PMID- 26494371
OWN - NLM
STAT- MEDLINE
DCOM- 20161020
LR  - 20181113
IS  - 1573-4986 (Electronic)
IS  - 0282-0080 (Linking)
VI  - 33
IP  - 1
DP  - 2016 Feb
TI  - Changes in glycosylation of human blood plasma chitotriosidase in patients with 
      type 2 diabetes.
PG  - 29-39
AB  - Human blood plasma chitotriosidase (CHIT1) is a glycoprotein with chitinolytic 
      activity with not fully elucidated biological function. Its increased level is 
      observed in type 2 diabetes mellitus (T2DM) and is associated with development of 
      diabetic complications. The CHIT1 glycosylation profile and degree is still 
      poorly studied and never investigated in T2DM. Therefore the aim of the present 
      study was to examine the association between glycosylation profile and degree and 
      diabetes with accompanying nephropathy. In blood plasma of 28 patients with T2DM 
      and 11 healthy subjects the CHIT1 concentration and specific activity were 
      examined. The profile and degree of CHIT1 glycosylation were determined by 
      lectin-ELISA using lectins specific to O-glycans (Jacalin, MPL, VVL) and 
      sialo-specific SNA and MAA. We revealed that both concentration and specific 
      activity of CHIT1 significantly increased in T2DM, especially in nephropathy with 
      elevated albuminuria. The relative reactivities with lectins, except Jacalin, 
      decreased progressively with T2DM occurrence and albuminuria progression. The 
      most significant differences were observed between control vs. albuminuric group 
      (Micro and Macro). It is also possible that the observed differences in 
      immunoblotting pattern in molecular masses of CHIT1 bands between T2DM patients 
      and healthy subjects may be caused by the differences in degree of CHIT1 
      glycosylation. The analysis of CHIT1 glycosylation status and the determination 
      of CHIT1 concentration together with its enzymatic activity in blood plasma might 
      constitute additional valuable diagnosis tools for the evaluation the T2DM 
      patients with accompanying nephropathy. Extension of the lectin panel specific to 
      O-glycans occurs useful for the further research using microarray formats, which 
      are expected to accelerate "lectin-based glycan profiling" of glycoproteins.
FAU - Zurawska-Plaksej, Ewa
AU  - Zurawska-Plaksej E
FAU - Kratz, Ewa Maria
AU  - Kratz EM
FAU - Ferens-Sieczkowska, Miroslawa
AU  - Ferens-Sieczkowska M
FAU - Knapik-Kordecka, Maria
AU  - Knapik-Kordecka M
FAU - Piwowar, Agnieszka
AU  - Piwowar A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Glycoconj J
JT  - Glycoconjugate journal
JID - 8603310
RN  - 0 (Biomarkers)
RN  - 0 (Lectins)
RN  - EC 3.2.1.- (Hexosaminidases)
RN  - EC 3.2.1.- (chitotriosidase)
SB  - IM
MH  - Albuminuria/*blood/enzymology
MH  - Biomarkers/blood
MH  - Case-Control Studies
MH  - Diabetes Mellitus, Type 2/*blood/enzymology
MH  - Diabetic Nephropathies/*blood/enzymology
MH  - Glycosylation
MH  - Hexosaminidases/*blood/metabolism
MH  - Humans
MH  - Lectins/metabolism
MH  - Protein Binding
MH  - *Protein Processing, Post-Translational
EDAT- 2015/10/24 06:00
MHDA- 2016/10/21 06:00
CRDT- 2015/10/24 06:00
PHST- 2015/07/26 00:00 [received]
PHST- 2015/10/14 00:00 [accepted]
PHST- 2015/10/13 00:00 [revised]
PHST- 2015/10/24 06:00 [entrez]
PHST- 2015/10/24 06:00 [pubmed]
PHST- 2016/10/21 06:00 [medline]
AID - 10.1007/s10719-015-9629-z [pii]
AID - 10.1007/s10719-015-9629-z [doi]
PST - ppublish
SO  - Glycoconj J. 2016 Feb;33(1):29-39. doi: 10.1007/s10719-015-9629-z.