PMID- 10369669
OWN - NLM
STAT- MEDLINE
DCOM- 19990819
LR  - 20181201
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 12
DP  - 1999 Jun 15
TI  - Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory
      pathway: identification of a nucleoside diphosphatase in the endoplasmic
      reticulum.
PG  - 3282-92
AB  - UDP is generated in the lumen of the endoplasmic reticulum (ER) as a product of
      the UDP-glucose-dependent glycoprotein reglucosylation in the
      calnexin/calreticulin cycle. We describe here the identification, purification
      and characterization of an ER enzyme that hydrolyzes UDP to UMP. This nucleoside 
      diphosphatase is a ubiquitously expressed, soluble 45 kDa glycoprotein devoid of 
      transmembrane domains and KDEL-related ER localization sequences. It requires
      divalent cations for activity and hydrolyzes UDP, GDP and IDP but not any other
      nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. By
      eliminating UDP, which is an inhibitory product of the UDP-Glc:glycoprotein
      glucosyltransferase, it is likely to promote reglucosylation reactions involved
      in glycoprotein folding and quality control in the ER.
FAU - Trombetta, E S
AU  - Trombetta ES
AD  - Department of Cell Biology, Yale Medical School, PO Box 208002, New Haven, CT
      06520-8002, USA. sergio.trombetta@yale.edu
FAU - Helenius, A
AU  - Helenius A
LA  - eng
SI  - GENBANK/AJ238636
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Cations, Divalent)
RN  - 0 (Glycoproteins)
RN  - 0 (Nucleotides)
RN  - EC 2.4.- (Glycosyltransferases)
RN  - EC 3.6.- (Acid Anhydride Hydrolases)
RN  - EC 3.6.1.6 (nucleoside-diphosphatase)
SB  - IM
MH  - Acid Anhydride Hydrolases/chemistry/genetics/isolation & purification/*metabolism
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - *Carbohydrate Metabolism
MH  - Cations, Divalent/pharmacology
MH  - Cattle
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Endoplasmic Reticulum/*enzymology/metabolism
MH  - Glycoproteins/*metabolism
MH  - Glycosylation
MH  - Glycosyltransferases/antagonists & inhibitors/metabolism
MH  - Golgi Apparatus/enzymology
MH  - Humans
MH  - Hydrolysis/drug effects
MH  - Liver/cytology/enzymology/metabolism
MH  - Mice
MH  - Molecular Sequence Data
MH  - Nucleotides/*metabolism/pharmacology
MH  - Substrate Specificity
PMC - PMC1171409
EDAT- 1999/06/16 00:00
MHDA- 1999/06/16 00:01
CRDT- 1999/06/16 00:00
PHST- 1999/06/16 00:00 [pubmed]
PHST- 1999/06/16 00:01 [medline]
PHST- 1999/06/16 00:00 [entrez]
AID - 10.1093/emboj/18.12.3282 [doi]
PST - ppublish
SO  - EMBO J. 1999 Jun 15;18(12):3282-92. doi: 10.1093/emboj/18.12.3282.