PMID- 34165207
OWN - NLM
STAT- MEDLINE
DCOM- 20211018
LR  - 20211018
IS  - 1097-0134 (Electronic)
IS  - 0887-3585 (Linking)
VI  - 89
IP  - 11
DP  - 2021 Nov
TI  - Characterization of glucose-binding proteins isolated from health volunteers and 
      human type 2 diabetes mellitus patients.
PG  - 1413-1424
LID - 10.1002/prot.26163 [doi]
AB  - Glucose is one of the most important monosaccharides. Although hyperglycemia in 
      type 2 diabetes mellitus (T2DM) lead to a series of changes; however, little is 
      known about the alterations of serum proteins in T2DM, especially those proteins 
      with glucose affinity. In this study, the glucose-binding proteins (GlcBPs) of 
      serum were isolated from 30 health volunteer (HV) and 30 T2DM patients by 
      glucose-magnetic particle conjugates (GMPC) and identified by mass spectrum 
      analysis. Gene ontology (GO) enrichment analysis and Kyoto Encyclopedia of Genes 
      and Genomes (KEGG) indicated the main gene annotations and pathways of this 
      GlcBPs, while Motif-X webtool provided the potential glucose-binding domains. 
      Further docking analysis and glycan microarray were used to understand the 
      interaction between the glucose and glucose-binding domains. A total of 149 and 
      119 GlcBPs were identified from HV and T2DM cases. Four hundred and sixty-eight 
      GO annotations in 165 identified GlcBPs were available, while the majority 
      involved in cellular processes and binding function. A short peptide, 
      EGDEEITCLNGFWLE, which was derived from the Motif-X analysis, presented a 
      high-binding ability to the glucose from both docking analysis and glycan 
      analysis. GMPC provides a powerful tool for GlcBPs isolation and indicates the 
      alteration of GlcBPs in T2DM.
CI  - (c) 2021 Wiley Periodicals LLC.
FAU - Chen, Wentian
AU  - Chen W
AUID- ORCID: 0000-0003-0187-5223
AD  - Laboratory for Functional Glycomics, College of Life Sciences, Northwest 
      University, Xi'an, China.
FAU - Zhong, Yaogang
AU  - Zhong Y
AD  - Laboratory for Functional Glycomics, College of Life Sciences, Northwest 
      University, Xi'an, China.
FAU - Shu, Jian
AU  - Shu J
AD  - Laboratory for Functional Glycomics, College of Life Sciences, Northwest 
      University, Xi'an, China.
FAU - Yu, Hanjie
AU  - Yu H
AD  - Laboratory for Functional Glycomics, College of Life Sciences, Northwest 
      University, Xi'an, China.
FAU - Chen, Zhuo
AU  - Chen Z
AD  - Laboratory for Functional Glycomics, College of Life Sciences, Northwest 
      University, Xi'an, China.
FAU - Ren, Xiameng
AU  - Ren X
AD  - Laboratory for Functional Glycomics, College of Life Sciences, Northwest 
      University, Xi'an, China.
FAU - Hui, Ziye
AU  - Hui Z
AD  - Laboratory for Functional Glycomics, College of Life Sciences, Northwest 
      University, Xi'an, China.
FAU - Li, Zheng
AU  - Li Z
AUID- ORCID: 0000-0002-1839-3450
AD  - Laboratory for Functional Glycomics, College of Life Sciences, Northwest 
      University, Xi'an, China.
LA  - eng
GR  - 31500130/National Natural Science Foundation of China/
GR  - NWU002/the emergency guidance fund for prevention of novel coronavirus pneumonia 
      from northwest university/
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20210720
PL  - United States
TA  - Proteins
JT  - Proteins
JID - 8700181
RN  - 0 (Blood Glucose)
RN  - 0 (Blood Proteins)
RN  - 0 (Peptide Fragments)
RN  - 0 (Polysaccharides)
SB  - IM
MH  - Binding Sites
MH  - Blood Chemical Analysis/methods
MH  - Blood Glucose/*metabolism
MH  - Blood Proteins/chemistry/*isolation & purification/*metabolism
MH  - Diabetes Mellitus, Type 2/*blood
MH  - Female
MH  - Healthy Volunteers
MH  - Humans
MH  - Male
MH  - Middle Aged
MH  - Molecular Docking Simulation
MH  - Molecular Dynamics Simulation
MH  - Molecular Sequence Annotation
MH  - Peptide Fragments/blood/chemistry/metabolism
MH  - Polysaccharides/analysis
MH  - Protein Interaction Maps
OTO - NOTNLM
OT  - LC-MS/MS
OT  - T2DM
OT  - glucose
OT  - glycan-binding proteins
OT  - molecular docking
EDAT- 2021/06/25 06:00
MHDA- 2021/10/21 06:00
CRDT- 2021/06/24 09:37
PHST- 2021/05/09 00:00 [revised]
PHST- 2021/01/05 00:00 [received]
PHST- 2021/06/15 00:00 [accepted]
PHST- 2021/06/25 06:00 [pubmed]
PHST- 2021/10/21 06:00 [medline]
PHST- 2021/06/24 09:37 [entrez]
AID - 10.1002/prot.26163 [doi]
PST - ppublish
SO  - Proteins. 2021 Nov;89(11):1413-1424. doi: 10.1002/prot.26163. Epub 2021 Jul 20.