CoChat
Sign Up
Cited by 283

Structural and biochemical features of human Serum albumin essential for eukaryotic cell culture

Mishra, Vibhor, Heath, Richard J.·2021·International Journal of Molecular Sciences
DOI 10.3390/ijms22168411PMC PMC8395139
Open this paper in CoChat — free account

Abstract

Serum albumin physically interacts with fatty acids, small molecules, metal ions, and several other proteins. Binding with a plethora of bioactive substances makes it a critical transport molecule. Albumin also scavenges the reactive oxygen species that are harmful to cell survival. These properties make albumin an excellent choice to promote cell growth and maintain a variety of eukaryotic cells under in vitro culture environment. Furthermore, purified recombinant human serum albumin is mostly free from impurities and modifications, providing a perfect choice as an additive in cell and tissue culture media while avoiding any regulatory constraints. This review discusses key features of human serum albumin implicated in cell growth and survival under in vitro conditions.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/ijms22168411

Cites

3 of 3 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Cites

Flagged first, then by citations

Research works printed but not linked: 143

  1. [1]Kalra H. Adda C.G. Liem M. Ang C.S. Mechler A. Simpson R.J. Hulett M.D. Mathivanan S. Comparative proteomics evaluation of plasma exosome isolation techniques and assessment of the stability of exosomes in normal human blood plasma Proteomics 2013 13 3354 3364 10.1002/pmic.201300282 24115447 · DOI
  2. [2]El-Fakharany E.M. Abu-Serie M.M. Litus E.A. Permyakov S.E. Permyakov E.A. Uversky V.N. Redwan E.M. The Use of Human, Bovine, and Camel Milk Albumins in Anticancer Complexes with Oleic Acid Protein J. 2018 37 203 215 10.1007/s10930-018-9770-1 29691701 · DOI
  3. [4]Zilic S. Barac M. Pesic M. Dodig D. Ignjatovic-Micic D. Characterization of proteins from grain of different bread and durum wheat genotypes Int. J. Mol. Sci. 2011 12 5878 5894 10.3390/ijms12095878 22016634 PMC3189758 · DOI
  4. [5]Peters T. All About Albumin: Biochemistry, Genetics and Medical Application Academic Press Limited Cambridge, MA, USA 1995
  5. [6]Fanali G. di Masi A. Trezza V. Marino M. Fasano M. Ascenzi P. Human serum albumin: From bench to bedside Mol. Asp. Med. 2012 33 209 290 10.1016/j.mam.2011.12.002 22230555 · DOI
  6. [7]Merlot A.M. Kalinowski D.S. Richardson D.R. Unraveling the mysteries of serum albumin-more than just a serum protein Front. Physiol. 2014 5 299 10.3389/fphys.2014.00299 25161624 PMC4129365 · DOI
  7. [8]Evans T.W. Albumin as a drug—biological effects of albumin unrelated to oncotic pressure Aliment. Pharmacol. Ther. 2002 16 Suppl. 5 6 11 10.1046/j.1365-2036.16.s5.2.x 12423448 · DOI
  8. [9]Ghuman J. Zunszain P.A. Petitpas I. Bhattacharya A.A. Otagiri M. Curry S. Structural basis of the drug-binding specificity of human serum albumin J. Mol. Biol. 2005 353 38 52 10.1016/j.jmb.2005.07.075 16169013 · DOI · Paper page
  9. [10]Lei J. Guan B. Li B. Duan Z. Chen Y. Li H. Jin J. Expression, purification and characterization of recombinant human interleukin-2-serum albumin (rhil-2-hsa) fusion protein in pichia pastoris Protein Expr. Purif. 2012 84 154 160 10.1016/j.pep.2012.05.003 22609631 · DOI
  10. [11]Francis G.L. Albumin and mammalian cell culture: Implications for biotechnology applications Cytotechnology 2010 62 1 16 10.1007/s10616-010-9263-3 20373019 PMC2860567 · DOI · Paper page
  11. [12]Keenan J. Dooley M. Pearson D. Clynes M. Recombinant Human Albumin in Cell Culture: Evaluation of Growth-Promoting Potential for NRK and SCC-9 Cells In Vitro Cytotechnology 1997 24 243 252 10.1023/A:1007916930200 22358768 PMC3449618 · DOI
  12. [13]Karimi M. Bahrami S. Ravari S.B. Zangabad P.S. Mirshekari H. Bozorgomid M. Shahreza S. Sori M. Hamblin M.R. Albumin nanostructures as advanced drug delivery systems Expert Opin. Drug Deliv. 2016 13 1609 1623 10.1080/17425247.2016.1193149 27216915 PMC5063715 · DOI
  13. [14]He Y. Ning T. Xie T. Qiu Q. Zhang L. Sun Y. Jiang D. Fu K. Yin F. Zhang W. Large-scale production of functional human serum albumin from transgenic rice seeds Proc. Natl. Acad. Sci. USA 2011 108 19078 19083 10.1073/pnas.1109736108 22042856 PMC3223471 · DOI
