scholarly journals Simultaneous Detection of Carbon Monoxide and Viscosity Changes in Cells

2020 ◽  
Vol 59 (48) ◽  
pp. 21431-21435
Author(s):  
Jonathan A. Robson ◽  
Markéta Kubánková ◽  
Tamzin Bond ◽  
Rian A. Hendley ◽  
Andrew J. P. White ◽  
...  
2020 ◽  
Vol 132 (48) ◽  
pp. 21615-21619
Author(s):  
Jonathan A. Robson ◽  
Markéta Kubánková ◽  
Tamzin Bond ◽  
Rian A. Hendley ◽  
Andrew J. P. White ◽  
...  

2016 ◽  
Vol 52 (35) ◽  
pp. 5902-5911 ◽  
Author(s):  
Cristina Marín-Hernández ◽  
Anita Toscani ◽  
Félix Sancenón ◽  
James D. E. T. Wilton-Ely ◽  
Ramón Martínez-Máñez

An overview of the design of chromo-fluorogenic probes for the detection of carbon monoxide and their application to CO sensing in air, solution and in cells.


2015 ◽  
Vol 804 (1) ◽  
pp. 61 ◽  
Author(s):  
Travis S. Barman ◽  
Quinn M. Konopacky ◽  
Bruce Macintosh ◽  
Christian Marois

2016 ◽  
Vol 70 (6) ◽  
pp. 962-971 ◽  
Author(s):  
Kyle Thurmond ◽  
Zachary Loparo ◽  
William Partridge ◽  
Subith S. Vasu

2012 ◽  
Vol 303 (1) ◽  
pp. C92-C101 ◽  
Author(s):  
Melissa A. Riddle ◽  
Benjimen R. Walker

A novel vasodilatory influence of endothelial cell (EC) large-conductance Ca2+-activated K+ (BK) channels is present after in vivo exposure to chronic hypoxia (CH) and may exist in other pathological states. However, the mechanism of channel activation that results in altered vasoreactivity is unknown. Previously, we demonstrated that inhibition of either BK channels or heme oxygenase (HO) restores vasoconstrictor reactivity after CH. Additionally, administration of the scaffolding domain of caveolin (Cav)-1 inhibits EC BK activity and restores vasoconstrictor reactivity in this setting. These results led us to hypothesize that CH exposure results in a loss in Cav-1 inhibition of EC BK channels, resulting in their activation by HO-derived carbon monoxide (CO). Experiments were conducted on freshly dispersed aortic ECs from control and CH-exposed (barometric pressure: 380 mmHg for 48 h) rats. In electrophysiology experiments, outward currents were greater in cells from CH rats as well as from cells from control rats treated with the cholesterol-depleting agent methyl-β-cyclodextrin. These enhanced currents were returned to control by HO inhibition. Channel activity could be restored by the CO donor CO-releasing molecule (CORM)-2 during HO inhibition. Administration of the Cav-1 scaffolding domain eliminated BK currents in cells from CH rats, and current was not restored by the addition of CORM-2. Colocalization experiments in ECs from control and CH rats demonstrated an association between HO-2, Cav-1, and BK. We conclude that EC BK channel activity is HO dependent in the absence of the inhibitory effect of the Cav-1 scaffolding domain.


The Analyst ◽  
2021 ◽  
Vol 146 (1) ◽  
pp. 118-123
Author(s):  
Yang Tian ◽  
Wen-Li Jiang ◽  
Wen-Xin Wang ◽  
Jie Peng ◽  
Xue-Meng Li ◽  
...  

A novel near-infrared fluorescent probe (FDX-CO) is developed to detect CO with a large Stokes shift and long emission wavelength. The probe can monitor CO in cells by fluorescence imaging, and is successfully applied for visualizing CO in vivo.


Chlorocruorin is a dichroic red-green respiratory protein. It is chemically similar to haemo­globin, and is only found dissolved in the blood of certain marine annelid worms. Chlorocruorin is the characteristic blood pigment of the Serpulimorpha (serpulids and sabellids), but in the genus Serpula both chlorocruorin and haemoglobin are present together in the blood. This is the first time that two respiratory pigments have been found in the blood of one animal. Young individuals have relatively more haemoglobin, older ones more chlorocruorin. Within the serpulid genus Spirorbis , one species has chlorocruorin in its blood, an other has haemoglobin, while a third has neither pigment. As their habitats are similar, no functional explanation for these differences suggests itself. The oxygen affinity of all chlorocruorins tested is considerably lower than that of most haemoglobins. But in Serpula the oxygen affinities of the chlorocruorin and haemoglobin are the same as one an other. The carbon monoxide affinity of chlorocruorin (in Branchiomma ) is higher than that of any haemoglobin. Although Serpulimorpha have chlorocruorin in their blood, the haem present in their tissues (muscles, eggs, sperm ) is protohaem, not chlorocruorohaem. One genus, Potamilla , with chlorocruorin in its blood, has haem oglobin in the muscles. Chlorocruorin is known only from blood, and from the mucous tube of Myxicola ; none has been found in cells. Coelomic fluid contains none. Protohaem is secreted in to the protective tubes of both serpulids and sabellids. A proto-haemochromogen is present in the gut fluid of serpulids, recalling that found in crustaceans and molluscs.


2018 ◽  
Vol 114 (9) ◽  
pp. 2212-2220 ◽  
Author(s):  
Gerardo Abbandonato ◽  
Dario Polli ◽  
Daniele Viola ◽  
Giulio Cerullo ◽  
Barbara Storti ◽  
...  

2003 ◽  
pp. 53-60
Author(s):  
Ernst J. M. Speel ◽  
Diane Lawson ◽  
Frans C. S. Ramaekers ◽  
John R. Gosden ◽  
Anton H. N. Hopman

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