Determination of Supplier-to-Supplier and Lot-to-Lot Variability in Glycation of Recombinant Human Serum Albumin Expressed in Oryza sativa

Frahm, Grant E.; Smith, Daryl G.S.; Kane, Anita; Lorbetskie, Barry; Cyr, Terry D.; Girard, Michel; Johnston, Michael

doi:10.1371/journal.pone.0109893

Cited by 18 publications

(25 citation statements)

References 56 publications

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“…OsrHSA-Sig1 (Lot# SLBC7527V) was rapidly defatted using published procedures [ 21 ]. Briefly, OsrHSA-Sig1 was exchanged into 5 mM citrate buffer (pH 3.2) as described above in “Albumin sample preparation” to partially unfold the protein to allow for improved removal of bound fatty acids (FA).…”

Section: Methodsmentioning

confidence: 99%

“…We have extensively studied commercially available rHSA and observed both supplier-to-supplier and lot-to-lot variability in rHSA expressed in O . sativa (Asian rice) (OsrHSA) when compared to either pHSA or rHSA expressed in yeast, with OsrHSA demonstrating the presence of bound fatty acids, increased arginine/lysine glycation, improved thermal stability and most interestingly the presence of higher molecular weight aggregates [ 20 , 21 ]. With the benefits that a plant based expression system provides in terms of yield and cost effective production [ 22 , 23 ], and the shortages of plasma derived HSA reported in various jurisdictions [ 24 ], it is conceivable that rHSA from rice would be used to fabricate nanoparticles for various scientific studies.…”

Section: Introductionmentioning

confidence: 99%

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Nanoparticle size and production efficiency are affected by the presence of fatty acids during albumin nanoparticle fabrication

et al. 2017

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We have previously identified extensive glycation, bound fatty acids and increased quantities of protein aggregates in commercially available recombinant HSA (rHSA) expressed in Oryza sativa (Asian rice) (OsrHSA) when compared to rHSA from other expression systems. We propose these differences may alter some attributes of nanoparticles fabricated with OsrHSA, as studies have associated greater quantities of aggregates with increased nanoparticle diameters. To determine if this is the case, nanoparticles were fabricated with OsrHSA from various suppliers using ethanol desolvation and subsequent glutaraldehyde cross-linking. All nanoparticles fabricated with OsrHSA showed larger diameters of approximately 20 to 90nm than particles fabricated with either defatted bovine serum albumin (DF-BSA) (100.9 ± 2.8nm) or human plasma albumin (pHSA) (112.0 ± 4.0nm). It was hypothesized that the larger nanoparticle diameters were due to the presence of bound fatty acids and this was confirmed through defatting OsrHSA prior to particle fabrication which yielded particles with diameters similar to those fabricated with pHSA. For additional conformation, DF-BSA was incubated with dodecanoic acid prior to desolvation yielding particles with significantly larger diameters. Further studies showed the increased nanoparticle diameters were due to the bound fatty acids modulating electrostatic interactions between albumin nanoparticles during the desolvation and not changes in protein structure, stability or generation of additional albumin oligomers. Finally the presence of dodecanoic acid was shown to improve doxorubicin loading efficiency onto preformed albumin nanoparticles.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Nanoparticle size and production efficiency are affected by the presence of fatty acids during albumin nanoparticle fabrication

et al. 2017

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“…Differences have been reported in drug-binding data among pharmaceutical-grade albumin and manufacturing lots of bovine serum albumin. 16,17) Furthermore, lot-to-lot variability in high-molecular-weight aggregates and the glycation of recombinant HSA expressed in Oryza sativa, 18) as well as differences in esterase-like activities of HSA among manufacturing lots and suppliers due to cholinesterase contamination 19) have also been reported. However, the effects of drug interactions on hydrolysis by HSA among manufacturing lots have not yet been investigated in sufficient detail.…”

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confidence: 99%

Differences in Esterase Activity to Aspirin and <i>p</i>-Nitrophenyl Acetate among Human Serum Albumin Preparations

Tatsumi

Okada

Inagaki

et al. 2016

Biological & Pharmaceutical Bulletin

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Human serum albumin (HSA) has two major ligand-binding sites, sites I and II, and also hydrolyzes some compounds at both sites. In the present study, we investigated differences in esterase activity among HSA preparations, and also the effects of warfarin, indomethacin, and naproxen on the hydrolytic activities of HSA to aspirin and p-nitrophenyl acetate. The esterase activities of HSA to aspirin or p-nitrophenyl acetate were measured from the pseudo-first-order formation rate constant (k obs ) of salicylic acid or p-nitrophenol by HSA. Inter-lot variations were observed in the esterase activities of HSA to aspirin and p-nitrophenyl acetate; however, the esterase activity of HSA to aspirin did not correlate with that to p-nitrophenyl acetate. The inhibitory effects of warfarin and indomethacin on the esterase activity of HSA to aspirin were stronger than that of naproxen. In contrast, the inhibitory effect of naproxen on the esterase activity of HSA to p-nitrophenyl acetate was stronger than those of warfarin and indomethacin. These results suggest that the administration of different commercial HSA preparations and the co-administration with site I or II high-affinity binding drugs may change the pharmacokinetic profiles of drugs that are hydrolyzed by HSA.

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“…As described in ‘Determination of Supplier-to-Supplier and Lot-to-Lot Variability in Glycation of Recombinant Human Serum Albumin Expressed in Oryza sativa ’ [1,2,3,5] .…”

Section: Experimental Design Materials and Methodsmentioning

confidence: 99%

Data set for mass spectrometric analysis of recombinant human serum albumin from various expression systems

et al. 2015

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Human serum albumin (HSA) is a versatile and important protein for the pharmaceutical industry (Fanali et al., Mol. Aspects Med. 33(3) (2012) 209–290). Due to the potential transmission of pathogens from plasma sourced albumin, numerous expression systems have been developed to produce recombinant HSA (rHSA) (Chen et al., Biochim. Biophys. Acta (BBA)—Gen. Subj. 1830(12) (2013) 5515–5525; Kobayashi, Biologicals 34(1) (2006) 55–59). Based on our previous study showing increased glycation of rHSA expressed in Asian rice (Frahm et al., J. Phys. Chem. B 116(15) (2012) 4661–4670), both supplier-to-supplier and lot-to-lot variability of rHSAs from a number of expression systems were evaluated using reversed phase liquid chromatography linked with MS and MS/MS analyses. The data are associated with the research article ‘Determination of Supplier-to-Supplier and Lot-to-Lot Variability in Glycation of Recombinant Human Serum Albumin Expressed in Oryza sativa’ where further analysis of rHSA samples with additional biophysical methods can be found (Frahm et al., PLoS ONE 10(9) (2014) e109893). We determined that all rHSA samples expressed in rice showed elevated levels of arginine and lysine hexose glycation compared to rHSA expressed in yeast, suggesting that the extensive glycation of the recombinant proteins is a by-product of either the expression system or purification process and not a random occurrence.

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Determination of Supplier-to-Supplier and Lot-to-Lot Variability in Glycation of Recombinant Human Serum Albumin Expressed in Oryza sativa

Cited by 18 publications

References 56 publications

Nanoparticle size and production efficiency are affected by the presence of fatty acids during albumin nanoparticle fabrication

Nanoparticle size and production efficiency are affected by the presence of fatty acids during albumin nanoparticle fabrication

Differences in Esterase Activity to Aspirin and <i>p</i>-Nitrophenyl Acetate among Human Serum Albumin Preparations

Data set for mass spectrometric analysis of recombinant human serum albumin from various expression systems

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