TY - JOUR

T1 - Comparison of interaction between ceruloplasmin and lactoferrin/transferrin

T2 - to bind or not to bind

AU - Sokolov, A. V.

AU - Voynova, I. V.

AU - Kostevich, V. A.

AU - Vlasenko, A. Yu

AU - Zakharova, E. T.

AU - Vasilyev, V. B.

PY - 2017/9/1

Y1 - 2017/9/1

N2 - The year 2016 marked the 50th anniversary of the discovery by S. Osaki who first showed that ceruloplasmin (CP, ferro:O2-oxidoreductase or ferroxidase) is capable of oxidizing Fe(II) to Fe(III) and favors the incorporation of the latter into transferrin (TF). However, much debate remains in the literature concerning the existence of a complex between the enzyme oxidizing iron and the protein facilitating its transport in plasma. We studied CP in exocrine fluids and demonstrated its high-affinity interaction with transferrin found in breast milk and in lacrimal fluid, i.e. with lactoferrin (LF). Here we present data obtained by comparing the interaction of CP with LF and TF using surface plasmon resonance and Hummel–Dreyer chromatography. Binding of apo-LF within the range of concentrations 1.6-51.3 μM with CP immobilized on a CM5-chip is characterized by KD = 1.07 μM. Under similar conditions, the KD for apo-TF was measured and appeared to be higher than 51.3 μM. Hummel–Dreyer chromatography of CP with 51 μM apo-LF/apo-TF in the effluent demonstrated the absence of interaction between apo-TF and CP in solution, contrary to efficient interaction between apoLF and CP. In contrast to LF, the interaction of apo-TF with CP is probably not stable within the physiological range of concentrations of TF.

AB - The year 2016 marked the 50th anniversary of the discovery by S. Osaki who first showed that ceruloplasmin (CP, ferro:O2-oxidoreductase or ferroxidase) is capable of oxidizing Fe(II) to Fe(III) and favors the incorporation of the latter into transferrin (TF). However, much debate remains in the literature concerning the existence of a complex between the enzyme oxidizing iron and the protein facilitating its transport in plasma. We studied CP in exocrine fluids and demonstrated its high-affinity interaction with transferrin found in breast milk and in lacrimal fluid, i.e. with lactoferrin (LF). Here we present data obtained by comparing the interaction of CP with LF and TF using surface plasmon resonance and Hummel–Dreyer chromatography. Binding of apo-LF within the range of concentrations 1.6-51.3 μM with CP immobilized on a CM5-chip is characterized by KD = 1.07 μM. Under similar conditions, the KD for apo-TF was measured and appeared to be higher than 51.3 μM. Hummel–Dreyer chromatography of CP with 51 μM apo-LF/apo-TF in the effluent demonstrated the absence of interaction between apo-TF and CP in solution, contrary to efficient interaction between apoLF and CP. In contrast to LF, the interaction of apo-TF with CP is probably not stable within the physiological range of concentrations of TF.

KW - ceruloplasmin

KW - Hummel–Dreyer chromatography

KW - lactoferrin

KW - protein–protein interaction

KW - surface plasmon resonance

KW - transferrin

UR - http://www.scopus.com/inward/record.url?scp=85029542634&partnerID=8YFLogxK

U2 - 10.1134/S0006297917090115

DO - 10.1134/S0006297917090115

M3 - Article

C2 - 28988537

AN - SCOPUS:85029542634

VL - 82

SP - 1073

EP - 1078

JO - Biochemistry (Moscow)

JF - Biochemistry (Moscow)

SN - 0006-2979

IS - 9

ER -