数字空间分析识别了-JNK作为早期前列腺癌侵袭性风险分层的生物标志物
Samaneh Eickelschulte1,2,3, Adam Kaczorowski4, Florian Janke3
1Junior Clinical Cooperation Unit, Multiparametric Methods for Early Detection of Prostate Cancer, German Cancer Research Center (DKFZ), Heidelberg, Germany.
Frontiers in oncology
|June 20, 2025
概括
酸化c-Jun N-终端蛋白激酶 (p-JNK) 在侵袭性前列腺癌 (PCa) 中被上调. 这一发现可能有助于分层PCa风险,并指导向治疗.
科学领域:
- 在瘤学瘤学.
- 分子生物学分子生物学
- 生物标志物发现发现
背景情况:
- 前列腺癌 (PCa) 是一种异质性疾病,具有不同的攻击性.
- 准确的风险分层对于有效的PCa管理至关重要.
- 数字空间分析 (DSP) 为PCa组织分析提供了一种新的方法.
研究的目的:
- 为了确定前列腺癌早期风险分层的新生物标志物.
- 调查特定信号通路在PCa进展中的作用.
- 评估DSP在识别攻击性PCa亚型中的实用性.
主要方法:
- 数字空间分析 (DSP) 分析了38名PCa患者中的94个区域.
- 评估了44种标记物的蛋白质表达,包括信号通路组件和免疫标记物.
- 免疫组织化学 (IHC) 在154名患者的单独队列中验证了生物标志物的发现.
主要成果:
- DSP确定了Ki-67和化c-Jun N-终端蛋白激酶T183/Y185 (p-JNK) 在激进的PCa (格莱森等级4-5) 和惰性PCa (格莱森等级3) 中被上调调节.
- 通过IHC证实了p-JNK的上调.
- 高的p-JNK表达与更短的生化复发时间相关.
结论:
- p-JNK可能会驱动PCa的进展,并作为侵袭性疾病的早期生物标志物.
- 通过DSP识别的生物标志物可以促进PCa管理和向治疗的开发.
- 需要进一步的研究来充分阐明p-JNK在PCa中的作用.
更多相关视频
12:23Phosphopeptide Enrichment Coupled with Label-free Quantitative Mass Spectrometry to Investigate the Phosphoproteome in Prostate Cancer
Published on: August 2, 2018
12.3K
13:19Microarray-based Identification of Individual HERV Loci Expression: Application to Biomarker Discovery in Prostate Cancer
Published on: November 2, 2013
16.7K
相关概念视频
01:20The JAK-STAT Signaling Pathway
9.3K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
9.3K
01:22PI3K/mTOR/AKT Signaling Pathway
4.0K
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a...
4.0K