TY - JOUR
T1 - In vivo imaging of fluorescent albumin modified with pyruvylated-human-type complex oligosaccharide reveals sialylation-like biodistribution and kinetics
AU - Fukuhara, Ryoichiro
AU - Ogura, Akihiro
AU - Yoshinaga, Sho
AU - Fukunaga, Takamasa
AU - Kinoshita, Takashi
AU - Sumiyoshi, Wataru
AU - Higuchi, Yujiro
AU - Tanaka, Katsunori
AU - Takegawa, Kaoru
N1 - Funding Information:
This work was partially supported by JSPS KAKENHI grant numbers JP17H03966 and JP21K19090, the Institute for Fermentation Osaka (IFO), Japan (KTakegawa). We would like to thank Glytech Inc. for supplying various N-glycans. This work was financially supported by the AMED Grant JP15KM0908001, a research grant from the Astellas Foundation, Mizutani Foundation for Glycoscience, and JSPS KAKENHI Grant Numbers, JP21H02065 and JP21K19042 (to K.Tanaka).
Publisher Copyright:
© 2022 Elsevier Ltd
PY - 2022/9/15
Y1 - 2022/9/15
N2 - Both pyruvylation and sialylation onto the terminus of oligosaccharides of N-glycoproteins seem to be structurally and functionally similar with a property of conferring negative charge. However, detailed molecular characteristics of pyruvylation and sialylation in vivo were elusive. Here, to investigate an effect of terminal pyruvylation to N-glycan on in vivo biodistribution and kinetics, we prepared human serum albumin (HSA) modified with pyruvylated N-glycan (PvG), conjugated with HiLyte Fluor 750 (FL750-PvGHSA). In vivo imaging by using FL750-PvGHSA revealed that terminally pyruvylated N-glycoalbumin was excreted like sialylated N-glycoalbumin, suggesting that pyruvylation mimics sialylation in in vivo biodistribution and kinetics of N-glycoproteins. Terminal pyruvylation onto N-glycans can be a potential tool for a novel glycoengineering strategy.
AB - Both pyruvylation and sialylation onto the terminus of oligosaccharides of N-glycoproteins seem to be structurally and functionally similar with a property of conferring negative charge. However, detailed molecular characteristics of pyruvylation and sialylation in vivo were elusive. Here, to investigate an effect of terminal pyruvylation to N-glycan on in vivo biodistribution and kinetics, we prepared human serum albumin (HSA) modified with pyruvylated N-glycan (PvG), conjugated with HiLyte Fluor 750 (FL750-PvGHSA). In vivo imaging by using FL750-PvGHSA revealed that terminally pyruvylated N-glycoalbumin was excreted like sialylated N-glycoalbumin, suggesting that pyruvylation mimics sialylation in in vivo biodistribution and kinetics of N-glycoproteins. Terminal pyruvylation onto N-glycans can be a potential tool for a novel glycoengineering strategy.
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U2 - 10.1016/j.bmc.2022.116943
DO - 10.1016/j.bmc.2022.116943
M3 - Article
C2 - 35905685
AN - SCOPUS:85134983283
SN - 0968-0896
VL - 70
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
M1 - 116943
ER -