PMID- 10353622
OWN - NLM
STAT- MEDLINE
DCOM- 19990610
LR  - 20190701
IS  - 0024-3205 (Print)
IS  - 0024-3205 (Linking)
VI  - 64
IP  - 17
DP  - 1999
TI  - In vitro and in vivo alterations of enzymatic glycosylation in diabetes.
PG  - 1571-83
AB  - Carbohydrate composition changes of glycoconjugates constituting the glycocalix
      of microvascular cells could be involved in the alterations of cell-cell
      interactions observed in diabetic retinopathy. In this field, we have recently
      reported that advanced glycation end products (AGEs) modify galactose, fucose and
      sialic acid contents of specific cellular glycoproteins. To better understand the
      mechanisms involved in glycoprotein modifications in diabetes, we now investigate
      whether glucose and AGEs could affect the activities of enzymes involved in
      galactose, fucose and sialic acid metabolism : glycosyltransferases (synthesis)
      and glycosidases (catabolism). For this, bovine retinal endothelial cells (BREC) 
      and pericytes (BRP) were cultured in the presence of high glucose concentration
      or AGEs, and cell glycosidase and glycosyltransferase activities were measured.
      The same enzymatic activities were studied in the whole retina from
      streptozotocin-treated rats. The results show that high glucose concentration did
      not affect glycosidases and glycosyltransferases neither in BRP nor in BREC
      except for galactosyltransferase activities in BREC. Concerning BRP, only
      galactosyltransferase activities were altered by AGEs. In contrast, in BREC, AGEs
      increased beta-D galactosidase, alpha-L fucosidase and neuraminidase activities
      (+37%, +56%, 36% respectively) whereas galactosyltransferase, fucosyltransferase 
      and sialyltransferase activities were decreased (-11%, -24% and -23%
      respectively). In the retina from diabetic rats, beta-D galactosidase, alpha-L
      fucosidase and neuraminidase activities increased (+70%, +57%, +78% respectively)
      whereas fucosyl and sialyltransferase decreased (-7% and -15% respectively). The 
      possible consequence of these enzymatic activity changes could be a defect in the
      carbohydrate content of some glycoproteins that might participate in the
      endothelial cell dysfunctions in diabetic microangiopathy.
FAU - Rellier, N
AU  - Rellier N
AD  - Diabetic Microangiopathy Research Unit, LIPHA-INSERM U352, INSA-Lyon,
      Villeurbanne, France.
FAU - Ruggiero-Lopez, D
AU  - Ruggiero-Lopez D
FAU - Lecomte, M
AU  - Lecomte M
FAU - Lagarde, M
AU  - Lagarde M
FAU - Wiernsperger, N
AU  - Wiernsperger N
LA  - eng
PT  - Journal Article
PL  - Netherlands
TA  - Life Sci
JT  - Life sciences
JID - 0375521
RN  - 0 (Glycation End Products, Advanced)
RN  - 5W494URQ81 (Streptozocin)
RN  - EC 2.4.- (Glycosyltransferases)
RN  - EC 3.2.1.- (Glycoside Hydrolases)
SB  - IM
MH  - Animals
MH  - Cattle
MH  - Cells, Cultured
MH  - Diabetes Mellitus, Experimental/*metabolism
MH  - Glycation End Products, Advanced/pharmacology
MH  - Glycoside Hydrolases/*metabolism
MH  - Glycosylation
MH  - Glycosyltransferases/*metabolism
MH  - Male
MH  - Rats
MH  - Rats, Wistar
MH  - Retina/enzymology
MH  - Streptozocin
EDAT- 1999/06/03 00:00
MHDA- 1999/06/03 00:01
CRDT- 1999/06/03 00:00
PHST- 1999/06/03 00:00 [pubmed]
PHST- 1999/06/03 00:01 [medline]
PHST- 1999/06/03 00:00 [entrez]
AID - S0024320599000946 [pii]
AID - 10.1016/s0024-3205(99)00094-6 [doi]
PST - ppublish
SO  - Life Sci. 1999;64(17):1571-83. doi: 10.1016/s0024-3205(99)00094-6.