PMID- 2856402
OWN - NLM
STAT- MEDLINE
DCOM- 19901205
LR  - 20151119
IS  - 0888-8809 (Print)
IS  - 0888-8809 (Linking)
VI  - 1
IP  - 11
DP  - 1987 Nov
TI  - Dual regulation of protein maturation in viral infected rat HTC hepatoma cells by 
      glucocorticoids and progesterone.
PG  - 823-33
AB  - Dexamethasone, a synthetic glucocorticoid, is required for full posttranslational 
      maturation of mouse mammary tumor virus (MMTV) phosphoproteins and glycoproteins 
      in M1.54 cells, a viral infected rat hepatoma (HTC) cell line. Pulse-chase 
      radiolabeling with [35S]methionine revealed that steroids with known 
      glucocorticoid activity (such as dexamethasone and hydrocortisone) regulated the 
      maturation of both MMTV polyproteins in a manner proportional to their occupancy 
      for glucocorticoid receptors and their biological potency. In contrast, 
      progesterone selectively induced the proteolytic processing of MMTV 
      phosphoproteins but simultaneously antagonized the dexamethasone-regulated 
      maturation of MMTV glycoproteins and all other tested glucocorticoid responses. 
      Exposure to suboptimal concentrations of both progesterone and dexamethasone 
      fully stimulated the processing of MMTV phosphoproteins, suggesting that steroid 
      receptors occupied with combinations of either steroid functionally interact at 
      the putative maturation gene. Moreover, treatment with either actinomycin D, a 
      potent inhibitor of de novo RNA synthesis, or RU38486, a synthetic antagonist of 
      glucocorticoid and progesterone action, prevented both the dexamethasone and 
      progesterone-regulated induction of MMTV phosphoprotein maturation. Sedimentation 
      velocity and saturation binding analysis revealed that the sizes and 
      concentrations of hepatoma cell progesterone and dexamethasone binding activities 
      are similar while specific binding of the active progestin R5020 was not detected 
      in either M1.54 cells or the glucocorticoid receptor deficient HTC cell line 
      MSN6.10.2. Taken together, our results demonstrate that two distinct classes of 
      steroid hormones can uniquely alter the posttranslational maturation of a 
      specific subset of phosphoprotein substrates by a common glucocorticoid 
      receptor-dependent process.
FAU - Winguth, S D
AU  - Winguth SD
AD  - Department of Physiology-Anatomy, University of California, Berkeley 94720.
FAU - Firestone, G L
AU  - Firestone GL
LA  - eng
GR  - CA-09041/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Mol Endocrinol
JT  - Molecular endocrinology (Baltimore, Md.)
JID - 8801431
RN  - 0 (Phosphoproteins)
RN  - 0 (Receptors, Glucocorticoid)
RN  - 0 (Sulfur Radioisotopes)
RN  - 0 (Viral Proteins)
RN  - 320T6RNW1F (Mifepristone)
RN  - 4G7DS2Q64Y (Progesterone)
RN  - 7S5I7G3JQL (Dexamethasone)
SB  - IM
MH  - Animals
MH  - Binding, Competitive/drug effects
MH  - Cell Line, Transformed
MH  - Dexamethasone/metabolism/*pharmacology
MH  - Electrophoresis, Polyacrylamide Gel
MH  - Liver Neoplasms, Experimental/*metabolism
MH  - Mammary Tumor Virus, Mouse
MH  - Mifepristone/pharmacology
MH  - Phosphoproteins/metabolism
MH  - Precipitin Tests
MH  - Progesterone/metabolism/*pharmacology
MH  - Protein Processing, Post-Translational/*drug effects
MH  - Receptors, Glucocorticoid/metabolism
MH  - Sulfur Radioisotopes
MH  - Tumor Cells, Cultured
MH  - Viral Proteins/*metabolism
EDAT- 1987/11/01 00:00
MHDA- 1987/11/01 00:01
CRDT- 1987/11/01 00:00
PHST- 1987/11/01 00:00 [pubmed]
PHST- 1987/11/01 00:01 [medline]
PHST- 1987/11/01 00:00 [entrez]
AID - 10.1210/mend-1-11-823 [doi]
PST - ppublish
SO  - Mol Endocrinol. 1987 Nov;1(11):823-33. doi: 10.1210/mend-1-11-823.