Phosphorylation-induced formation of a cytochrome c-peptide complex: a novel fluorescent sensing platform for protein kinase assay

2016 ◽  
Vol 52 (4) ◽  
pp. 776-779 ◽  
Author(s):  
Shuang Wu ◽  
Xiang-Juan Kong ◽  
Yao Cen ◽  
Ru-Qin Yu ◽  
Xia Chu

A novel fluorescent sensing platform has been developed for protein kinase assay based on the phosphorylation-induced formation of a cytochrome c-peptide complex.

RSC Advances ◽  
2014 ◽  
Vol 4 (67) ◽  
pp. 35422-35427 ◽  
Author(s):  
Yue He ◽  
Bining Jiao

An ultrasensitive and straightforward fluorescent sensing platform for S1 nuclease activity has been developed based on cytochrome c.


2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Anna Kanegae ◽  
Yusuke Takata ◽  
Ippei Takashima ◽  
Shohei Uchinomiya ◽  
Ryosuke Kawagoe ◽  
...  

AbstractDespite continuous and active development of fluorescent metal-ion probes, their molecular design for ratiometric detection is restricted by the limited choice of available sensing mechanisms. Here we present a multicolor and ratiometric fluorescent sensing platform for metal ions based on the interaction between the metal ion and the aromatic ring of a fluorophore (arene–metal-ion, AM, coordination). Our molecular design provided the probes possessing a 1,9-bis(2′-pyridyl)-2,5,8-triazanonane as a flexible metal ion binding unit attached to a tricyclic fluorophore. This architecture allows to sense various metal ions, such as Zn(II), Cu(II), Cd(II), Ag(I), and Hg(II) with emission red-shifts. We showed that this probe design is applicable to a series of tricyclic fluorophores, which allow ratiometric detection of the metal ions from the blue to the near-infrared wavelengths. X-ray crystallography and theoretical calculations indicate that the coordinated metal ion has van der Waals contact with the fluorophore, perturbing the dye’s electronic structure and ring conformation to induce the emission red-shift. A set of the probes was useful for the differential sensing of eight metal ions in a one-pot single titration via principal component analysis. We also demonstrate that a xanthene fluorophore is applicable to the ratiometric imaging of metal ions under live-cell conditions.


2013 ◽  
Vol 41 ◽  
pp. 442-445 ◽  
Author(s):  
Rong Hu ◽  
Ya-Ru Liu ◽  
Xiao-Bing Zhang ◽  
Weihong Tan ◽  
Guo-Li Shen ◽  
...  

2002 ◽  
Vol 282 (1) ◽  
pp. H320-H327 ◽  
Author(s):  
Yukitaka Shizukuda ◽  
Peter M. Buttrick

We hypothesized that thromboxane A2 (TxA2) receptor stimulation directly induces apoptosis in adult cardiac myocytes. To investigate this, we exposed cultured adult rat ventricular myocytes (ARVM) to a TxA2 mimetic [1S-[1α,2α(Z),3β(1E,3S*),4α]]-7-[3-[3-hydroxy-4-(4-iodophenoxy)-1-butenyl]-7-oxabicyclo[2.2.1]hept-2-yl]-5-heptenoic acid (I-BOP) for 24 h. Stimulation with I-BOP induced apoptosis in a dose-dependent manner and was completely prevented by a TxA2 receptor antagonist, SQ-29548. We further investigated the role of protein kinase C (PKC) in this process. TxA2 stimulation resulted in membrane translocation of PKC-ζ but not PKC-α, -βII, -δ, and -ε at 3 min and 1 h. The activation of PKC-ζ by I-BOP was confirmed using an immune complex kinase assay. Treatment of ARVM with a cell-permeable PKC-ζ pseudosubstrate peptide (ζ-PS) significantly attenuated apoptosis by I-BOP. In addition, I-BOP treatment decreased baseline Akt activity and its decrease was reversed by treatment with ζ-PS. The inhibition of phosphatidylinositol 3-kinase upstream of Akt by wortmannin or LY-294002 abolished the antiapoptotic effect of ζ-PS. Therefore, our results suggest that the activation of PKC-ζ modulates TxA2 receptor-mediated apoptosis at least, in part, through Akt activity in adult cardiac myocytes.


Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 10271-10276 ◽  
Author(s):  
Lawren C. Wu ◽  
Paul B. Laub ◽  
Gulnur A. Elove ◽  
Jannette Carey ◽  
Heinrich Roder

1991 ◽  
Vol 11 (2) ◽  
pp. 913-919 ◽  
Author(s):  
H App ◽  
R Hazan ◽  
A Zilberstein ◽  
A Ullrich ◽  
J Schlessinger ◽  
...  

Raf-1 serine- and threonine-specific protein kinase is transiently activated in cells expressing the epidermal growth factor (EGF) receptor upon treatment with EGF. The stimulated EGF receptor coimmunoprecipitates with Raf-1 kinase and mediates protein kinase C-independent phosphorylation of Raf-1 on serine residues. Hyperphosphorylated Raf-1 has lower mobility on sodium dodecyl sulfate gels and has sixfold-increased activity in immunocomplex kinase assay with histone H1 or Raf-1 sequence-derived peptide as a substrate. Raf-1 activation requires kinase-active EGF receptor; a point mutant lacking tyrosine kinase activity in inactive in Raf-1 coupling and association. It is noteworthy that tyrosine phosphorylation of c-Raf-1 induced by EGF was not detected in these cells. These observations suggest that Raf-1 kinase may act as an important downstream effector of EGF signal transduction.


2015 ◽  
Vol 3 (17) ◽  
pp. 3541-3547 ◽  
Author(s):  
Huaming Wang ◽  
Wei Tang ◽  
Hejia Wei ◽  
Yan Zhao ◽  
Shichao Hu ◽  
...  

A fluorescent dye-intercalated DNA dendrimer probe was integrated with electrospun nanofibers to create an amplified sensing platform for disease-related species.


2018 ◽  
Vol 90 (24) ◽  
pp. 14507-14513 ◽  
Author(s):  
Lili Tong ◽  
Xiuxiu Wang ◽  
Wen Gao ◽  
Zhenhua Liu ◽  
Zhenzhen Chen ◽  
...  

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