Abstract
Post-translational modifications (PTMs) of proteins play important roles in the physiology of eukaryotes. In the PTMs, non-reversible glycosylations are classified as N-glycosylations and O-glycosylations, and are catalyzed by various glycosidases and glycosyltransferases. However, β-glycosidases are not known to play a role in N- and O-glycan processing, although both glycans provide partial structures as substrates for β-galactosidase and β-N-acetylglucosaminidase in the Golgi apparatus of human cells. We explored human Golgi β-galactosidase using fluorescent substrates based on a quinone methide cleavage (QMC) substrate design platform that was previously developed to image exo-type glycosidases in living cells. As a result, we discovered a novel Golgi β-galactosidase in human cells. It is possible to predict a novel and important function in glycan processing of this β-galactosidase, because various β-galactosyl linkages in N- and O-glycans exist in Golgi apparatus. In addition, these results show that the QMC platform is excellent for imaging exo-type glycosidases.
| Original language | English |
|---|---|
| Pages (from-to) | 1369-1375 |
| Number of pages | 7 |
| Journal | Bioorganic and Medicinal Chemistry |
| Volume | 24 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 2016 Mar 15 |
| Externally published | Yes |
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Keywords
- Fluorescent imaging
- Glycan processing
- Golgi apparatus
- Post-translational modifications
- Quinone methide cleavage
- β-Galactosidase
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry
Cite this
Discovery of human Golgi β-galactosidase with no identified glycosidase using a QMC substrate design platform for exo-glycosidase. / Miura, Kazuki; Hakamata, Wataru; Tanaka, Ayako; Hirano, Takako; Nishio, Toshiyuki.
In: Bioorganic and Medicinal Chemistry, Vol. 24, No. 6, 15.03.2016, p. 1369-1375.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Discovery of human Golgi β-galactosidase with no identified glycosidase using a QMC substrate design platform for exo-glycosidase
AU - Miura, Kazuki
AU - Hakamata, Wataru
AU - Tanaka, Ayako
AU - Hirano, Takako
AU - Nishio, Toshiyuki
PY - 2016/3/15
Y1 - 2016/3/15
N2 - Post-translational modifications (PTMs) of proteins play important roles in the physiology of eukaryotes. In the PTMs, non-reversible glycosylations are classified as N-glycosylations and O-glycosylations, and are catalyzed by various glycosidases and glycosyltransferases. However, β-glycosidases are not known to play a role in N- and O-glycan processing, although both glycans provide partial structures as substrates for β-galactosidase and β-N-acetylglucosaminidase in the Golgi apparatus of human cells. We explored human Golgi β-galactosidase using fluorescent substrates based on a quinone methide cleavage (QMC) substrate design platform that was previously developed to image exo-type glycosidases in living cells. As a result, we discovered a novel Golgi β-galactosidase in human cells. It is possible to predict a novel and important function in glycan processing of this β-galactosidase, because various β-galactosyl linkages in N- and O-glycans exist in Golgi apparatus. In addition, these results show that the QMC platform is excellent for imaging exo-type glycosidases.
AB - Post-translational modifications (PTMs) of proteins play important roles in the physiology of eukaryotes. In the PTMs, non-reversible glycosylations are classified as N-glycosylations and O-glycosylations, and are catalyzed by various glycosidases and glycosyltransferases. However, β-glycosidases are not known to play a role in N- and O-glycan processing, although both glycans provide partial structures as substrates for β-galactosidase and β-N-acetylglucosaminidase in the Golgi apparatus of human cells. We explored human Golgi β-galactosidase using fluorescent substrates based on a quinone methide cleavage (QMC) substrate design platform that was previously developed to image exo-type glycosidases in living cells. As a result, we discovered a novel Golgi β-galactosidase in human cells. It is possible to predict a novel and important function in glycan processing of this β-galactosidase, because various β-galactosyl linkages in N- and O-glycans exist in Golgi apparatus. In addition, these results show that the QMC platform is excellent for imaging exo-type glycosidases.
KW - Fluorescent imaging
KW - Glycan processing
KW - Golgi apparatus
KW - Post-translational modifications
KW - Quinone methide cleavage
KW - β-Galactosidase
UR - http://www.scopus.com/inward/record.url?scp=84958999273&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84958999273&partnerID=8YFLogxK
U2 - 10.1016/j.bmc.2016.02.010
DO - 10.1016/j.bmc.2016.02.010
M3 - Article
C2 - 26875935
AN - SCOPUS:84958999273
VL - 24
SP - 1369
EP - 1375
JO - Bioorganic and Medicinal Chemistry
JF - Bioorganic and Medicinal Chemistry
SN - 0968-0896
IS - 6
ER -