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定量蛋白质组学鉴定出一种与垂体腺瘤 EMT 相关的新型侵袭性生物标志物。

Quantitative proteomics identified a novel invasion biomarker associated with EMT in pituitary adenomas.

机构信息

Department of Neurosurgery, Beijing Tiantan Hospital, Capital Medical University, Beijing, China.

Central Laboratory, Capital Medical University, Beijing, China.

出版信息

Front Endocrinol (Lausanne). 2023 Mar 3;14:1137648. doi: 10.3389/fendo.2023.1137648. eCollection 2023.

DOI:10.3389/fendo.2023.1137648
PMID:36936141
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10020714/
Abstract

BACKGROUND

Complete resection of invasive pituitary adenoma is usually difficult, resulting in a high recurrence rate. Therefore, it is needed to find potential diagnostic markers and therapeutic targets for invasive pituitary adenoma.

METHODS

We collected samples from patients with invasive and non-invasive pituitary adenomas from Beijing Tiantan Hospital for protein extraction and quantitative analysis. We identified differential proteins (DEPs) by differential analysis of the two groups. The intersection of differential proteins related to invasion and epithelial-mesenchymal transition (EMT) in the GeneCards database was identified as EMT-DEPs. The protein network of EMT-DEPs was analyzed using the STRING database and Cytoscape software, and the hub EMT-DEPs were obtained by the MCC algorithm of the cytoHubba plugin. Correlation analysis was used to obtain the interpairing proteins among EMT-DEPs, and core EMT-DEPs were identified based on the number of paired proteins. The Venn program was used to identify the intersection of hub EMT-DEPs and core EMT-DEPs as key EMT-DEPs. Finally, a series of analyses plus experiments were used to verify the correlation of the target protein with invasion and EMT in pituitary adenoma.

RESULTS

Quantitative comparison of proteins between invasive and non-invasive pituitary adenomas indicated 833 differential proteins. The overlaps of EMT-related proteins and differential proteins consisted of 46 EMT-DEPs. There were 6 intersections between the hub EMT-DEPs and core EMT-DEPs. Using quantitative protein data and GSE169498 chip, we found that solute carrier family 2 member 1 (SLC2A1) was our target protein. SLC2A1 was significantly correlated with the invasiveness of pituitary adenoma, and the ROC curve was satisfactory. The functions and pathways of SLC2A1 and paired protein enrichment were closely linked to the EMT. Consistently, SLC2A1 expression was significantly and positively correlated with the expression of classical markers of EMT. The final experiment revealed that SLC2A1 was significantly upregulated in invasive pituitary adenoma.

CONCLUSION

SLC2A1 is significantly upregulated in invasive pituitary adenoma with satisfactory predictive value. It may regulate EMT. It may be a potential diagnostic marker for invasive pituitary adenoma.

摘要

背景

侵袭性垂体腺瘤的完全切除通常较为困难，导致复发率较高。因此，需要寻找侵袭性垂体腺瘤的潜在诊断标志物和治疗靶点。

方法

我们从北京天坛医院的侵袭性和非侵袭性垂体腺瘤患者中收集样本进行蛋白质提取和定量分析。通过两组间的差异分析，我们确定了差异蛋白（DEPs）。在 GeneCards 数据库中，鉴定出与侵袭性和上皮间质转化（EMT）相关的差异蛋白的交集，将其定义为 EMT-DEPs。使用 STRING 数据库和 Cytoscape 软件分析 EMT-DEPs 的蛋白网络，并用 cytoHubba 插件的 MCC 算法获取关键 EMT-DEPs。通过相关性分析获得 EMT-DEPs 之间的配对蛋白，根据配对蛋白的数量确定核心 EMT-DEPs。使用 Venn 程序鉴定关键 EMT-DEPs 和核心 EMT-DEPs 的交集作为关键 EMT-DEPs。最后，通过一系列分析和实验验证目标蛋白与垂体腺瘤侵袭性和 EMT 的相关性。

结果

侵袭性和非侵袭性垂体腺瘤之间的蛋白定量比较表明，有 833 个差异蛋白。EMT 相关蛋白与差异蛋白的重叠包含 46 个 EMT-DEPs。关键 EMT-DEPs 和核心 EMT-DEPs 之间有 6 个交集。使用定量蛋白数据和 GSE169498 芯片，我们发现溶质载体家族 2 成员 1（SLC2A1）是我们的靶蛋白。SLC2A1 与垂体腺瘤的侵袭性显著相关，ROC 曲线令人满意。SLC2A1 和配对蛋白富集的功能和途径与 EMT 密切相关。一致地，SLC2A1 的表达与 EMT 的经典标志物的表达呈显著正相关。最终的实验表明，SLC2A1 在侵袭性垂体腺瘤中表达显著上调。

结论

SLC2A1 在侵袭性垂体腺瘤中表达显著上调，具有令人满意的预测价值。它可能调节 EMT。它可能是侵袭性垂体腺瘤的一个潜在诊断标志物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/0cf93c3e1161/fendo-14-1137648-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/0fb90d6bd4e3/fendo-14-1137648-g001.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/b42d88fc9a35/fendo-14-1137648-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/94551e72bda1/fendo-14-1137648-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/7b6bc09708a3/fendo-14-1137648-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/91841ec4e328/fendo-14-1137648-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/0cf93c3e1161/fendo-14-1137648-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/0fb90d6bd4e3/fendo-14-1137648-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/28f1dee2e814/fendo-14-1137648-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/f6bd9bc0e024/fendo-14-1137648-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/630487ab99e8/fendo-14-1137648-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/b42d88fc9a35/fendo-14-1137648-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/94551e72bda1/fendo-14-1137648-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/7b6bc09708a3/fendo-14-1137648-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/91841ec4e328/fendo-14-1137648-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/aa9c/10020714/0cf93c3e1161/fendo-14-1137648-g009.jpg

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