JBC Avanti Polar Lipids

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


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Kobayashi, S.
Right arrow Articles by Nagai, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kobayashi, S.
Right arrow Articles by Nagai, K.
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?

Volume 272, Number 26, Issue of June 27, 1997 pp. 16262-16267
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Activation of pp60c-src Depending on Cell Density in PC12h Cells

(Received for publication, August 14, 1997, and in revised form, March 10, 1997)

Shin Kobayashi , Nobuaki Okumura , Tetsuya Nakamoto § , Masato Okada , Hisamaru Hirai § and Katsuya Nagai

From the Division of Protein Metabolism, Institute for Protein Research, Osaka University, 3-2 Yamada-Oka, Suita, Osaka 565, Japan and the § Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

The Src family tyrosine kinases and their substrates are involved in cell-cell and cell-matrix interactions. We found that in PC12h cells, an increase of cell density enhanced the tyrosine phosphorylation levels of several intracellular proteins including p130cas. Because it is a possible substrate for Src family kinases, we measured pp60c-src activity and found that it was higher in high density cultures than in low density cultures. This phenomenon was also observed in PC12 (the parental cell line of the PC12h subclone), Balb/c 3T3, Swiss 3T3, and Hela cells. One of the possible mechanisms regulating the kinase activity of pp60c-src is the phosphorylation and dephosphorylation of its negative regulatory site located at its C terminus. However, the tyrosine phosphorylation level of the regulatory site did not change depending on cell density. Subcellular fractionation showed that in high density culture, pp60c-src was translocated from detergent-soluble to detergent-insoluble fractions. These results suggest that cell-cell interaction might induce the activation of pp60c-src without changing its tyrosine phosphorylation levels.


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. Cell Sci.Home page
Y. Obara, K. Labudda, T. J. Dillon, and P. J. S. Stork
PKA phosphorylation of Src mediates Rap1 activation in NGF and cAMP signaling in PC12 cells
J. Cell Sci., December 1, 2004; 117(25): 6085 - 6094.
[Abstract] [Full Text] [PDF]

Home page
 J. Cell Biol.Home page
L. Zeng, X. Si, W.-P. Yu, H. T. Le, K. P. Ng, R. M.H. Teng, K. Ryan, D. Z.-M. Wang, S. Ponniah, and C. J. Pallen
PTP{alpha} regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
J. Cell Biol., January 2, 2003; 160(1): 137 - 146.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L.-T. Yang, K. Alexandropoulos, and J. Sap
c-SRC Mediates Neurite Outgrowth through Recruitment of Crk to the Scaffolding Protein Sin/Efs without Altering the Kinetics of ERK Activation
J. Biol. Chem., May 10, 2002; 277(20): 17406 - 17414.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Shima, N. Okumura, T. Takao, Y. Satomi, T. Yagi, M. Okada, and K. Nagai
Interaction of the SH2 Domain of Fyn with a Cytoskeletal Protein, beta -Adducin
J. Biol. Chem., November 2, 2001; 276(45): 42233 - 42240.
[Abstract] [Full Text] [PDF]

Home page
 JNCI J Natl Cancer InstHome page
E. A. Sheta, M. A. Harding, M. R. Conaway, and D. Theodorescu
Focal Adhesion Kinase, Rap1, and Transcriptional Induction of Vascular Endothelial Growth Factor
J Natl Cancer Inst, July 5, 2000; 92(13): 1065 - 1073.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
D. B. Batt and T. M. Roberts
Cell Density Modulates Protein-tyrosine Phosphorylation
J. Biol. Chem., February 6, 1998; 273(6): 3408 - 3414.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Noguchi, M. Tsuda, H. Takeda, T. Takada, K. Inagaki, T. Yamao, K. Fukunaga, T. Matozaki, and M. Kasuga
Inhibition of Cell Growth and Spreading by Stomach Cancer-associated Protein-tyrosine Phosphatase-1 (SAP-1) through Dephosphorylation of p130cas
J. Biol. Chem., April 27, 2001; 276(18): 15216 - 15224.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.