of the combination of the methioninase gene and methioninase in a lung cancer orthotopic model

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