Abstract：
Renalase (RNLS) is a recently discovered protein that plays an important role in the regulation of blood pressure by acting inside and outside cells. Intracellular RNLS is a FAD-dependent oxidoreductase that oxidizes isomeric forms of β-NAD(P)H. Extracellular renalase lacking its N-terminal peptide and cofactor FAD exerts various protective effects via non-catalytic mechanisms. Certain experimental evidence exists in the literature that the RP220 peptide (a 20-mer peptide corresponding to the amino acid sequence RNLS 220-239) reproduces a number of non-catalytic effects of this protein, acting on receptor proteins of the plasma membrane. The possibility of interaction of this peptide with intracellular proteins has not been studied. Taking into consideration the known role of RNLS as a possible antihypertensive factor, the aim of this study was to perform proteomic profiling of the kidneys of normotensive and hypertensive rats using RP220 as an affinity ligand. Proteomic (semi-quantitative) identification revealed changes in the relative content of about 200 individual proteins in the kidneys of hypertensive rats bound to the affinity sorbent as compared to the kidneys of normotensive animals. Increased binding of SHR renal proteins to RP220 over the normotensive control was found for proteins involved in the development of cardiovascular pathology. Decreased binding of the kidney proteins from hypertensive animals to RP220 was noted for components of the ubiquitin-proteasome system, ribosomes, and cytoskeleton.
摘要：
Renalase（RNLS）是最近发现的一种蛋白质，通过在细胞内外作用在血压调节中起重要作用。细胞内RNLS是一种FAD依赖性氧化还原酶，可氧化β-NAD（P）H的异构形式。缺乏其N末端肽和辅因子FAD的细胞外肾酶通过非催化机制发挥各种保护作用。文献中存在某些实验证据，表明RP220肽（对应于氨基酸序列RNLS220-239的20聚体肽）再现了该蛋白质的许多非催化作用，作用于质膜的受体蛋白。尚未研究该肽与细胞内蛋白质相互作用的可能性。考虑到RNLS作为可能的抗高血压因子的已知作用，本研究的目的是使用RP220作为亲和配体,对正常血压和高血压大鼠的肾脏进行蛋白质组学分析.蛋白质组学（半定量）鉴定显示，与正常血压动物的肾脏相比，与亲和吸附剂结合的高血压大鼠肾脏中约200种单个蛋白质的相对含量发生变化。与正常血压对照相比，发现SHR肾蛋白与RP220的结合增加，涉及心血管病理学发展的蛋白。对于泛素-蛋白酶体系统的成分，高血压动物的肾脏蛋白与RP220的结合减少。核糖体,和细胞骨架。
