DNA and oligosaccharides stimulate oligomerization of human milk lactoferrin

被引:2
|
作者
Soboleva , S. E. [1 ,3 ]
Tuzikov, F. V. [2 ]
Tuzikova, N. A. [2 ]
Buneva, V. N. [1 ,3 ]
Nevinsky, G. A. [1 ,3 ]
机构
[1] Russian Acad Sci, Inst Chem Biol & Fundamental Med, Siberian Branch, Novosibirsk 630090, Russia
[2] Russian Acad Sci, Boreskov Inst Catalysis, Siberian Branch, Novosibirsk 630090, Russia
[3] Novosibirsk State Univ, Novosibirsk 630090, Russia
关键词
human lactoferrin; DNA; ATP; effects on oligomerization rate and degree; BINDING; GRANULOPOIESIS; POLYMERIZATION; INTERACTS; CELLS;
D O I
10.1134/S0026893309010191
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Lactoferrin (LF) is a Fe3+-transferring glycoprotein and is contained in human barrier fluids, blood, and milk. LF is an acute phase protein, is involved in nonspecific defense, and displays a unique set of biological functions. Small-angle X-ray scattering and light scattering experiments demonstrated that DNA and oligosaccharides added to LF with various levels of initial oligomerization increased the oligomerization rate. Almost complete dissociation into monomers was observed when 1 M NaCl was added to LF oligomers obtained in the presence of DNA, oligosaccharides, and nucleotides, previously identified as oligomerization effectors. LF complexes obtained with different oligomerization effectors differed in stability. Incubation with 50 mM MgCl2 completely destructed LF complexes formed in the presence of ATP and oligosaccharides but only partly destructed AMP- and d(pT)(10)-dependent complexes, which was followed by the formation of new complexes with a higher salt stability. A possible role of oligomerization in various LF functions is discussed.
引用
收藏
页码:142 / 149
页数:8
相关论文
共 50 条
  • [1] DNA and oligosaccharides stimulate oligomerization of human milk lactoferrin
    S. E. Soboleva (Babina)
    F. V. Tuzikov
    N. A. Tuzikova
    V. N. Buneva
    G. A. Nevinsky
    Molecular Biology, 2009, 43 : 142 - 149
  • [2] DNA, oligosaccharides, and mononucleotides stimulate oligomerization of human lactoferrin
    Nevinskii, Alexander G.
    Soboleva, Svetlana E.
    Tuzikov, Fedor V.
    Buneva, Valentina N.
    Nevinsky, Georgy A.
    JOURNAL OF MOLECULAR RECOGNITION, 2009, 22 (04) : 330 - 342
  • [3] Production of human lactoferrin in animal milk
    Goldman, I. L.
    Georgieva, S. G.
    Gurskiy, Ya. G.
    Krasnov, A. N.
    Deykin, A. V.
    Popov, A. N.
    Ermolkevich, T. G.
    Budzevich, A. I.
    Chernousov, A. D.
    Sadchikova, E. R.
    BIOCHEMISTRY AND CELL BIOLOGY, 2012, 90 (03) : 513 - 519
  • [4] The functional biology of human milk oligosaccharides
    Bode, Lars
    EARLY HUMAN DEVELOPMENT, 2015, 91 (11) : 619 - 622
  • [5] Human milk oligosaccharides - the plot thickens
    Donovan, Sharon M.
    BRITISH JOURNAL OF NUTRITION, 2009, 101 (09) : 1267 - 1269
  • [6] EXPRESSION OF HUMAN LACTOFERRIN IN MILK OF TRANSGENIC MICE
    PLATENBURG, GJ
    KOOTWIJK, EPA
    KOOIMAN, PM
    WOLOSHUK, SL
    NUIJENS, JH
    KRIMPENFORT, PJA
    PIEPER, FR
    DEBOER, HA
    STRIJKER, R
    TRANSGENIC RESEARCH, 1994, 3 (02) : 99 - 108
  • [7] The lactoferrin receptor may mediate the reduction of eosinophils in the duodenum of pigs consuming milk containing recombinant human lactoferrin
    Cooper, Caitlin
    Nonnecke, Eric
    Loennerdal, Bo
    Murray, James
    BIOMETALS, 2014, 27 (05) : 1031 - 1038
  • [8] Human Milk Oligosaccharides Promote the Growth of Staphylococci
    Hunt, K. M.
    Preuss, J.
    Nissan, C.
    Davlin, C. A.
    Williams, J. E.
    Shafii, B.
    Richardson, A. D.
    McGuire, M. K.
    Bode, L.
    McGuire, M. A.
    APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2012, 78 (14) : 4763 - 4770
  • [9] Human Milk Lactoferrin Hydrolyzes Ribonucleoside 5′-Triphosphates
    S. E. Babina
    D. V. Semenov
    V. N. Buneva
    G. A. Nevinsky
    Molecular Biology, 2005, 39 : 452 - 458
  • [10] Human milk lactoferrin hydrolyzes ribonucleoside 5′-triphosphates
    Babina, SE
    Semenov, DV
    Buneva, VN
    Nevinsky, GA
    MOLECULAR BIOLOGY, 2005, 39 (03) : 452 - 458