scholarly journals Quantitative Differentiation of Cell Surface-Bound and Internalized Cationic Gold Nanoparticles Using Mass Spectrometry

ACS Nano ◽  
2016 ◽  
Vol 10 (7) ◽  
pp. 6731-6736 ◽  
Author(s):  
Singyuk Hou ◽  
Kristen N. Sikora ◽  
Rui Tang ◽  
Yuanchang Liu ◽  
Yi-Wei Lee ◽  
...  
2008 ◽  
Vol 2 (2) ◽  
pp. 152-156 ◽  
Author(s):  
Guoping Chen ◽  
Michiaki Takezawa ◽  
Naoki Kawazoe ◽  
Tetsuya Tateishi

2014 ◽  
Vol 2014 ◽  
pp. 1-11 ◽  
Author(s):  
Yunlong Pan ◽  
Qing Wu ◽  
Li Qin ◽  
Jiye Cai ◽  
Bin Du

The early stages of angiogenesis can be divided into three steps: endothelial cell proliferation, migration, and tube formation. Vascular endothelial growth factor (VEGF) is considered the most important proangiogenic factor; in particular, VEGF165plays a critical role in angiogenesis. Here, we evaluated whether gold nanoparticles (AuNPs) could inhibit the VEGF165-induced human umbilical vein endothelial cell (HUVEC) migration and tube formation. AuNPs and VEGF165were coincubated overnight at 4°C, after which the effects on cell migration and tube formation were assessed. Cell migration was assessed using a modified wound-healing assay and a transwell chamber assay; tube formation was assessed using a capillary-like tube formation assay and a chick chorioallantoic membrane (CAM) assay. We additionally detected the cell surface morphology and ultrastructure using atomic force microscopy (AFM). Furthermore, Akt phosphorylation downstream of VEGFR-2/PI3K in HUVECs was determined in a Western blot analysis. Our study demonstrated that AuNPs significantly inhibited VEGF165-induced HUVEC migration and tube formation by affecting the cell surface ultrastructure, cytoskeleton and might have inhibited angiogenesis via the Akt pathway.


Open Biology ◽  
2011 ◽  
Vol 1 (3) ◽  
pp. 110010 ◽  
Author(s):  
Clive Metcalfe ◽  
Peter Cresswell ◽  
Laura Ciaccia ◽  
Benjamin Thomas ◽  
A. Neil Barclay

Redox conditions change in events such as immune and platelet activation, and during viral infection, but the biochemical consequences are not well characterized. There is evidence that some disulfide bonds in membrane proteins are labile while others that are probably structurally important are not exposed at the protein surface. We have developed a proteomic/mass spectrometry method to screen for and identify non-structural, redox-labile disulfide bonds in leucocyte cell-surface proteins. These labile disulfide bonds are common, with several classes of proteins being identified and around 30 membrane proteins regularly identified under different reducing conditions including using enzymes such as thioredoxin. The proteins identified include integrins, receptors, transporters and cell–cell recognition proteins. In many cases, at least one cysteine residue was identified by mass spectrometry as being modified by the reduction process. In some cases, functional changes are predicted (e.g. in integrins and cytokine receptors) but the scale of molecular changes in membrane proteins observed suggests that widespread effects are likely on many different types of proteins including enzymes, adhesion proteins and transporters. The results imply that membrane protein activity is being modulated by a ‘redox regulator’ mechanism.


PLoS ONE ◽  
2016 ◽  
Vol 11 (8) ◽  
pp. e0159824 ◽  
Author(s):  
Christian Niehage ◽  
Jana Karbanová ◽  
Charlotte Steenblock ◽  
Denis Corbeil ◽  
Bernard Hoflack

2018 ◽  
Vol 54 (43) ◽  
pp. 5486-5489
Author(s):  
Qing-Ran Bai ◽  
Lu Dong ◽  
Yi Hao ◽  
Xing Chen ◽  
Qin Shen

Metabolic labeling with azidosugars in a neural stem cell (NSC)-enriched endothelial coculture followed by mass-spectrometry profiling identifies sialoglycoproteins on NSCs.


2018 ◽  
Vol 54 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Daiki Muko ◽  
Takanori Ikenaga ◽  
Masanori Kasai ◽  
Janice B. Rabor ◽  
Atsushi Nishitani ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document