  14. [15]Zhu W. Gong G. Pan J. Han S. Zhang W. Hu Y. Xie L. High level expression and purification of recombinant human serum albumin in Pichia pastoris Protein Expr. Purif. 2018 147 61 68 10.1016/j.pep.2018.02.003 29518537 · DOI
  15. [16]Sun Q.Y. Ding L.W. Lomonossoff G.P. Sun Y.B. Luo M. Li C.Q. Jiang L. Xu Z.F. Improved expression and purification of recombinant human serum albumin from transgenic tobacco suspension culture J. Biotechnol. 2011 155 164 172 10.1016/j.jbiotec.2011.06.033 21762733 · DOI
  16. [17]Chen Z. He Y. Shi B. Yang D. Human serum albumin from recombinant DNA technology: Challenges and strategies Biochim. Biophys. Acta Gen. Subj. 2013 1830 5515 5525 10.1016/j.bbagen.2013.04.037 23644036 · DOI
  17. [18]Sharma A. Chaudhuri T.K. Revisiting Escherichia coli as microbial factory for enhanced production of human serum albumin Microb. Cell Factories 2017 16 173 10.1186/s12934-017-0784-8 28982367 PMC5629808 · DOI
  18. [19]Nguyen M.T. Heo Y. Do B.H. Baek S. Kim C.J. Jang Y.J. Lee W. Choe H. Bacterial overexpression and purification of soluble recombinant human serum albumin using maltose-binding protein and protein disulphide isomerase Protein Expr. Purif. 2020 167 105530 10.1016/j.pep.2019.105530 31698036 · DOI
  19. [20]Sleep D. Belfield G.P. Goodey A.R. The secretion of human serum albumin from the yeast Saccharomyces cerevisiae using five different leader sequences Biotechnology 1990 8 42 46 10.1038/nbt0190-42 1366511 · DOI
  20. [21]Fleer R. Yeh P. Amellal N. Maury I. Fournier A. Bacchetta F. Baduel P. Jung G. L’Hote H. Becquart J. Stable multicopy vectors for high-level secretion of recombinant human serum albumin by Kluyveromyces yeasts Biotechnology 1991 9 968 975 10.1038/nbt1091-968 1367806 · DOI
  21. [22]Barash I. Faerman A. Baruch A. Nathan M. Hurwitz D.R. Shani M. Synthesis and secretion of human serum albumin by mammary gland explants of virgin and lactating transgenic mice Transgenic Res. 1993 2 266 276 10.1007/BF01968839 8242096 · DOI
  22. [23]Chuang V.T. Otagiri M. Recombinant human serum albumin Drugs Today (Barc) 2007 43 547 561 10.1358/dot.2007.43.8.1067343 17925886 · DOI
  23. [24]Larsen M.T. Kuhlmann M. Hvam M.L. Howard K.A. Albumin-based drug delivery: Harnessing nature to cure disease Mol. Cell Ther. 2016 4 3 10.1186/s40591-016-0048-8 26925240 PMC4769556 · DOI
  24. [25]Zhou G. Jin X. Zhu P. Yao J.U. Zhang Y. Teng L. Lee R.J. Zhang X. Hong W. Human serum albumin nanoparticles as a novel delivery system for cabazitaxel Anticancer Res. 2016 36 1649 1656 27069142
  25. [26]An F.F. Zhang X.H. Strategies for preparing albumin-based nanoparticles for multifunctional bioimaging and drug delivery Theranostics 2017 7 3667 3689 10.7150/thno.19365 29109768 PMC5667340 · DOI
  26. [27]Liu Z. Chen X. Simple bioconjugate chemistry serves great clinical advances: Albumin as a versatile platform for diagnosis and precision therapy Chem. Soc. Rev. 2016 45 1432 1456 10.1039/C5CS00158G 26771036 PMC5227548 · DOI
  27. [28]Tao C. Chuah Y.J. Xu C. Wang D.A. Albumin conjugates and assemblies as versatile bio-functional additives and carriers for biomedical applications J. Mater. Chem. B 2019 7 357 367 10.1039/C8TB02477D 32254722 · DOI
  28. [29]Merten O.W. Development of serum-free media for cell growth and production of viruses/viral vaccines—safety issues of animal products used in serum-free media Dev. Biol. 2002 111 233 257 12678248
  29. [30]Keenan J. Pearson D. Clynes M. The role of recombinant proteins in the development of serum-free media Cytotechnology 2006 50 49 56 10.1007/s10616-006-9002-y 19003070 PMC3476004 · DOI
  30. [31]Keenan J. Doherty G. Clynes M. Separation of growth-stimulating activity of BSA fraction V from the bulk of albumin using Heparin Sepharose Chromatography Cytotechnology 1995 19 63 72 10.1007/BF00749756 22358906 · DOI
  31. [32]Curling J.M. Berglof J. Lindquist L.O. Eriksson S. A chromatographic procedure for the purification of human plasma albumin Vox Sang. 1977 33 97 107 10.1111/j.1423-0410.1977.tb02240.x 883250 · DOI
  32. [33]Ohtani W. Ohda T. Sumi A. Kobayashi K. Ohmura T. Analysis of Pichia pastoris components in recombinant human serum albumin by immunological assays and by HPLC with pulsed amperometric detection Anal. Chem. 1998 70 425 429 10.1021/ac970596h 9450369 · DOI
