JBC Anatrace, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dunn, R.
Right arrow Articles by Marks, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dunn, R.
Right arrow Articles by Marks, A.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 262, Issue 8, 3562-3566, 03, 1987

Reduction in S100 protein beta subunit mRNA in C6 rat glioma cells following treatment with anti-microtubular drugs

R Dunn, C Landry, D O'Hanlon, J Dunn, R Allore, I Brown and A Marks

S100 protein is a calcium-binding protein found in vertebrate nervous tissue. Synthesis of S100 protein in the rat glioma cell line, C6, is inhibited by the addition of anti-microtubular drugs. We have cloned a cDNA for the beta subunit of S100 protein from rat brain in a lambda gt 11 expression vector and used this cDNA to measure the amounts of S100 beta subunit mRNA in C6 cells after treatment with anti-microtubular drugs. Levels of alpha-tubulin and beta-actin mRNAs were also measured. All measurements were performed using RNA-RNA hybridization techniques at high stringency with rat mRNA-specific probes. After 24 h of treatment, the S100 beta subunit mRNA was reduced to levels of 25% by colchicine and 32% by vinblastine when compared to untreated controls. In contrast, the levels of tubulin and actin mRNAs were only slightly changed by these treatments. These studies demonstrate that disruption of the microtubular cytoskeleton causes a specific reduction in the level of S100 protein mRNA in C6 cells.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J. N. Tsoporis, A. Marks, H. J. Kahn, J. W. Butany, P. P. Liu, D. O'Hanlon, and T. G. Parker
S100beta Inhibits alpha 1-Adrenergic Induction of the Hypertrophic Phenotype in Cardiac Myocytes
J. Biol. Chem., December 12, 1997; 272(50): 31915 - 31921.
[Abstract] [Full Text] [PDF]


Home page
EndocrinologyHome page
D. B. Zimmer, J. Chessher, G. L. Wilson, and W. E. Zimmer
S100A1 and S100B Expression and Target Proteins in Type I Diabetes
Endocrinology, December 1, 1997; 138(12): 5176 - 5183.
[Abstract] [Full Text] [PDF]


Home page
ScienceHome page
R Allore, D O'Hanlon, R Price, K Neilson, H. Willard, D. Cox, A Marks, and R. Dunn
Gene encoding the beta subunit of S100 protein is on chromosome 21: implications for Down syndrome
Science, March 11, 1988; 239(4845): 1311 - 1313.
[Abstract] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1987 by the American Society for Biochemistry and Molecular Biology.