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The purification and identification of human blood serum proteins with affinity to the antitumor active RL2 lactaptin using magnetic microparticles

N. Manko, M. Starykovych, Y. Bobak, R. Stoika, V. Richter, O. Koval, I. Lavrik, D. Horák, S. Souchelnytskyi, Y. Kit,

. 2019 ; 33 (11) : e4647. [pub] 20190818

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/bmc20006160

Grantová podpora
Grant # VW 90315 Volkswagen Shifting

The cytopoxic effect of RL2 lactaptin (the recombinant analog of proteolytic fragment of human kappa-casein) toward tumor cells in vitro and in vivo presents it as a novel promising antitumor drug. The binding of any drug with serum proteins can affect their activity, distribution, rate of excretion and toxicity in the human body. Here, we studied the ability of RL2 to bind to various blood serum proteins. Using magnetic microparticles bearing by RL2 as an affinity matrix, in combination with mass spectrometry and western blot analysis, we found a number of blood serum proteins possessing affinity for RL2. Among them IgA, IgM and IgG subclasses of immunoglobulins, apolipoprotein A1 and various cortactin isoforms were identified. This data suggests that in the bloodstream RL2 lactaptin takes part in complicate protein-protein interactions, which can affect its activity.

Citace poskytuje Crossref.org

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$a The cytopoxic effect of RL2 lactaptin (the recombinant analog of proteolytic fragment of human kappa-casein) toward tumor cells in vitro and in vivo presents it as a novel promising antitumor drug. The binding of any drug with serum proteins can affect their activity, distribution, rate of excretion and toxicity in the human body. Here, we studied the ability of RL2 to bind to various blood serum proteins. Using magnetic microparticles bearing by RL2 as an affinity matrix, in combination with mass spectrometry and western blot analysis, we found a number of blood serum proteins possessing affinity for RL2. Among them IgA, IgM and IgG subclasses of immunoglobulins, apolipoprotein A1 and various cortactin isoforms were identified. This data suggests that in the bloodstream RL2 lactaptin takes part in complicate protein-protein interactions, which can affect its activity.
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$a Starykovych, Marina $u Institute of Cell Biology NAS Ukraine, Lviv, Ukraine.
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$a Bobak, Yaroslav $u Institute of Cell Biology NAS Ukraine, Lviv, Ukraine.
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$a Stoika, Rostyslav $u Institute of Cell Biology NAS Ukraine, Lviv, Ukraine.
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$a Richter, Vladimir $u Department of Biotechnology, Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia.
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$a Koval, Olga $u Department of Biotechnology, Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk, Russia.
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$a Lavrik, Inna $u Department of Translational Inflammation Research, Medical Faculty, Otto von Guericke University, Magdeburg, Germany.
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$a Horák, Daniel $u Institute of Macromolecular Chemistry, AS CR, Prague, Czech Republic.
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$a Souchelnytskyi, Serhiy $u Medical College, Qatar University, Doha, Qatar.
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