  33. [34]Mallem M. Warburton S. Li F. Shandil I. Nylen A. Kim S. Jiang Y. Meehl M. d’Anjou M. Stadheim T.A. Maximizing recombinant human serum albumin production in a Mut(s) pichia pastoris strain Biotechnol. Prog. 2014 30 1488 1496 10.1002/btpr.1990 25196297 · DOI
  34. [35]Taghizadeh S.M. Ebrahiminezhad A. Ghoshoon M.B. Dehshahri A. Berenjian A. Ghasemi Y. Magnetic immobilization of Pichia pastoris cells for the production of recombinant human serum albumin Nanomaterials 2020 10 111 10.3390/nano10010111 PMC7022243 31935937 · DOI
  35. [36]Li S. Li L. Chen Z. Xue G. Jiang L. Zheng K. Chen J. Li R. Yuan C. Huang M. A novel purification procedure for recombinant human serum albumin expressed in pichia pastoris Protein Expr. Purif. 2018 149 37 42 10.1016/j.pep.2018.04.012 29678737 · DOI
  36. [37]Zhu R.Y. Xin X. Dai H.Y. Li Q. Lei J.Y. Chen Y. Jin J. Expression and purification of recombinant human serum albumin fusion protein with VEGF165b in Pichia pastoris Protein Expr. Purif. 2012 85 32 37 10.1016/j.pep.2012.06.009 22750397 · DOI
  37. [38]Liu Y.K. Li Y.T. Lu C.F. Huang L.F. Enhancement of recombinant human serum albumin in transgenic rice cell culture system by cultivation strategy New Biotechnol. 2015 32 328 334 10.1016/j.nbt.2015.03.001 25765580 · DOI
  38. [39]Pang J. Zhou J. Yang D. Knock-in at GluA1 locus improves recombinant human serum albumin expression in rice grain J. Biotechnol. 2020 321 87 95 10.1016/j.jbiotec.2020.06.018 32619642 · DOI
  39. [40]Saunders C.W. Schmidt B.J. Mallonee R.L. Guyer M.S. Secretion of human serum albumin from Bacillus subtilis J. Bacteriol. 1987 169 2917 2925 10.1128/jb.169.7.2917-2925.1987 3110129 PMC212327 · DOI
  40. [41]Sharma A. Chaudhuri T.K. Physicochemical characterization of E. coli-derived human serum albumin and its comparison with the human plasma counterpart reveals it as a promising biosimilar J. Biotechnol. 2018 274 1 8 10.1016/j.jbiotec.2018.03.004 29524439 · DOI
  41. [42]Strauss A.W. Bennett C.A. Donohue A.M. Rodkey J.A. Boime I. Alberts A.W. Conversion of rat pre-proalbumin to proalbumin in vitro by ascites membranes. Demonstration by NH2-TERMINAL SEQUENCE ANALYSIS J. Biol. Chem. 1978 253 6270 6274 10.1016/S0021-9258(17)34610-0 681351 · DOI
  42. [43]Brennan S.O. Carrell R.W. A circulating variant of human proalbumin Nature 1978 274 908 909 10.1038/274908a0 683332 · DOI
  43. [44]He X.M. Carter D.C. Atomic structure and chemistry of human serum albumin Nature 1992 358 209 215 10.1038/358209a0 1630489 · DOI
  44. [45]Sugio S. Kashima A. Mochizuki S. Noda M. Kobayashi K. Crystal structure of human serum albumin at 2.5 A resolution Protein Eng. 1999 12 439 446 10.1093/protein/12.6.439 10388840 · DOI
  45. [46]Murayama K. Tomida M. Heat-induced secondary structure and conformation change of bovine serum albumin investigated by Fourier transform infrared spectroscopy Biochemistry 2004 43 11526 11532 10.1021/bi0489154 15350138 · DOI
  46. [47]Bujacz A. Structures of bovine, equine and leporine serum albumin Acta Crystallogr. Sect. D Biol. Crystallogr. 2012 68 1278 1289 10.1107/S0907444912027047 22993082 · DOI
  47. [48]Majorek K.A. Porebski P.J. Dayal A. Zimmerman M.D. Jablonska K. Stewart A.J. Chruszcz M. Minor W. Structural and immunologic characterization of bovine, horse, and rabbit serum albumins Mol. Immunol. 2012 52 174 182 10.1016/j.molimm.2012.05.011 22677715 PMC3401331 · DOI
  48. [49]Ketrat S. Japrung D. Pongprayoon P. Exploring how structural and dynamic properties of bovine and canine serum albumins differ from human serum albumin J. Mol. Graph. Model. 2020 98 107601 10.1016/j.jmgm.2020.107601 32311662 · DOI
  49. [50]Huang B.X. Kim H.Y. Dass C. Probing three-dimensional structure of bovine serum albumin by chemical cross-linking and mass spectrometry J. Am. Soc. Mass Spectrom. 2004 15 1237 1247 10.1016/j.jasms.2004.05.004 15276171 · DOI
  50. [51]Paris G. Kraszewski S. Ramseyer C. Enescu M. About the structural role of disulfide bridges in serum albumins: Evidence from protein simulated unfolding Biopolymers 2012 97 889 898 10.1002/bip.22096 22899364 · DOI
  51. [52]Chubarov A. Spitsyna A. Krumkacheva O. Mitin D. Suvorov D. Tormyshev V. Fedin M. Bowman M.K. Bagryanskaya E. Reversible dimerization of human serum albumin Molecules 2021 26 108 10.3390/molecules26010108 33383640 PMC7795135 · DOI
