In their recent study published in Nature,Yuan and colleagues enlighten the role of histone lysine crotonylation(Kcr)in brain tumor biology.They report a novel lysine-dependent mechanism through which glioblastoma ste...In their recent study published in Nature,Yuan and colleagues enlighten the role of histone lysine crotonylation(Kcr)in brain tumor biology.They report a novel lysine-dependent mechanism through which glioblastoma stem cells modulate type I interferon(IFNα/IFNβ)signaling to create an immunosuppressive environment.展开更多
Protein adsorption on biomaterials for bone substitution,such as calcium phosphates(CaP),evokes biological responses and shapes the interactions of biomaterials with the surrounding biological environment.Proteins ads...Protein adsorption on biomaterials for bone substitution,such as calcium phosphates(CaP),evokes biological responses and shapes the interactions of biomaterials with the surrounding biological environment.Proteins adsorb when CaP materials are combined with growth factor-rich hemoderivatives prior to implantation to achieve enhanced angiogenesis and stimulate new bone formation.However,the identification of the adsorbed proteins and their angiogenic effect on bone homeostasis remain incompletely investigated.In this study,we analyzed the adsorbed complex protein composition on CaP surfaces when using the hemoderivatives plasma,platelet lysate in plasma(PL),and washed platelet lysate proteins(wPL).We detected highly abundant,non-regenerative proteins and anti-angiogenic proteins adsorbed on CaP surfaces after incubation with PL and wPL by liquid chromatography and mass spectrometry(LC–MS)proteomics.Additionally,we measured a decreased amount of adsorbed pro-angiogenic growth factors.Tube formation assays with human umbilical endothelial cells demonstrated that the CaP surfaces only stimulate an angiogenic response when kept in the hemoderivative medium but not after washing with PBS.Our results highlight the necessity to correlate biomaterial surfaces with complex adsorbed protein compositions to tailor the biomaterial surface toward an enrichment of pro-angiogenic factors.展开更多
文摘In their recent study published in Nature,Yuan and colleagues enlighten the role of histone lysine crotonylation(Kcr)in brain tumor biology.They report a novel lysine-dependent mechanism through which glioblastoma stem cells modulate type I interferon(IFNα/IFNβ)signaling to create an immunosuppressive environment.
基金financially supported by the focus group BiomaTiCS of University Medical Center of the Johannes Gutenberg-University Mainz.K.J.was supported by the German Federal Ministry of Education and Research(BMBF 01EO1003/01EO1503).
文摘Protein adsorption on biomaterials for bone substitution,such as calcium phosphates(CaP),evokes biological responses and shapes the interactions of biomaterials with the surrounding biological environment.Proteins adsorb when CaP materials are combined with growth factor-rich hemoderivatives prior to implantation to achieve enhanced angiogenesis and stimulate new bone formation.However,the identification of the adsorbed proteins and their angiogenic effect on bone homeostasis remain incompletely investigated.In this study,we analyzed the adsorbed complex protein composition on CaP surfaces when using the hemoderivatives plasma,platelet lysate in plasma(PL),and washed platelet lysate proteins(wPL).We detected highly abundant,non-regenerative proteins and anti-angiogenic proteins adsorbed on CaP surfaces after incubation with PL and wPL by liquid chromatography and mass spectrometry(LC–MS)proteomics.Additionally,we measured a decreased amount of adsorbed pro-angiogenic growth factors.Tube formation assays with human umbilical endothelial cells demonstrated that the CaP surfaces only stimulate an angiogenic response when kept in the hemoderivative medium but not after washing with PBS.Our results highlight the necessity to correlate biomaterial surfaces with complex adsorbed protein compositions to tailor the biomaterial surface toward an enrichment of pro-angiogenic factors.