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血小板糖蛋白VI缺失与脾酪氨酸激酶抑制对小鼠颈静脉穿刺伤口结构的对比作用

Contrasting Effects of Platelet GPVI Deletion Versus Syk Inhibition on Mouse Jugular Vein Puncture Wound Structure.

作者信息

Pokrovskaya Irina D, Ball Kelly K, Webb Michael W, Joshi Smita, Rhee Sung W, Ware Jerry, Storrie Brian

机构信息

Department of Physiology and Cell Biology, College of Medicine, University of Arkansas for Medical Sciences, Little Rock, AR 77205, USA.

Department of Molecular and Cellular Biochemistry, College of Medicine, University of Kentucky, Lexington, KY 40536, USA.

出版信息

Int J Mol Sci. 2025 May 1;26(9):4294. doi: 10.3390/ijms26094294.

Abstract

Platelet glycoprotein (GP)VI is a transmembrane protein that was originally characterized as a collagen receptor supporting platelet adhesion and activation through its association with the Fc receptor γ-chain (FcRγ). The FcRγ subunit contains immunoreceptor tyrosine-based activation motifs (ITAMs) that recruit and activate Syk (spleen tyrosine kinase), a key player in intracellular signaling pathways. The absence or dysfunction of GPVI produces a mild bleeding defect in humans like the impaired hemostasis reported in the murine knockout. Here, we took an ultrastructure approach to examine the impact of ligand binding to GPVI versus the downstream pharmacologic inhibition of the GPVI-dependent ITAM signaling pathway. Clots were generated for analysis following a puncture wound in the mouse external jugular vein. Images were obtained using mice genetically missing GPVI and mice pretreated with the Syk inhibitor, BI 1002494. Our study was designed to test the hypothesis that the predominant contribution of GPVI to hemostasis is mediated by a Syk-dependent signaling cascade. If true, the clot structure observed with a Syk inhibitor versus the GPVI knockout would be similar. If the extracellular domains of the protein had a Syk-independent platelet adhesion role, then significant comparative differences in the thrombus structure would be expected. Our results clearly indicate an important, Syk-independent role of the GPVI extracellular domain in the adherence of platelets within the intravascular crown of a growing venous clot, a site distant from exposed collagen-rich adventitia. In striking contrast, the adventitial proximal role of GPVI was Syk-dependent, with the GPVI knockout and Syk inhibitor giving the same, limited structural outcome of collagen-proximal platelet cytosol loss and a thinned extravascular cap. Consistent with the lesser role of Syk-dependent processes on the thrombus structure, the Syk inhibitor had no detectable effect on jugular puncture wound bleeding times, while the knockout had a statistically significant, but modest effect on bleeding time. Based on this contrast, we suggest that Syk inhibition may be the more selective approach to modulating the role of GPVI in occlusive clotting.

摘要

血小板糖蛋白(GP)VI是一种跨膜蛋白,最初被鉴定为一种胶原受体,通过与Fc受体γ链(FcRγ)结合来支持血小板的黏附和激活。FcRγ亚基包含基于免疫受体酪氨酸的激活基序(ITAM),可募集并激活Syk(脾酪氨酸激酶),后者是细胞内信号通路中的关键因子。GPVI的缺失或功能障碍会在人类中导致轻度出血缺陷,类似于在小鼠基因敲除中报道的止血功能受损。在此,我们采用超微结构方法来研究配体与GPVI结合的影响,以及与GPVI依赖性ITAM信号通路的下游药理学抑制作用的对比。在小鼠颈外静脉穿刺伤口后生成凝块用于分析。使用基因缺失GPVI的小鼠和用Syk抑制剂BI 1002494预处理的小鼠获取图像。我们的研究旨在检验以下假设:GPVI对止血的主要贡献是由Syk依赖性信号级联介导的。如果是这样,那么用Syk抑制剂与GPVI基因敲除观察到的凝块结构将相似。如果该蛋白的细胞外结构域具有不依赖Syk的血小板黏附作用,那么血栓结构将会有显著的比较差异。我们的结果清楚地表明,GPVI细胞外结构域在生长中的静脉凝块血管内冠内血小板黏附中具有重要的、不依赖Syk的作用,该部位远离富含胶原的外膜。形成鲜明对比的是,GPVI在外膜近端的作用是依赖Syk的,GPVI基因敲除和Syk抑制剂导致相同的、有限的结构结果,即胶原近端血小板胞质丢失和血管外帽变薄。与Syk依赖性过程对血栓结构的作用较小一致,Syk抑制剂对颈静脉穿刺伤口出血时间没有可检测到的影响,而基因敲除对出血时间有统计学上显著但适度的影响。基于这种对比,我们认为抑制Syk可能是调节GPVI在闭塞性凝血中作用的更具选择性的方法。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/94e9/12072639/394f69a934e9/ijms-26-04294-g001.jpg

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