  52. [53]Steglich M. Lombide R. Lopez I. Portela M. Flo M. Marin M. Alvarez B. Turell L. Expression, purification and initial characterization of human serum albumin domain I and its cysteine 34 PLoS ONE 2020 15 e0240580 10.1371/journal.pone.0240580 33045024 PMC7549792 · DOI
  53. [54]Roche M. Rondeau P. Singh N.R. Tarnus E. Bourdon E. The antioxidant properties of serum albumin FEBS Lett. 2008 582 1783 1787 10.1016/j.febslet.2008.04.057 18474236 · DOI · Paper page
  54. [55]Oettl K. Stauber R.E. Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties Br. J. Pharmacol. 2007 151 580 590 10.1038/sj.bjp.0707251 17471184 PMC2013999 · DOI
  55. [56]Bourdon E. Loreau N. Lagrost L. Blache D. Differential effects of cysteine and methionine residues in the antioxidant activity of human serum albumin Free Radic. Res. 2005 39 15 20 10.1080/10715760400024935 15875807 · DOI
  56. [57]van der Vusse G.J. Albumin as fatty acid transporter Drug Metab. Pharmacokinet. 2009 24 300 307 10.2133/dmpk.24.300 19745557 · DOI
  57. [58]Curry S. Mandelkow H. Brick P. Franks N. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites Nat. Struct. Biol. 1998 5 827 835 10.1038/1869 9731778 · DOI
  58. [59]Brown N.A. Wilson A.G. Bridges J.W. Chain length dependency of fatty acid and carbamate binding to serum albumin Biochem. Pharmacol. 1982 31 4019 4029 10.1016/0006-2952(82)90650-5 7159478 · DOI
  59. [60]Fanali G. Fesce R. Agrati C. Ascenzi P. Fasano M. Allosteric modulation of myristate and Mn(III)heme binding to human serum albumin. Optical and NMR spectroscopy characterization FEBS J. 2005 272 4672 4683 10.1111/j.1742-4658.2005.04883.x 16156788 · DOI
  60. [61]Huang B.X. Dass C. Kim H.Y. Probing conformational changes of human serum albumin due to unsaturated fatty acid binding by chemical cross-linking and mass spectrometry Biochem. J. 2005 387 695 702 10.1042/BJ20041624 15588254 PMC1134999 · DOI
  61. [62]Bos O.J. Labro J.F. Fischer M.J. Wilting J. Janssen L.H. The molecular mechanism of the neutral-to-base transition of human serum albumin: Acid/Base titration and proton nuclear magnetic resonance studies on a large peptic and a large tryptic fragment of albumin J. Biol. Chem. 1989 264 953 959 10.1016/S0021-9258(19)85036-6 2910873 · DOI
  62. [63]Dockal M. Carter D.C. Ruker F. Conformational transitions of the three recombinant domains of human serum albumin depending on pH J. Biol. Chem. 2000 275 3042 3050 10.1074/jbc.275.5.3042 10652284 · DOI
  63. [64]Barbosa L.R. Ortore M.G. Spinozzi F. Mariani P. Bernstorff S. Itri R. The importance of protein-protein interactions on the pH-induced conformational changes of bovine serum albumin: A small-angle X-ray scattering study Biophys. J. 2010 98 147 157 10.1016/j.bpj.2009.09.056 20085727 PMC2800971 · DOI
  64. [65]Simard J.R. Zunszain P.A. Ha C.E. Yang J.S. Bhagavan N.V. Petitpas I. Curry S. Hamilton J.A. Locating high-affinity fatty acid-binding sites on albumin by x-ray crystallography and NMR spectroscopy Proc. Natl. Acad. Sci. USA 2005 102 17958 17963 10.1073/pnas.0506440102 16330771 PMC1312385 · DOI
  65. [66]Simard J.R. Zunszain P.A. Hamilton J.A. Curry S. Location of high and low affinity fatty acid binding sites on human serum albumin revealed by NMR drug-competition analysis J. Mol. Biol. 2006 361 336 351 10.1016/j.jmb.2006.06.028 16844140 · DOI · Paper page
  66. [67]Bhattacharya A.A. Grune T. Curry S. Crystallographic analysis reveals common modes of binding of medium and long-chain fatty acids to human serum albumin J. Mol. Biol. 2000 303 721 732 10.1006/jmbi.2000.4158 11061971 · DOI
  67. [68]Sudlow G. Birkett D.J. Wade D.N. The characterization of two specific drug binding sites on human serum albumin Mol. Pharmacol. 1975 11 824 832 1207674
  68. [69]Krzywoszynska K. Witkowska D. Swiatek-Kozlowska J. Szebesczyk A. Kozlowski H. General aspects of metal ions as signaling agents in health and disease Biomolecules 2020 10 1417 10.3390/biom10101417 PMC7600656 33036384 · DOI
  69. [70]Al-Harthi S. Lachowicz J.I. Nowakowski M.E. Jaremko M. Jaremko L. Towards the functional high-resolution coordination chemistry of blood plasma human serum albumin J. Inorg. Biochem. 2019 198 110716 10.1016/j.jinorgbio.2019.110716 31153112 · DOI
  70. [71]Angele-Martinez C. Nguyen K.V. Ameer F.S. Anker J.N. Brumaghim J.L. Reactive oxygen species generation by copper(II) oxide nanoparticles determined by DNA damage assays and EPR spectroscopy Nanotoxicology 2017 11 278 288 10.1080/17435390.2017.1293750 28248593 PMC5494152 · DOI
