Effect of bovine milk antigens and egg lysozyme on the binding of 59Fe-lactoferrin to platelet plasma membranes |
| |
| Institution: | 1. Kaufman Center for Heart Failure, Department of Cardiovascular Medicine, Heart and Vascular Institute, Cleveland Clinic, Cleveland, OH, United States;2. Department of Cellular and Molecular Medicine, Lerner Research Institute, Cleveland, OH, United States;3. Division of Cardiology, Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, United States;1. Arbuzov Institute of Organic and Physical Chemistry, FRC Kazan Scientific Center of RAS, Arbuzov str. 8, 420088 Kazan, Russian Federation;2. Kazan Federal University, Kremlevskaya st. 18, 420008 Kazan, Russian Federation;3. Kazan National Research Technical University named after A.N. Tupolev - KAI, 10, K.Marx str., Kazan 420111, Russian Federation;1. Botanischer Garten/Herbarium, Universität Ulm, Hans-Krebs-Weg, 89081 Ulm, Germany;2. Department of Botany and Biodiversity Research, University of Vienna, Rennweg 14, 1030 Wien, Austria;3. Department of Biosciences, Paris-Lodron-University of Salzburg, Hellbrunnerstrasse 34, 5020 Salzburg, Austria |
| |
| Abstract: | - 1.1. Platelets bind specifically to lactoferrin. A significant similarity between human lactoferrin and some bovine milk proteins has been established.
- 2.2. Because of the structural homology of lactoferrin and cows milk proteins they are able to influence lactoferrins regulatory function on the level of its binding to membrane receptors on platelets.
- 3.3. An inhibitory effect of bovine α-lactalbumin and of β-lactoglobulin on lactoferrin-receptor interaction was shown.
- 4.4. Bovine α-lactalbumin competes with lactoferrin for the binding sites.
- 5.5. Scatchard plot analysis of data shows one binding site for lactoferrin in the presence of α-lactalbumin with an affinity constant, Ka = 0.46 × 109 mol/1 and 335 receptors/cell.
- 6.6. The inhibitory effect of β-lactoglobulin reaches 62% and is different for the common fraction ⨿-lactoglobulin and the genetic variants β-lactoglobulin A and B.
- 7.7. β-lactoglobulin does not compete with lactoferrin for the membrane receptors.
- 8.8. Bovine casein and egg lysozyme stimulate 59Fe-lactoferrin binding to the receptors. The mechanism of these effects is still unknown.
- 9.9. Tested alimentary antigens are able to interact with lactoferrin and also with some platelet membrane structures.
- 10.10. Established changes in lactoferrin binding to the platelet membrane might be in relation to lactoferrins regulatory function and (or) eliminating mechanisms of these alimentary antigens.
|
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
