scholarly journals Base-modified GDP-mannose derivatives and their substrate activity towards a yeast mannosyltransferase

2017 ◽  
Vol 452 ◽  
pp. 91-96
Author(s):  
Alice Collier ◽  
Gerd K. Wagner
Keyword(s):  
2021 ◽  
Vol 22 (6) ◽  
pp. 2820
Author(s):  
Stephan Altmann ◽  
Jürgen Mut ◽  
Natalia Wolf ◽  
Jutta Meißner-Weigl ◽  
Maximilian Rudert ◽  
...  

Metabolic glycoengineering enables a directed modification of cell surfaces by introducing target molecules to surface proteins displaying new features. Biochemical pathways involving glycans differ in dependence on the cell type; therefore, this technique should be tailored for the best results. We characterized metabolic glycoengineering in telomerase-immortalized human mesenchymal stromal cells (hMSC-TERT) as a model for primary hMSC, to investigate its applicability in TERT-modified cell lines. The metabolic incorporation of N-azidoacetylmannosamine (Ac4ManNAz) and N-alkyneacetylmannosamine (Ac4ManNAl) into the glycocalyx as a first step in the glycoengineering process revealed no adverse effects on cell viability or gene expression, and the in vitro multipotency (osteogenic and adipogenic differentiation potential) was maintained under these adapted culture conditions. In the second step, glycoengineered cells were modified with fluorescent dyes using Cu-mediated click chemistry. In these analyses, the two mannose derivatives showed superior incorporation efficiencies compared to glucose and galactose isomers. In time-dependent experiments, the incorporation of Ac4ManNAz was detectable for up to six days while Ac4ManNAl-derived metabolites were absent after two days. Taken together, these findings demonstrate the successful metabolic glycoengineering of immortalized hMSC resulting in transient cell surface modifications, and thus present a useful model to address different scientific questions regarding glycosylation processes in skeletal precursors.


1990 ◽  
Vol 111 (4) ◽  
pp. 1639-1643 ◽  
Author(s):  
S C Ho ◽  
M Schindler ◽  
J L Wang

Extracts of Bradyrhizobium japonicum were fractionated on Sepharose columns covalently derivatized with lactose. Elution of the material that was specifically bound to the affinity column with lactose yielded a protein of Mr approximately 38,000. Isoelectric focusing of this sample yielded two spots with pI values of 6.4 and 6.8. This protein specifically bound to galactose-containing glycoconjugates, but did not bind either to glucose or mannose. Derivatives of galactose at the C-2 position showed much weaker binding; there was an 18-fold difference in the relative binding affinities of galactose versus N-acetyl-D-galactosamine. These results indicate that we have purified a newly identified carbohydrate-binding protein from Bradyrhizobium japonicum, that can exquisitely distinguish galactose from its derivatives at the C-2 position.


1984 ◽  
Vol 15 (41) ◽  
Author(s):  
J. N. VOS ◽  
J. H. VAN BOOM ◽  
C. A. A. VAN BOECKEL ◽  
T. BEETZ
Keyword(s):  

ChemInform ◽  
2010 ◽  
Vol 30 (41) ◽  
pp. no-no
Author(s):  
Twana Saleh ◽  
Gerard Rousseau
Keyword(s):  

1983 ◽  
Vol 47 (10) ◽  
pp. 2385-2386
Author(s):  
Kiyonobu Ikezaki ◽  
Michihiko Kuwano ◽  
Takao Kishie ◽  
Kazuko Murakami ◽  
Tomohisa Nagasaki ◽  
...  

2019 ◽  
Vol 481 ◽  
pp. 67-71
Author(s):  
Hidde Elferink ◽  
Kim Geurts ◽  
Stijn Jue ◽  
Somhairle MacCormick ◽  
Gerrit Veeneman ◽  
...  

1984 ◽  
Vol 127 (1) ◽  
pp. 129-135 ◽  
Author(s):  
Makoto Kiso ◽  
Hideharu Ishida ◽  
Akihito Kawaide ◽  
Akira Hasegawa

1996 ◽  
Vol 37 (50) ◽  
pp. 9037-9040 ◽  
Author(s):  
Thomas G. Marron ◽  
Thomas J. Woltering ◽  
Gabriele Weitz-Schmidt ◽  
Chi-Huey Wong

2018 ◽  
Vol 11 (3) ◽  
pp. 70 ◽  
Author(s):  
Alessandra Boschi ◽  
Micòl Pasquali ◽  
Claudio Trapella ◽  
Alessandro Massi ◽  
Petra Martini ◽  
...  

Background: New approaches based on the receptor-targeted molecular interaction have been recently developed with the aim to investigate specific probes for sentinel lymph nodes. In particular, the mannose receptors expressed by lymph node macrophages became an attractive target and different multifunctional mannose derivate ligands for the labeling with 99mTc have been developed. In this study, we report the synthesis of a specific class of dextran-based, macromolecular, multifunctional ligands specially designed for labeling with the highly stable [99mTc≡N]2+ core. Methods: The ligands have been obtained by appending to a macromolecular dextran scaffold pendant arms bearing a chelating moiety for the metallic group and a mannosyl residue for allowing the interaction of the resulting macromolecular 99mTc conjugate with specific receptors on the external membrane of macrophages. Two different chelating systems have been selected, S-methyl dithiocarbazate [H2N‒NH‒C(=S)SCH3=HDTCZ] and a sequence of two cysteine residues, that in combination with a monophosphine coligand, are able to bind the [99mTc≡N]2+ core. Conclusions: High-specific-activity labeling has been obtained by simple mixing and heating of the [99mTc≡N]2+ group with the new mannose-dextran derivatives.


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