  71. [72]Bal W. Sokolowska M. Kurowska E. Faller P. Binding of transition metal ions to albumin: Sites, affinities and rates Biochim. Biophys. Acta 2013 1830 5444 5455 10.1016/j.bbagen.2013.06.018 23811338 · DOI
  72. [73]Sadler P.J. Tucker A. Viles J.H. Involvement of a lysine residue in the N-terminal Ni2+ and Cu2+ binding site of serum albumins. Comparison with Co2+, Cd2+ and Al3+ Eur. J. Biochem. 1994 220 193 200 10.1111/j.1432-1033.1994.tb18614.x 8119287 · DOI
  73. [74]Masuoka J. Hegenauer J. Van Dyke B.R. Saltman P. Intrinsic stoichiometric equilibrium constants for the binding of zinc(ii) and copper(II) to the high affinity site of serum albumin J. Biol. Chem. 1993 268 21533 21537 10.1016/S0021-9258(20)80574-2 8408004 · DOI
  74. [75]Glennon J.D. Sarkar B. The non-specificity of dog serum albumin and the N-terminal model peptide glycylglycyl-L-tyrosine N-methylamide for nickel is due to the lack of histidine in the third position Biochem. J. 1982 203 25 31 10.1042/bj2030025 7103937 PMC1158188 · DOI
  75. [76]Bujacz A. Talaj J.A. Zielinski K. Pietrzyk-Brzezinska A.J. Neumann P. Crystal structures of serum albumins from domesticated ruminants and their complexes with 3,5-diiodosalicylic acid Acta Crystallogr. Sect. D Struct. Biol. 2017 73 896 909 10.1107/S205979831701470X 29095162 PMC5683013 · DOI
  76. [77]Shen X.C. Liang H. Guo J.H. Song C. He X.W. Yuan Y.Z. Studies on the interaction between Ag+ and human serum albumin J. Inorg. Biochem. 2003 95 124 130 10.1016/S0162-0134(03)00094-1 12763656 · DOI
  77. [78]Sadler P.J. Viles J.H. 1H and (113)Cd NMR investigations of Cd2+ and Zn2+ binding sites on serum albumin: Competition with Ca2+, Ni2+, Cu2+, and Zn2+ Inorg. Chem. 1996 35 4490 4496 10.1021/ic951005d 11666670 · DOI
  78. [79]Stewart A.J. Blindauer C.A. Berezenko S. Sleep D. Sadler P.J. Interdomain zinc site on human albumin Proc. Natl. Acad. Sci. USA 2003 100 3701 3706 10.1073/pnas.0436576100 12598656 PMC152985 · DOI
  79. [80]Lu J. Stewart A.J. Sadler P.J. Pinheiro T.J. Blindauer C.A. Albumin as a zinc carrier: Properties of its high-affinity zinc-binding site Biochem. Soc. Trans. 2008 36 1317 1321 10.1042/BST0361317 19021548 · DOI
  80. [81]Mothes E. Faller P. Evidence that the principal CoII-binding site in human serum albumin is not at the N-terminus: Implication on the albumin cobalt binding test for detecting myocardial ischemia Biochemistry 2007 46 2267 2274 10.1021/bi061783p 17274600 · DOI
  81. [82]Makinen M.W. Brady M.J. Structural origins of the insulin-mimetic activity of bis(acetylacetonato)oxovanadium(IV) J. Biol. Chem. 2002 277 12215 12220 10.1074/jbc.M110798200 11815612 · DOI
  82. [83]Liboiron B.D. Thompson K.H. Hanson G.R. Lam E. Aebischer N. Orvig C. New insights into the interactions of serum proteins with bis(maltolato)oxovanadium(IV): Transport and biotransformation of insulin-enhancing vanadium pharmaceuticals J. Am. Chem. Soc. 2005 127 5104 5115 10.1021/ja043944n 15810845 · DOI
  83. [84]Haratake M. Hongoh M. Miyauchi M. Hirakawa R. Ono M. Nakayama M. Albumin-mediated selenium transfer by a selenotrisulfide relay mechanism Inorg. Chem. 2008 47 6273 6280 10.1021/ic800310j 18563895 · DOI
  84. [85]Taverna M. Marie A.L. Mira J.P. Guidet B. Specific antioxidant properties of human serum albumin Ann. Intensive Care 2013 3 4 10.1186/2110-5820-3-4 23414610 PMC3577569 · DOI
  85. [86]Phaniendra A. Jestadi D.B. Periyasamy L. Free radicals: Properties, sources, targets, and their implication in various diseases Indian J. Clin. Biochem. 2015 30 11 26 10.1007/s12291-014-0446-0 25646037 PMC4310837 · DOI · Paper page
  86. [87]Quinlan G.J. Martin G.S. Evans T.W. Albumin: Biochemical properties and therapeutic potential Hepatology 2005 41 1211 1219 10.1002/hep.20720 15915465 · DOI
  87. [88]Liang J. Han Q. Tan Y. Ding H. Li J. Current advances on structure-function relationships of pyridoxal 5′-phosphate-dependent enzymes Front. Mol. Biosci. 2019 6 4 10.3389/fmolb.2019.00004 30891451 PMC6411801 · DOI
  88. [89]Fonda M.L. Trauss C. Guempel U.M. The binding of pyridoxal 5′-phosphate to human serum albumin Arch. Biochem. Biophys. 1991 288 79 86 10.1016/0003-9861(91)90167-H 1898027 · DOI
