Direct evidence of the key role of UV-formed peroxide species in photocatalytic gas–solid oxidation in air on anatase TiO2 particles

2020 ◽  
Vol 22 (4) ◽  
pp. 2200-2211 ◽  
Author(s):  
Irina Rudol’fovna Subbotina ◽  
Denis Valer’evich Barsukov

Surface peroxide species are key intermediates of photocatalytic oxidation at the TiO2 adsorbed water–gas interface.

AIP Advances ◽  
2018 ◽  
Vol 8 (10) ◽  
pp. 105319
Author(s):  
Zhaohui Qiu ◽  
Jing Huang ◽  
Rong Shen ◽  
Ying Wang ◽  
Xiaoyi Wu ◽  
...  

2003 ◽  
Vol 244 (2) ◽  
pp. 383-391 ◽  
Author(s):  
Teruhisa Ohno ◽  
Kojiro Tokieda ◽  
Suguru Higashida ◽  
Michio Matsumura

1999 ◽  
Vol 53 (4) ◽  
pp. 695-702 ◽  
Author(s):  
G Martra ◽  
S Coluccia ◽  
L Marchese ◽  
V Augugliaro ◽  
V Loddo ◽  
...  

2009 ◽  
Author(s):  
M. Karl Healey ◽  
Karen L. Campbell ◽  
Lynn Hasher ◽  
Lynn Ossher
Keyword(s):  

1999 ◽  
Vol 19 (1) ◽  
pp. 495-504 ◽  
Author(s):  
John Sok ◽  
Xiao-Zhong Wang ◽  
Nikoleta Batchvarova ◽  
Masahiko Kuroda ◽  
Heather Harding ◽  
...  

ABSTRACT CHOP (also called GADD153) is a stress-inducible nuclear protein that dimerizes with members of the C/EBP family of transcription factors and was initially identified as an inhibitor of C/EBP binding to classic C/EBP target genes. Subsequent experiments suggested a role for CHOP-C/EBP heterodimers in positively regulating gene expression; however, direct evidence that this is the case has so far not been uncovered. Here we describe the identification of a positively regulated direct CHOP-C/EBP target gene, that encoding murine carbonic anhydrase VI (CA-VI). The stress-inducible form of the gene is expressed from an internal promoter and encodes a novel intracellular form of what is normally a secreted protein. Stress-induced expression of CA-VI is both CHOP and C/EBPβ dependent in that it does not occur in cells deficient in either gene. A CHOP-responsive element was mapped to the inducibleCA-VI promoter, and in vitro footprinting revealed binding of CHOP-C/EBP heterodimers to that site. Rescue of CA-VIexpression in c/ebpβ−/− cells by exogenous C/EBPβ and a shorter, normally inhibitory isoform of the protein known as LIP suggests that the role of the C/EBP partner is limited to targeting the CHOP-containing heterodimer to the response element and points to a preeminent role for CHOP in CA-VI induction during stress.


Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3578
Author(s):  
Federica Mastroiacovo ◽  
Francesca Biagioni ◽  
Paola Lenzi ◽  
Larisa Ryskalin ◽  
Stefano Puglisi-Allegra ◽  
...  

The heat shock protein (HSP) 70 is considered the main hallmark in preclinical studies to stain the peri-infarct region defined area penumbra in preclinical models of brain ischemia. This protein is also considered as a potential disease modifier, which may improve the outcome of ischemic damage. In fact, the molecule HSP70 acts as a chaperonine being able to impact at several level the homeostasis of neurons. Despite being used routinely to stain area penumbra in light microscopy, the subcellular placement of this protein within area penumbra neurons, to our knowledge, remains undefined. This is key mostly when considering studies aimed at deciphering the functional role of this protein as a determinant of neuronal survival. The general subcellular placement of HSP70 was grossly reported in studies using confocal microscopy, although no direct visualization of this molecule at electron microscopy was carried out. The present study aims to provide a direct evidence of HSP70 within various subcellular compartments. In detail, by using ultrastructural morphometry to quantify HSP70 stoichiometrically detected by immuno-gold within specific organelles we could compare the compartmentalization of the molecule within area penumbra compared with control brain areas. The study indicates that two cell compartments in control conditions own a high density of HSP70, cytosolic vacuoles and mitochondria. In these organelles, HSP70 is present in amount exceeding several-fold the presence in the cytosol. Remarkably, within area penumbra a loss of such a specific polarization is documented. This leads to the depletion of HSP70 from mitochondria and mostly cell vacuoles. Such an effect is expected to lead to significant variations in the ability of HSP70 to exert its physiological roles. The present findings, beyond defining the neuronal compartmentalization of HSP70 within area penumbra may lead to a better comprehension of its beneficial/detrimental role in promoting neuronal survival.


Author(s):  
M.I. Ariëns ◽  
V. Chlan ◽  
P. Novák ◽  
L.G.A. van de Water ◽  
A.I. Dugulan ◽  
...  

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