PMID- 8431454
OWN - NLM
STAT- MEDLINE
DCOM- 19930317
LR  - 20190610
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1145
IP  - 2
DP  - 1993 Feb 9
TI  - Modulation of the synthesis and glycosylation of the glucose transporter protein 
      by transforming growth factor-beta 1 in Swiss 3T3 fibroblasts.
PG  - 227-34
AB  - Transforming growth factor-beta 1 (TGF-beta 1) stimulated growth and glucose 
      uptake in Swiss mouse fibroblasts. DNA synthesis was increased 2-3-fold after 48 
      h incubation of growing 3T3 cells with TGF-beta 1 in calf serum-containing 
      medium. Glucose transport activity in the cells was increased within 3 h after 
      addition of TGF-beta 1 and this stimulation continued during incubation for 48 h. 
      TGF-beta 1 also increased the levels of a brain type-glucose transporter (GLUT1) 
      mRNA and the GLUT1 protein (55 kDa) in the membranes, consistent with the 
      increase in glucose uptake. Furthermore, a longer exposure of TGF-beta 1 for 
      24-48 h induced a marked increase in the 65 kDa GLUT1 in 3T3 cell membranes. 
      Other growth factors such as epidermal growth factor, fibroblast growth factor, 
      transforming growth factor-alpha, and insulin did not elevate glucose uptake and 
      the levels of 55 and 65 kDa GLUT1 proteins. Adding tunicamycin or 
      deoxymannojirimycin to the TGF-beta 1-treated and untreated cells caused these 55 
      and 65 kDa glucose transporters to migrate as one band at 40-43 kDa. In addition, 
      treating membrane proteins with glycopeptidase F, which removes N-linked 
      oligosaccharides, also generated a glucose transporter of 40 kDa, suggesting that 
      the 55 and 65 kDa GLUT1 proteins have a similar or identical core polypeptide but 
      with different N-linked oligosaccharides. These results indicate that TGF-beta 1 
      modulates the synthesis of GLUT1 protein as well as its glycosylation in Swiss 
      3T3 cells, and that these changes may contribute to the control of cell 
      proliferation by TGF-beta 1.
FAU - Masumi, A
AU  - Masumi A
AD  - Department of Chemistry, National Institute of Health, Tokyo, Japan.
FAU - Akamatsu, Y
AU  - Akamatsu Y
FAU - Kitagawa, T
AU  - Kitagawa T
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (Glucose Transporter Type 1)
RN  - 0 (Monosaccharide Transport Proteins)
RN  - 0 (RNA, Messenger)
RN  - 0 (Slc2a1 protein, mouse)
RN  - 0 (Transforming Growth Factor beta)
RN  - 11089-65-9 (Tunicamycin)
RN  - 9G2MP84A8W (Deoxyglucose)
SB  - IM
MH  - 3T3 Cells/metabolism
MH  - Animals
MH  - Cell Division/drug effects
MH  - DNA Replication
MH  - Deoxyglucose/metabolism
MH  - Gene Expression Regulation/drug effects
MH  - Glucose Transporter Type 1
MH  - Glycosylation/drug effects
MH  - Mice
MH  - Monosaccharide Transport Proteins/*biosynthesis
MH  - RNA, Messenger/metabolism
MH  - Stimulation, Chemical
MH  - Transforming Growth Factor beta/*pharmacology
MH  - Tunicamycin/pharmacology
EDAT- 1993/02/09 00:00
MHDA- 1993/02/09 00:01
CRDT- 1993/02/09 00:00
PHST- 1993/02/09 00:00 [pubmed]
PHST- 1993/02/09 00:01 [medline]
PHST- 1993/02/09 00:00 [entrez]
AID - 0005-2736(93)90293-9 [pii]
AID - 10.1016/0005-2736(93)90293-9 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 1993 Feb 9;1145(2):227-34. doi: 
      10.1016/0005-2736(93)90293-9.