  89. [90]Bohney J.P. Fonda M.L. Feldhoff R.C. Identification of Lys190 as the primary binding site for pyridoxal 5′-phosphate in human serum albumin FEBS Lett. 1992 298 266 268 10.1016/0014-5793(92)80073-P 1544460 · DOI
  90. [91]Hilak M.C. Harmsen B.J. Joordens J.J. Van Os G.A. Binding of pyridoxal 5′-phosphate to bovine serum albumin and albumin fragments obtained after proteolytic hydrolysis. Localization and nature of the primary plp binding site Int. J. Pept. Protein Res. 1975 7 411 416 10.1111/j.1399-3011.1975.tb02461.x 1184290 · DOI
  91. [92]Remucal C.K. McNeill K. Photosensitized amino acid degradation in the presence of riboflavin and its derivatives Environ. Sci. Technol. 2011 45 5230 5237 10.1021/es200411a 21591753 · DOI
  92. [93]Huang R. Kim H.J. Min D.B. Photosensitizing effect of riboflavin, lumiflavin, and lumichrome on the generation of volatiles in soy milk J. Agric. Food Chem. 2006 54 2359 2364 10.1021/jf052448v 16536619 · DOI
  93. [94]Innis W.S. McCormick D.B. Merrill A.H. Jr. Variations in riboflavin binding by human plasma: Identification of immunoglobulins as the major proteins responsible Biochem. Med. 1985 34 151 165 10.1016/0006-2944(85)90106-1 4084240 · DOI
  94. [95]Jusko W.J. Levy G. Plasma protein binding of riboflavin and riboflavin-5′-phosphate in man J. Pharm. Sci. 1969 58 58 62 10.1002/jps.2600580110 5765837 · DOI
  95. [96]Lee P. Wu X. Modifications of human serum albumin and their binding effect Curr. Pharm. Des. 2015 21 1862 1865 10.2174/1381612821666150302115025 25732553 PMC4654954 · DOI
  96. [97]Ahmed N. Dobler D. Dean M. Thornalley P.J. Peptide mapping identifies hotspot site of modification in human serum albumin by methylglyoxal involved in ligand binding and esterase activity J. Biol. Chem. 2005 280 5724 5732 10.1074/jbc.M410973200 15557329 · DOI
  97. [98]Otagiri M. Chuang V.T. Pharmaceutically important pre- and posttranslational modifications on human serum albumin Biol. Pharm. Bull. 2009 32 527 534 10.1248/bpb.32.527 19336879 · DOI
  98. [99]Coussons P.J. Jacoby J. McKay A. Kelly S.M. Price N.C. Hunt J.V. Glucose modification of human serum albumin: A structural study Free Radic. Biol. Med. 1997 22 1217 1227 10.1016/S0891-5849(96)00557-6 9098096 · DOI
  99. [100]Ahmed N. Thornalley P.J. Chromatographic assay of glycation adducts in human serum albumin glycated in vitro by derivatization with 6-aminoquinolyl-N-hydroxysuccinimidyl-carbamate and intrinsic fluorescence Biochem. J. 2002 364 15 24 10.1042/bj3640015 11988071 PMC1222540 · DOI
  100. [101]Iwao Y. Anraku M. Hiraike M. Kawai K. Nakajou K. Kai T. Suenaga A. Otagiri M. The structural and pharmacokinetic properties of oxidized human serum albumin, advanced oxidation protein products (AOPP) Drug Metab. Pharmacokinet. 2006 21 140 146 10.2133/dmpk.21.140 16702734 · DOI
  101. [102]Bertucci C. Nanni B. Salvadori P. Reversible binding of ethacrynic acid to human serum albumin: Difference circular dichroism study Chirality 1999 11 33 38 10.1002/(SICI)1520-636X(1999)11:1<33::AID-CHIR6>3.0.CO;2-U 9914651 · DOI
  102. [103]Stewart A.J. Blindauer C.A. Berezenko S. Sleep D. Tooth D. Sadler P.J. Role of Tyr84 in controlling the reactivity of Cys34 of human albumin FEBS J. 2005 272 353 362 10.1111/j.1742-4658.2004.04474.x 15654874 · DOI
  103. [104]Luo S. Levine R.L. Methionine in proteins defends against oxidative stress FASEB J. 2009 23 464 472 10.1096/fj.08-118414 18845767 PMC2630790 · DOI
  104. [105]Carter D.C. Ho J.X. Structure of serum albumin Adv. Protein Chem. 1994 45 153 203 10.1016/s0065-3233(08)60640-3 8154369 · DOI
  105. [106]Zsila F. Subdomain IB is the third major drug binding region of human serum albumin: Toward the three-sites model Mol. Pharm. 2013 10 1668 1682 10.1021/mp400027q 23473402 · DOI
  106. [107]Carter D.C. Crystallographic Survey of Albumin Drug Interaction and Applications in Cancer Chemotherapy Burger’s Drug Design and Development 7th ed. John Wiley & Sons Hoboken, NJ, USA 2010 437 468
  107. [108]Ascenzi P. di Masi A. Fanali G. Fasano M. Heme-based catalytic properties of human serum albumin Cell Death Discov. 2015 1 15025 10.1038/cddiscovery.2015.25 27551458 PMC4991842 · DOI
  108. [109]Dutra F.F. Bozza M.T. Heme on innate immunity and inflammation Front. Pharmacol. 2014 5 115 10.3389/fphar.2014.00115 24904418 PMC4035012 · DOI
