Document Detail


Expression of the major protein kinase C substrate, the acidic 80-kilodalton myristoylated alanine-rich C kinase substrate, increases sharply when Swiss 3T3 cells move out of cycle and enter G0.
MedLine Citation:
PMID:  8464911     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The expression of the major protein kinase C (PKC) substrate, originally called "80K" for acidic SDS/PAGE-observed 80-kDa PKC substrate and now called "MARCKS" for myristoylated alanine-rich C kinase substrate, in Swiss 3T3 fibroblasts changes strikingly (15- to 22-fold) during transitions of cell growth. Quiescent cells in G0 express high levels of MARCKS mRNA and protein. However, plating these cells in fresh medium at low density to stimulate multiple rounds of cell division caused a striking down-regulation of MARCKS expression. The mRNA level declined to a minimum of 4.5% compared with quiescent control cells 6 hr after plating, and protein levels declined during the same period to 6.5% of the control value. This rapid down-regulation was independent of PKC activation and length of exposure to trypsin (1-10 min) but required plating in medium containing fresh serum. MARCKS mRNA and protein levels remained down-regulated for 3 days, during which time the cells were actively progressing through the cell cycle as judged by fluorescence-activated cell sorting analysis. However, on reaching quiescence, the expression of MARCKS mRNA and protein increased markedly. Furthermore, the rate of recovery of MARCKS mRNA and protein levels was shown to be dependent on the supply of serum-derived growth factors in the medium. Addition of hydroxyurea to arrest the cells in S phase or at the G1/S boundary rather than G0 completely prevented the recovery of MARCKS protein. The down-regulation of MARCKS following plating and its serum-dependent recovery was also demonstrated in tertiary cultures of mouse embryo fibroblasts. The results suggest that MARCKS may play a role in the regulation of entry and exit of cells from G0.
Authors:
T Herget; S F Brooks; S Broad; E Rozengurt
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  90     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  1993 Apr 
Date Detail:
Created Date:  1993-05-04     Completed Date:  1993-05-04     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2945-9     Citation Subset:  IM    
Affiliation:
Imperial Cancer Research Fund, London, United Kingdom.
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MeSH Terms
Descriptor/Qualifier:
3T3 Cells
Animals
Blotting, Northern
Blotting, Western
Cell Cycle / physiology*
Cell Division / physiology
Flow Cytometry
G0 Phase / physiology
G1 Phase / physiology
Gene Expression / drug effects
Growth Substances / pharmacology
Intracellular Signaling Peptides and Proteins*
Kinetics
Membrane Proteins*
Mice
Protein Biosynthesis*
Protein Kinase C / metabolism*
Proteins / genetics
RNA, Messenger / genetics,  metabolism
Restriction Mapping
S Phase / physiology
Time Factors
Chemical
Reg. No./Substance:
0/Growth Substances; 0/Intracellular Signaling Peptides and Proteins; 0/Membrane Proteins; 0/Proteins; 0/RNA, Messenger; 125267-21-2/myristoylated alanine-rich C kinase substrate; EC 2.7.11.13/Protein Kinase C
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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