scholarly journals Direct Visualization of Live Zebrafish Glycans via Single‐Step Metabolic Labeling with Fluorophore‐Tagged Nucleotide Sugars

2019 ◽  
Vol 58 (40) ◽  
pp. 14327-14333 ◽  
Author(s):  
Senlian Hong ◽  
Pankaj Sahai‐Hernandez ◽  
Digantkumar Gopaldas Chapla ◽  
Kelley W. Moremen ◽  
David Traver ◽  
...  
2019 ◽  
Vol 131 (40) ◽  
pp. 14465-14471 ◽  
Author(s):  
Senlian Hong ◽  
Pankaj Sahai‐Hernandez ◽  
Digantkumar Gopaldas Chapla ◽  
Kelley W. Moremen ◽  
David Traver ◽  
...  

2019 ◽  
Author(s):  
Senlian Hong ◽  
Pankaj Sahai-Hernandez ◽  
David Traver ◽  
Peng Wu

ABSTRACTDynamic turnover of cell-surface glycans is involved in a myriad of biological events, making this process an attractive target for in vivo molecular imaging. The metabolic glycan labeling coupled with ‘bioorthogonal chemistry’ has paved the way for visulizing glycans in living organisms. However, a two-step labeling sequence is required, which is prone to tissue penetration difficulties of the imaging probes. Here, by exploring the substrate promiscuity of endogenous glycosyltransferases, we developed a single-step fluorescent glycan labeling strategy by using fluorophore-tagged analogs of nucleotide sugars directly. Injecting the fluorophore-tagged sialic acid and fucose into the yolk of zebrafish embryos at the one-cell stage enables a systematic imaging of sialylation and fucosylation in live zebrafish embryos at various developmental stages. From these studies, we obtained insights into the role of sialylated and fucosylated glycans in zebrafish hematopoiesis.


2019 ◽  
Vol 144 (08) ◽  
pp. 547-552
Author(s):  
Michaela Merten ◽  
Peter Sattler ◽  
Christian Karagiannidis

AbstractBedside percutaneous dilatational tracheostomy has become one of the most commonly used interventions in ICU medicine. Different techniques have been developed, but guidance of percutaneous dilatational tracheostomy by video bronchoscope has been suggested to be clinically reasonable for direct visualization. The current Step-by-Step tutorial gives a detailed instruction of the procedure with visualization of every single step offering tips and pitfalls of the procedure.


Author(s):  
S. W. Hui ◽  
T. P. Stewart

Direct electron microscopic study of biological molecules has been hampered by such factors as radiation damage, lack of contrast and vacuum drying. In certain cases, however, the difficulties may be overcome by using redundent structural information from repeating units and by various specimen preservation methods. With bilayers of phospholipids in which both the solid and fluid phases co-exist, the ordering of the hydrocarbon chains may be utilized to form diffraction contrast images. Domains of different molecular packings may be recgnizable by placing properly chosen filters in the diffraction plane. These domains would correspond to those observed by freeze fracture, if certain distinctive undulating patterns are associated with certain molecular packing, as suggested by X-ray diffraction studies. By using an environmental stage, we were able to directly observe these domains in bilayers of mixed phospholipids at various temperatures at which their phases change from misible to inmissible states.


2007 ◽  
Vol 177 (4S) ◽  
pp. 319-319
Author(s):  
Naoto Sassa ◽  
Ryohei Hattori ◽  
Yoshinari Ono ◽  
Tokunori Yamamoto ◽  
Momokazu Gotoh

2005 ◽  
Vol 173 (4S) ◽  
pp. 240-240
Author(s):  
Premal J. Desai ◽  
David A. Hadley ◽  
Lincoln J. Maynes ◽  
D. Duane Baldwin

2009 ◽  
Vol 42 (05) ◽  
Author(s):  
MD Filiou ◽  
YY Zhang ◽  
B Bisle ◽  
E Frank ◽  
MS Kessler ◽  
...  

1996 ◽  
Vol 75 (03) ◽  
pp. 497-502 ◽  
Author(s):  
Hadewijch L M Pekelharing ◽  
Henne A Kleinveld ◽  
Pieter F C.C.M Duif ◽  
Bonno N Bouma ◽  
Herman J M van Rijn

SummaryLp(a) is an LDL-like lipoprotein plus an additional apolipoprotein apo(a). Based on the structural homology of apo(a) with plasminogen, it is hypothesized that Lp(a) interferes with fibrinolysis. Extracellular matrix (ECM) produced by human umbilical vein endothelial cells was used to study the effect of Lp(a) and LDL on plasminogen binding and activation. Both lipoproteins were isolated from the same plasma in a single step. Plasminogen bound to ECM via its lysine binding sites. Lp(a) as well as LDL were capable of competing with plasminogen binding. The degree of inhibition was dependent on the lipoprotein donor as well as the ECM donor. When Lp(a) and LDL obtained from one donor were compared, Lp(a) was always a much more potent competitor. The effect of both lipoproteins on plasminogen binding was reflected in their effect on plasminogen activation. It is speculated that Lp(a) interacts with ECM via its LDL-like lipoprotein moiety as well as via its apo(a) moiety.


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