  109. [110]Balla G. Jacob H.S. Eaton J.W. Belcher J.D. Vercellotti G.M. Hemin: A possible physiological mediator of low density lipoprotein oxidation and endothelial injury Arterioscler. Thromb. 1991 11 1700 1711 10.1161/01.ATV.11.6.1700 1931871 · DOI
  110. [111]Kamal J.K. Behere D.V. Binding of heme to human serum albumin: Steady-state fluorescence, circular dichroism and optical difference spectroscopic studies Indian J. Biochem. Biophys. 2005 42 7 12 23923575
  111. [112]Hosainzadeh A. Gharanfoli M. Saberi M. Chamani J. Probing the interaction of human serum albumin with bilirubin in the presence of aspirin by multi-spectroscopic, molecular modeling and zeta potential techniques: Insight on binary and ternary systems J. Biomol. Struct. Dyn. 2012 29 1013 1050 10.1080/073911012010525029 22292958 · DOI
  112. [113]Schnitzer J.E. Carley W.W. Palade G.E. Albumin interacts specifically with a 60-kDa microvascular endothelial glycoprotein Proc. Natl. Acad. Sci. USA 1988 85 6773 6777 10.1073/pnas.85.18.6773 3413125 PMC282060 · DOI
  113. [114]Ghinea N. Fixman A. Alexandru D. Popov D. Hasu M. Ghitescu L. Eskenasy M. Simionescu M. Simionescu N. Identification of albumin-binding proteins in capillary endothelial cells J. Cell Biol. 1988 107 231 239 10.1083/jcb.107.1.231 2839518 PMC2115163 · DOI
  114. [115]Roopenian D.C. Akilesh S. FcRn: The neonatal Fc receptor comes of age Nat. Rev. Immunol. 2007 7 715 725 10.1038/nri2155 17703228 · DOI · Paper page
  115. [116]Schnitzer J.E. Oh P. Antibodies to SPARC Inhibit albumin binding to SPARC, gp60, and microvascular endothelium Am. J. Physiol. 1992 263 H1872 H1879 10.1152/ajpheart.1992.263.6.H1872 1481911 · DOI
  116. [117]Schnitzer J.E. Update on the cellular and molecular basis of capillary permeability Trends Cardiovasc. Med. 1993 3 124 130 10.1016/1050-1738(93)90012-U 21244938 · DOI
  117. [118]Nilsen J. Trabjerg E. Grevys A. Azevedo C. Brennan S.O. Stensland M. Wilson J. Sand K.M.K. Bern M. Dalhus B. An intact C-terminal end of albumin is required for its long half-life in humans Commun. Biol. 2020 3 181 10.1038/s42003-020-0903-7 32313072 PMC7171077 · DOI
  118. [121]Anderson C.L. Chaudhury C. Kim J. Bronson C.L. Wani M.A. Mohanty S. Perspective—FcRn transports albumin: Relevance to immunology and medicine Trends Immunol. 2006 27 343 348 10.1016/j.it.2006.05.004 16731041 · DOI
  119. [122]Al-Rubeai M. Singh R.P. Goldman M.H. Emery A.N. Death mechanisms of animal cells in conditions of intensive agitation Biotechnol. Bioeng. 1995 45 463 472 10.1002/bit.260450602 18623245 · DOI
  120. [123]Ma N. Koelling K.W. Chalmers J.J. Fabrication and use of a transient contractional flow device to quantify the sensitivity of mammalian and insect cells to hydrodynamic forces Biotechnol. Bioeng. 2002 80 428 437 10.1002/bit.10387 12325151 · DOI
  121. [124]Mollet M. Godoy-Silva R. Berdugo C. Chalmers J.J. Acute hydrodynamic forces and apoptosis: A complex question Biotechnol. Bioeng. 2007 98 772 788 10.1002/bit.21476 17497730 · DOI
  122. [125]Chisti Y. Hydrodynamic damage to animal cells Crit. Rev. Biotechnol. 2001 21 67 110 10.1080/20013891081692 11451047 · DOI
  123. [126]Chisti Y. Animal-cell damage in sparged bioreactors Trends Biotechnol. 2000 18 420 432 10.1016/S0167-7799(00)01474-8 10998508 · DOI
  124. [127]Hesse F. Ebel M. Konisch N. Sterlinski R. Kessler W. Wagner R. Comparison of a production process in a membrane-aerated stirred tank and up to 1000-L airlift bioreactors using BHK-21 cells and chemically defined protein-free medium Biotechnol. Prog. 2003 19 833 843 10.1021/bp0257630 12790647 · DOI
  125. [128]Kunas K.T. Papoutsakis E.T. Damage mechanisms of suspended animal cells in agitated bioreactors with and without bubble entrainment Biotechnol. Bioeng. 2009 102 980 987 10.1002/bit.22263 19156925 · DOI
  126. [129]Kunas K.T. Papoutsakis E.T. Damage mechanisms of suspended animal cells in agitated bioreactors with and without bubble entrainment Biotechnol. Bioeng. 1990 36 476 483 10.1002/bit.260360507 18595104 · DOI
  127. [130]Smith C.G. Greenfield P.F. Mechanical agitation of hybridoma suspension cultures: Metabolic effects of serum, pluronic F68, and albumin supplements Biotechnol. Bioeng. 1992 40 1045 1055 10.1002/bit.260400908 18601213 · DOI
