Sulphide activity-dependent multicolor emission dyes and its applications in vivo imaging

The Analyst ◽  
2021 ◽  
Author(s):  
Yongbin Zhang ◽  
le wen ◽  
Weijie Zhang ◽  
yongkang yue ◽  
Jianbin Chao ◽  
...  
Keyword(s):  
In Vivo Imaging ◽  
Sulfur Species ◽  
Physiological Processes ◽  
Reactive Sulfur Species ◽  
Activity Dependent

Reactive sulfur species (RSS) plays pivotal roles in various pathological and physiological processes. There exists an intricate relevance in generation and metabolism among these substances. Although they are nucleophilic, there...

scholarly journals Is aldehyde dehydrogenase inhibited by sulfur compounds? In vitro and in vivo studies

2018 ◽  
Vol 65 (1) ◽  
pp. 125-132 ◽  
Author(s):  
Malgorzata Iciek ◽  
Magdalena Górny ◽  
Anna Bilska-Wilkosz ◽  
Danuta Kowalczyk-Pachel
Keyword(s):  
Aldehyde Dehydrogenase ◽  
Active Site ◽  
Ethanol Metabolism ◽  
Aldh Activity ◽  
Sulfur Species ◽  
Reactive Sulfur Species ◽  
Allyl Sulfides ◽  
Sulfur Containing

Aldehyde dehydrogenase (ALDH) catalyzes the critical step of ethanol metabolism, i.e.  transformation of toxic acetaldehyde to acetic acid. It is a redox sensitive protein with the key Cys in its active site. Recently, it has been documented that activity of some proteins can be modified by sulfur-containing molecules called reactive sulfur species leading to the formation of hydropersulfides. The aim of the present study was to examine whether ALDH activity can be modified through this way.Studies were performed in vitro using yeast ALDH and various reactive sulfur species, including Na2S, GSSH, K2Sx, Na2S2O3, and garlic-derived allyl sulfides. The effect of garlic-derived trisulfide on ALDH activity was  also studied  in vivo in the rat liver.The obtained results clearly demonstrated that ALDH could be regulated by sulfur species which inhibited its enzymatic activity. The results also suggested that not H2S but polysulfides or hydropersulfides were the oxidizing species responsible for this modification. This process was easily reversible by reducing agents. After the treatment with polysulfides or hydropersulfides the level of protein-bound sulfur increased, while the activity of the enzyme dramatically decreased. Moreover, the study demonstrated that ALDH activity was inhibited in vivo in the rat liver after garlic-derived trisulfide administration. This is the first study reporting the regulation of  ALDH activity by sulfane sulfur species and the results suggest that it led to the inhibition of the enzyme.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

In vivo imaging of beta-amyloid load in transgenic rodents with [F-18]FDDNP microPET

2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S588-S588
Author(s):  
Vladimir Kepe ◽  
Gregory M Cole ◽  
Jie Liu ◽  
Dorothy G Flood ◽  
Stephen P Trusko ◽  
...  
Keyword(s):  
In Vivo Imaging ◽  
Beta Amyloid ◽  
Amyloid Load

In vivo imaging of liver injury and regeneration by functional two-photon microscopy

2016 ◽  
Vol 54 (12) ◽  
pp. 1343-1404
Author(s):  
A Ghallab ◽  
R Reif ◽  
R Hassan ◽  
AS Seddek ◽  
JG Hengstler
Keyword(s):  
Liver Injury ◽  
In Vivo Imaging ◽  
Two Photon Microscopy ◽  
Two Photon

Platelet Microtubules in Clot Structure Formation and Contractile Force Generation: Investigation of a Controversy

1986 ◽  
Vol 56 (01) ◽  
pp. 023-027 ◽  
Author(s):  
C J Jen ◽  
L V McIntire
Keyword(s):  
Network Formation ◽  
Contractile Force ◽  
Second Phase ◽  
Clot Retraction ◽  
Forming Process ◽  
Microtubule Organization ◽  
Physiological Processes ◽  
Fibrin Network ◽  
Two Parameters

SummaryWhether platelet microtubules are involved in clot retraction/ contraction has been controversial. To address this question we have simultaneously measured two clotting parameters, clot structural rigidity and isometric contractile force, using a rheological technique. For recalcified PRP clots these two parameters began rising together at about 15 min after CaCl2 addition. In the concentration range affecting microtubule organization in platelets, colchicine, vinca alkaloids and taxol demonstrated insignificant effects on both clotting parameters of a recalcified PRP clot. For PRP clots induced by adding small amounts of exogenous thrombin, the kinetic curves of clot rigidity were biphasic and without a lag time. The first phase corresponded to a platelet-independent network forming process, while the second phase corresponded to a platelet-dependent process. These PRP clots began generating contractile force at the onset of the second phase. For both rigidity and force parameters, only the second phase of clotting kinetics was retarded by microtubule affecting reagents. When PRP samples were clotted by adding a mixture of CaCl2 and thrombin, the second phase clotting was accelerated and became superimposed on the first phase. The inhibitory effects of micro tubule affecting reagents became less pronounced. Thrombin clotting of a two-component system (washed platelets/ purified fibrinogen) was also biphasic, with the second phase being microtubule-dependent. In conclusion, platelet microtubules are important in PRP clotted with low concentrations of thrombin, during which fibrin network formation precedes platelet-fibrin interactions. On the other hand they are unimportant if a PRP clot is induced by recalcification, during which the fibrin network is constructed in the presence of platelet-fibrin interactions. The latter is likely to be more analogous to physiological processes in vivo.

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