PMID- 10580430
OWN - NLM
STAT- MEDLINE
DCOM- 19991213
LR  - 20190515
IS  - 0012-1797 (Print)
IS  - 0012-1797 (Linking)
VI  - 48
IP  - 12
DP  - 1999 Dec
TI  - Localization of the O-linked N-acetylglucosamine transferase in rat pancreas.
PG  - 2407-13
AB  - O-linked N-acetylglucosamine transferase (OGT) catalyzes the attachment
      ofN-acetylglucosamine (GlcNAc) monosaccharides to the hydroxyl group of serine or
      threonine residues of intracellular proteins and may play an important role in
      the hexosamine pathway. Glucose-induced insulin resistance is mediated by
      increased activity of the hexosamine pathway. In the present study, we examined
      the localization of OGT mRNA and OGT protein in the rat pancreas. The sites of
      OGT mRNA expression were determined by in situ hybridization histochemistry with 
      a digoxigenin (DIG)-labeled antisense cRNA probe. Intense hybridization signals
      were present in the exocrine acinar cells, while weaker ones were detected in the
      islets of Langerhans. This distribution was confirmed using additional antisense 
      cRNA or oligo-cDNA probes complementary to different regions of OGT mRNA. In
      addition, immunofluorescence staining with antibody raised against OGT stained
      both the exocrine acinar cells and endocrine islet cells. In the acinar cell
      nucleus, the zymogen granule region and contour of the cell were intensely
      stained. In the islets of Langerhans, especially in the alpha-cells, intense
      staining with anti-OGT antibody was observed. These staining patterns were almost
      identical to those seen when staining for the O-linked GlcNAc (O-GlcNAc)
      modification. Immuno-electron microscopy showed that OGT is localized to the
      euchromatin of the nucleus and around the secretory granules of exocrine acinar
      cells and endocrine islet cells. These results suggest that OGT is involved in
      the regulation of transcription and of granular secretion. Thus, one or more
      O-GlcNAcylated proteins may be important components of the glucose-sensing
      mechanism in the pancreas.
FAU - Akimoto, Y
AU  - Akimoto Y
AD  - Department of Biochemistry and Molecular Genetics Schools of Medicine/Dentistry, 
      University of Alabama at Birmingham Station, USA.
FAU - Kreppel, L K
AU  - Kreppel LK
FAU - Hirano, H
AU  - Hirano H
FAU - Hart, G W
AU  - Hart GW
LA  - eng
GR  - HD13563/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Diabetes
JT  - Diabetes
JID - 0372763
RN  - 0 (Insulin)
RN  - 0 (RNA, Messenger)
RN  - 9007-92-5 (Glucagon)
RN  - EC 2.4.1.- (N-Acetylglucosaminyltransferases)
RN  - EC 2.4.1.- (UDP-N-acetylglucosamine-peptide beta-N-acetylglucosaminyltransferase)
SB  - IM
MH  - Animals
MH  - Glucagon/analysis
MH  - Immunohistochemistry
MH  - In Situ Hybridization
MH  - Insulin/analysis
MH  - Islets of Langerhans/cytology/enzymology/ultrastructure
MH  - Liver/cytology/*enzymology/ultrastructure
MH  - Male
MH  - Microscopy, Immunoelectron
MH  - N-Acetylglucosaminyltransferases/*analysis/*genetics
MH  - Pancreas/cytology/*enzymology/ultrastructure
MH  - RNA, Messenger/analysis/genetics
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Transcription, Genetic
EDAT- 1999/12/02 00:00
MHDA- 1999/12/02 00:01
CRDT- 1999/12/02 00:00
PHST- 1999/12/02 00:00 [pubmed]
PHST- 1999/12/02 00:01 [medline]
PHST- 1999/12/02 00:00 [entrez]
AID - 10.2337/diabetes.48.12.2407 [doi]
PST - ppublish
SO  - Diabetes. 1999 Dec;48(12):2407-13. doi: 10.2337/diabetes.48.12.2407.