Abstract
Background. Increased expression of transforming growth factor beta-1 (TGF-β1) in malignant brain tumors promotes cancer cells survival enhancing their growth, migration, invasion, angiogenesis, immune system suppression. Objective is to study molecular mechanisms of TGF-β1 action on U87 human glioblastoma cells by means of proteomic high-resolution massspectrometry. Results. We have identified intracell signal pathways responsible for TGF-β1 involvement in malignant gliomas oncogenesis including differential expressed proteins of tight cell junctions, focal adhesion, histone deacetylases, heat shock, S100 family. Conclusions. Important patterns are determined that could be used for the development of new approaches for detection of glioblastoma metastasis candidate markers and potential therapy targets of this decease.
Highlights
Increased expression of transforming growth factor beta-1 (TGF-β1) in malignant brain tumors promotes cancer cells survival enhancing their growth, migration, invasion, angiogenesis, immune system suppression
We have identified intracell signal pathways responsible for TGF-β1 involvement in malignant gliomas oncogenesis including differential expressed proteins of tight cell junctions, focal adhesion, histone deacetylases, heat shock, S100 family
Important patterns are determined that could be used for the development of new approaches for detection of glioblastoma metastasis candidate markers and potential therapy targets of this decease
Summary
Increased expression of transforming growth factor beta-1 (TGF-β1) in malignant brain tumors promotes cancer cells survival enhancing their growth, migration, invasion, angiogenesis, immune system suppression. Результаты Мы использовали label-free количественный протеомный nano-LC–MS/MS метод для детектирования и сравнения ДЭБ в лизатах линии клеток глиобластомы человека U87 до и после обработки их TGF-β1. Для всех линий клеток ~91 % белков идентифицировали по более чем 2 пептидам. Коэффициент корреляции Пирсона для данных образцов клеток U87 до и после стимуляции TGF-β1 был 0,904–0,952. Во всех клеточных лизатах детектировались 2459 (95 % от 2589) белков, только в клетках U87 – 23 и 107 протеинов были уникальными для клеток U87 после их стимуляции TGF-β1. Статистически значимые (p < 0,05) изменения в экспрессии после обработки клеток TGF-β1 зарегистрированы для 656 белков. Из 2589 идентифицированных белков мы рассчитали количество протеинов (n = 656), экспрессия которых статистически значимо изменялась при стимуляции клеток U87 фактором TGF-β1. Участвующих в образовании плотных межклеточных контактов, после стимуляции TGF-β1 клеток U87
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