PMID- 8497272
OWN - NLM
STAT- MEDLINE
DCOM- 19930623
LR  - 20210526
IS  - 0270-7306 (Print)
IS  - 1098-5549 (Electronic)
IS  - 0270-7306 (Linking)
VI  - 13
IP  - 6
DP  - 1993 Jun
TI  - A GC-rich domain with bifunctional effects on mRNA and protein levels: 
      implications for control of transforming growth factor beta 1 expression.
PG  - 3588-97
AB  - Chimeric plasmids containing selected reporter coding domains and portions of the 
      transforming growth factor beta 1 (TGF-beta 1) 3' untranslated region (UTR) were 
      prepared and used to identify potential mechanisms involved in regulating the 
      biosynthesis of TGF-beta 1. Transient transfections with core and chimeric 
      constructs containing the chloramphenicol acetyltransferase (CAT) reporter showed 
      that steady-state CAT mRNA levels were decreased two- to threefold in response to 
      the TGF-beta 1 3' UTR. Interestingly, CAT activity was somewhat increased in the 
      same transfectants. Thus, production of CAT protein per unit of mRNA was 
      stimulated by the TGF-beta 1 3' UTR (approximately fourfold in three cell lines 
      of distinct lineage). The translation-stimulatory effect of the TGF-beta 1 3' UTR 
      suggested by these studies in vivo was confirmed in vitro by cell-free 
      translation of core and chimeric transcripts containing the growth hormone coding 
      domain. These studies showed that production of growth hormone was stimulated 
      threefold by the TGF-beta 1 3' UTR. A deletion analysis in vivo indicated that 
      the GC-rich domain in the TGF-beta 1 3' UTR was responsible for both the decrease 
      in mRNA levels and stimulation of CAT activity-mRNA. We conclude that this 
      GC-rich domain can have a bifunctional effect on overall protein expression. 
      Moreover, the notable absence of this GC-rich domain in TGF-beta 2, TGF-beta 3, 
      TGF-beta 4, and TGF-beta 5 indicates that expression of distinct TGF-beta family 
      members can be differentially controlled in cells.
FAU - Scotto, L
AU  - Scotto L
AD  - Department of Biochemistry and Molecular Biophysics, College of Physicians and 
      Surgeons, Columbia University, New York, New York 10032.
FAU - Assoian, R K
AU  - Assoian RK
LA  - eng
GR  - HL38884/HL/NHLBI 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  - Mol Cell Biol
JT  - Molecular and cellular biology
JID - 8109087
RN  - 0 (RNA, Messenger)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Transforming Growth Factor beta)
RN  - 5Z93L87A1R (Guanine)
RN  - 8J337D1HZY (Cytosine)
RN  - EC 2.3.1.28 (Chloramphenicol O-Acetyltransferase)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Chloramphenicol O-Acetyltransferase/genetics/metabolism
MH  - Clone Cells
MH  - *Cytosine
MH  - *Guanine
MH  - Humans
MH  - Molecular Sequence Data
MH  - Oocytes/metabolism
MH  - Plasmids
MH  - Protein Biosynthesis
MH  - RNA, Messenger/genetics/*metabolism
MH  - Rabbits
MH  - Recombinant Fusion Proteins/biosynthesis
MH  - Restriction Mapping
MH  - Reticulocytes/metabolism
MH  - Transcription, Genetic
MH  - Transfection
MH  - Transforming Growth Factor beta/*biosynthesis/*genetics
MH  - Tumor Cells, Cultured
PMC - PMC359828
EDAT- 1993/06/01 00:00
MHDA- 1993/06/01 00:01
PMCR- 1993/06/01
CRDT- 1993/06/01 00:00
PHST- 1993/06/01 00:00 [pubmed]
PHST- 1993/06/01 00:01 [medline]
PHST- 1993/06/01 00:00 [entrez]
PHST- 1993/06/01 00:00 [pmc-release]
AID - 10.1128/mcb.13.6.3588-3597.1993 [doi]
PST - ppublish
SO  - Mol Cell Biol. 1993 Jun;13(6):3588-97. doi: 10.1128/mcb.13.6.3588-3597.1993.