Liu Shuang
School of Health Sciences, Purdue University, 550 Stadium Mall Drive, West Lafayette, Indiana 47907, United States.
Bioconjug Chem. 2015 Aug 19;26(8):1413-38. doi: 10.1021/acs.bioconjchem.5b00327. Epub 2015 Aug 3.
Angiogenesis is a requirement for tumor growth and metastasis. The angiogenic process depends on vascular endothelial cell migration and invasion, and is regulated by various cell adhesion receptors. Integrins are such a family of receptors that facilitate the cellular adhesion to and migration on extracellular matrix proteins in the intercellular spaces and basement membranes. Among 24 members of the integrin family, αvβ3 is studied most extensively for its role in tumor angiogenesis and metastasis. The αvβ3 is expressed at relatively low levels on epithelial cells and mature endothelial cells, but it is highly expressed on the activated endothelial cells of tumor neovasculature and some tumor cells. This restricted expression makes αvβ3 an excellent target to develop antiangiogenic drugs and diagnostic molecular imaging probes. Since αvβ3 is a receptor for extracellular matrix proteins with one or more RGD tripeptide sequence, many radiolabeled cyclic RGD peptides have been evaluated as "αvβ3-targeted" radiotracers for tumor imaging over the past decade. This article will use the dimeric and tetrameric cyclic RGD peptides developed in our laboratories as examples to illustrate basic principles for development of αvβ3-targeted radiotracers. It will focus on different approaches to maximize the radiotracer tumor uptake and tumor/background ratios. This article will also discuss some important assays for preclinical evaluations of integrin-targeted radiotracers. In general, multimerization of cyclic RGD peptides increases their integrin binding affinity and the tumor uptake and retention times of their radiotracers. Regardless of their multiplicity, the capability of cyclic RGD peptides to bind other integrins (namely, αvβ5, α5β1, α6β4, α4β1, and αvβ6) is expected to enhance the radiotracer tumor uptake due to the increased integrin population. The results from preclinical and clinical studies clearly show that radiolabeled cyclic RGD peptides (such as (99m)Tc-3P-RGD2, (18)F-Alfatide-I, and (18)F-Alfatide-II) are useful as the molecular imaging probes for early cancer detection and noninvasive monitoring of the tumor response to antiangiogenic therapy.
血管生成是肿瘤生长和转移的必要条件。血管生成过程依赖于血管内皮细胞的迁移和侵袭,并受多种细胞粘附受体的调节。整合素就是这样一类受体,它有助于细胞粘附于细胞间空间和基底膜中的细胞外基质蛋白并在其上迁移。在整合素家族的24个成员中,αvβ3因其在肿瘤血管生成和转移中的作用而得到了最广泛的研究。αvβ3在上皮细胞和成熟内皮细胞上表达水平相对较低,但在肿瘤新生血管的活化内皮细胞和一些肿瘤细胞上高度表达。这种局限性表达使αvβ3成为开发抗血管生成药物和诊断性分子成像探针的理想靶点。由于αvβ3是具有一个或多个RGD三肽序列的细胞外基质蛋白的受体,在过去十年中,许多放射性标记的环RGD肽已被评估为用于肿瘤成像的“αvβ3靶向”放射性示踪剂。本文将以我们实验室开发的二聚体和四聚体环RGD肽为例,说明开发αvβ3靶向放射性示踪剂的基本原理。它将专注于最大化放射性示踪剂肿瘤摄取和肿瘤/本底比值的不同方法。本文还将讨论一些用于整合素靶向放射性示踪剂临床前评估的重要检测方法。一般来说,环RGD肽的多聚化增加了它们与整合素的结合亲和力以及它们放射性示踪剂的肿瘤摄取和保留时间。无论其多聚程度如何,环RGD肽与其他整合素(即αvβ5、α5β1、α6β4、α4β1和αvβ6)结合的能力预计会由于整合素数量的增加而提高放射性示踪剂的肿瘤摄取。临床前和临床研究结果清楚地表明,放射性标记的环RGD肽(如(99m)Tc-3P-RGD2、(18)F-艾氟肽-I和(18)F-艾氟肽-II)可用作早期癌症检测和肿瘤对抗血管生成治疗反应的无创监测的分子成像探针。