TY - JOUR

T1 - DNase and RNase activities of fresh cow milk lactoferrin

AU - Soboleva, Svetlana E.

AU - Zakharova, Ol'ga D.

AU - Sedykh, Sergey E.

AU - Ivanisenko, Nikita V.

AU - Buneva, Valentina N.

AU - Nevinsky, Georgy A.

N1 - Funding Information: This research was supported by the grant from the Russian Foundation for Basic Research (16‐04‐00609) and by the Russian State funded budget project VI.62.1.5 (0309‐2016‐0003). Publisher Copyright: © 2019 John Wiley & Sons, Ltd. Copyright: Copyright 2019 Elsevier B.V., All rights reserved.

PY - 2019/7

Y1 - 2019/7

N2 - Lactoferrin (LF) is an Fe3+-binding glycoprotein first recognized in milk and then in other epithelial secretions and barrier body fluids to which many different functions have been attributed to LF, including protection from iron-induced lipid peroxidation, immunomodulation, cell growth regulation, DNA and RNA binding, as well as transcriptional activation, еtс. The polyfunctional physiological role of LF is still unclear, but it has been suggested to be responsible for primary defense against microbial and viral infections. Here, we present the first evidence that LF preparations isolated from milk of 18 cows of different breeds possess various levels of metal-dependent DNase and metal-independent RNase activities. For univocal assignment of DNase and RNase activities to cow LF, it was subjected to SDS-PAGE using gels with copolymerized calf thymus DNA or polymeric yeast RNA. In situ analysis was revealed DNase and RNase activities only in the gel zones corresponding to homogeneous LF. In contrast to human LF, cow LF possesses a relatively low cytotoxicity towards human tumor cells. The discovery that cow LF has these activities may contribute to understanding the multiple physiological functions of this extremely polyfunctional protein, including its protective role against microbial and viral infections. The computational spatial model of cow LF complex with DNA was obtained: according to the model positively charged residues of LF contact with DNA.

AB - Lactoferrin (LF) is an Fe3+-binding glycoprotein first recognized in milk and then in other epithelial secretions and barrier body fluids to which many different functions have been attributed to LF, including protection from iron-induced lipid peroxidation, immunomodulation, cell growth regulation, DNA and RNA binding, as well as transcriptional activation, еtс. The polyfunctional physiological role of LF is still unclear, but it has been suggested to be responsible for primary defense against microbial and viral infections. Here, we present the first evidence that LF preparations isolated from milk of 18 cows of different breeds possess various levels of metal-dependent DNase and metal-independent RNase activities. For univocal assignment of DNase and RNase activities to cow LF, it was subjected to SDS-PAGE using gels with copolymerized calf thymus DNA or polymeric yeast RNA. In situ analysis was revealed DNase and RNase activities only in the gel zones corresponding to homogeneous LF. In contrast to human LF, cow LF possesses a relatively low cytotoxicity towards human tumor cells. The discovery that cow LF has these activities may contribute to understanding the multiple physiological functions of this extremely polyfunctional protein, including its protective role against microbial and viral infections. The computational spatial model of cow LF complex with DNA was obtained: according to the model positively charged residues of LF contact with DNA.

KW - and RNase activities

KW - cow milk lactoferrin

KW - cytotoxicity

KW - DNase

KW - interaction with DNA and RNA

KW - RECOGNITION

KW - SPECIFICITY

KW - MEMBRANE

KW - PURIFICATION

KW - GROWTH

KW - BINDING

KW - COLOSTRUM

KW - RIBONUCLEASE

KW - BOVINE LACTOFERRIN

UR - http://www.scopus.com/inward/record.url?scp=85061603145&partnerID=8YFLogxK

U2 - 10.1002/jmr.2777

DO - 10.1002/jmr.2777

M3 - Article

C2 - 30761635

AN - SCOPUS:85061603145

VL - 32

JO - Journal of Molecular Recognition

JF - Journal of Molecular Recognition

SN - 0952-3499

IS - 7

M1 - e2777

ER -