  128. [131]Glassy M.C. Tharakan J.P. Chau P.C. Serum-free media in hybridoma culture and monoclonal antibody production Biotechnol. Bioeng. 1988 32 1015 1028 10.1002/bit.260320809 18587819 · DOI
  129. [132]Stadlmann J. Pabst M. Kolarich D. Kunert R. Altmann F. Analysis of immunoglobulin glycosylation by LC-ESI-MS of glycopeptides and oligosaccharides Proteomics 2008 8 2858 2871 10.1002/pmic.200700968 18655055 · DOI
  130. [133]Desai N. Rambhia P. Gishto A. Human embryonic stem cell cultivation: Historical perspective and evolution of xeno-free culture systems Reprod. Biol. Endocrinol. 2015 13 9 10.1186/s12958-015-0005-4 25890180 PMC4351689 · DOI
  131. [134]Otsuki J. Nagai Y. Matsuyama Y. Terada T. Era S. The redox state of recombinant human serum albumin and its optimal concentration for mouse embryo culture Syst. Biol. Reprod. Med. 2013 59 48 52 10.3109/19396368.2012.727946 23050831 · DOI
  132. [135]Yamazoe H. Uemura T. Tanabe T. Facile cell patterning on an albumin-coated surface Langmuir 2008 24 8402 8404 10.1021/la801221r 18627191 · DOI
  133. [136]Yamazoe H. Tanabe T. Preparation of water-insoluble albumin film possessing nonadherent surface for cells and ligand binding ability J. Biomed. Mater. Res. A 2008 86 228 234 10.1002/jbm.a.31654 17975816 · DOI
  134. [137]Lang B.E. Cole K.D. Unfolding properties of recombinant human serum albumin products are due to bioprocessing steps Biotechnol. Prog. 2015 31 62 69 10.1002/btpr.1996 25270911 · DOI
  135. [138]Frahm G.E. Smith D.G. Kane A. Lorbetskie B. Cyr T.D. Girard M. Johnston M.J. Determination of supplier-to-supplier and lot-to-lot variability in glycation of recombinant human serum albumin expressed in oryza sativa PLoS ONE 2014 9 e109893 10.1371/journal.pone.0109893 25299339 PMC4192584 · DOI
  136. [139]Raoufinia R. Mota A. Keyhanvar N. Safari F. Shamekhi S. Abdolalizadeh J. Overview of albumin and its purification methods Adv. Pharm. Bull. 2016 6 495 507 10.15171/apb.2016.063 28101456 PMC5241407 · DOI
  137. [140]Bar-Or D. Bar-Or R. Rael L.T. Gardner D.K. Slone D.S. Craun M.L. Heterogeneity and oxidation status of commercial human albumin preparations in clinical use Crit. Care Med. 2005 33 1638 1641 10.1097/01.CCM.0000169876.14858.91 16003075 · DOI
  138. [141]Miyamura S. Imafuku T. Anraku M. Taguchi K. Yamasaki K. Tominaga Y. Maeda H. Ishima Y. Watanabe H. Otagiri M. Comparison of posttranslational modification and the functional impairment of human serum albumin in commercial preparations J. Pharm. Sci. 2016 105 1043 1049 10.1016/j.xphs.2015.12.015 26928399 · DOI
  139. [142]Yao T. Asayama Y. Animal-cell culture media: History, characteristics, and current issues Reprod. Med. Biol. 2017 16 99 117 10.1002/rmb2.12024 29259457 PMC5661806 · DOI
  140. [143]George F. Kerschen D. Van Nuffel A. Rees J.F. Donnay I. Plant protein hydrolysates (plant peptones) as substitutes for animal proteins in embryo culture medium Reprod. Fertil. Dev. 2009 21 587 598 10.1071/RD08147 19383265 · DOI
  141. [144]Simon A. Safran A. Revel A. Aizenman E. Reubinoff B. Porat-Katz A. Lewin A. Laufer N. Hyaluronic acid can successfully replace albumin as the sole macromolecule in a human embryo transfer medium Fertil. Steril. 2003 79 1434 1438 10.1016/S0015-0282(03)00349-2 12798894 · DOI
  142. [145]Biggers J.D. Summers M.C. McGinnis L.K. Polyvinyl alcohol and amino acids as substitutes for bovine serum albumin in culture media for mouse preimplantation embryos Hum. Reprod. Update 1997 3 125 135 10.1093/humupd/3.2.125 9286737 · DOI
  143. [146]Burteau C.C. Verhoeye F.R. Mols J.F. Ballez J.S. Agathos S.N. Schneider Y.J. Fortification of a protein-free cell culture medium with plant peptones improves cultivation and productivity of an interferon-gamma-producing CHO cell line In Vitro Cell Dev. Biol. Anim. 2003 39 291 296 10.1290/1543-706X(2003)039<0291:FOAPCC>2.0.CO;2 14753850 · DOI

Cited by

Sorted by citations

Authors
Mishra, V., & Heath, R. J.
Affiliations
Protein Production Facility, Shared Resource Center, St. Jude Children’s Research Hospital, Memphis, TN 38105, USA
ORCID
Mishra, Vibhor
Venue
International Journal of Molecular Sciences
Publisher
MDPI AG
Published
2021-08-05
Volume
22
Issue
16
Pages
8411
ISSN
1422-0067
DOI
10.3390/ijms22168411
PMC
PMC8395139
Cited by
283
References
3
Language
en
Licence
creativecommons.org/licenses/by/4.0/ (vor)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review