Kuzan Aleksandra, Chwiłkowska Agnieszka, Maksymowicz Krzysztof, Abramczyk Urszula, Gamian Andrzej
Department of Preclinical Sciences, Pharmacology and Medical Diagnostics, Faculty of Medicine, Wrocław University of Science and Technology, Wybrzeże Stanisława Wyspiańskiego 27, 50-370 Wroclaw, Poland.
Department of Molecular and Cellular Biology, Faculty of Pharmacy, Wroclaw Medical University, Borowska 211A, 50-556 Wroclaw, Poland.
Biomedicines. 2024 Apr 11;12(4):847. doi: 10.3390/biomedicines12040847.
Osteopontin (OPN) and osteoprotegerin (OPG) are glycoproteins that participate in the regulation of tissue biomineralization. The aim of the project is to verify the hypothesis that the content of OPN and OPG in the aorta walls increases with the development of atherosclerosis and that these proteins are quantitatively related to the main proteins in the extracellular arteries matrix. Quantitative and qualitative analyses of the OPN and OPG content in 101 aorta sections have been conducted. Additionally, an enzyme-linked immunosorbent assay (ELISA) test has been performed to determine the collagen types I-IV and elastin content in the tissues. Correlations between the biochemical data and patients' age/sex, atherosclerosis stages, and calcification occurrences in the tissue have been established. We are the first to report correlations between OPN or OPG and various types of collagen and elastin content (OPG/type I collagen correlation: r = 0.37, = 0.004; OPG/type II collagen: r = 0.34, = 0.007; OPG/type III collagen: r = 0.39, = 0.002, OPG/type IV collagen: r = 0.27, = 0.03; OPG/elastin: r = 0.42, = 0.001; OPN/collagen type I: r = 0.34, = 0.007; OPN/collagen type II: r = 0.52, = 0.000; OPN/elastin: r = 0.61, = 0.001). OPN overexpression accompanies calcium deposit (CA) formation with the protein localized in the calcium deposit, whereas OPG is located outside the CA. Although OPN and OPG seem to play a similar function (inhibiting calcification), these glycoproteins have different tissue localizations and independent expression regulation. The independent expression regulation presumably depends on the factors responsible for stimulating the synthesis of collagens and elastin.
骨桥蛋白（OPN）和骨保护素（OPG）是参与组织生物矿化调节的糖蛋白。该项目的目的是验证以下假设：主动脉壁中OPN和OPG的含量会随着动脉粥样硬化的发展而增加，并且这些蛋白质与细胞外动脉基质中的主要蛋白质存在定量关系。已对101个主动脉切片中OPN和OPG的含量进行了定量和定性分析。此外，还进行了酶联免疫吸附测定（ELISA）试验，以确定组织中I-IV型胶原蛋白和弹性蛋白的含量。已建立了生化数据与患者年龄/性别、动脉粥样硬化阶段以及组织中钙化发生情况之间的相关性。我们首次报告了OPN或OPG与各种类型胶原蛋白和弹性蛋白含量之间的相关性（OPG/I型胶原蛋白相关性：r = 0.37，P = 0.004；OPG/II型胶原蛋白：r = 0.34，P = 0.007；OPG/III型胶原蛋白：r = 0.39，P = 0.002，OPG/IV型胶原蛋白：r = 0.27，P = 0.03；OPG/弹性蛋白：r = 0.42，P = 0.001；OPN/I型胶原蛋白：r = 0.34，P = 0.00 —— 此处原文有误，应为P = 0.007；OPN/II型胶原蛋白：r = 0.52，P = 0.000；OPN/弹性蛋白：r = 0.61，P = 0.001）。OPN的过表达伴随着钙沉积物（CA）的形成，该蛋白定位于钙沉积物中，而OPG位于CA之外。尽管OPN和OPG似乎发挥着相似的功能（抑制钙化），但这些糖蛋白具有不同的组织定位和独立的表达调控。这种独立的表达调控可能取决于负责刺激胶原蛋白和弹性蛋白合成的因素。
