JBC

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


     


Originally published In Press as doi:10.1074/jbc.M207934200 on September 16, 2002

J. Biol. Chem., Vol. 277, Issue 47, 45243-45248, November 22, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/47/45243    most recent
M207934200v1
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 Park, S. G.
Right arrow Articles by Kim, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Park, S. G.
Right arrow Articles by Kim, S.
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?

Dose-dependent Biphasic Activity of tRNA Synthetase-associating Factor, p43, in Angiogenesis*

Sang Gyu ParkDagger , Young-Sun KangDagger , Young Ha AhnDagger , Soon Hee LeeDagger , Kwang-Rok Kim§, Kyu-Won Kim§, Gou Young Koh, Young-Gyu KoDagger ||, and Sunghoon KimDagger **

From the Dagger  National Creative Research Initiatives Center for ARS Network, the § Angiogenesis Research Laboratory, College of Pharmacy, Seoul National University, Seoul 151-742 and the  National Creative Research Initiatives Center for Cardiac Regeneration, Postech, Pohang 790-784, Korea

Mammalian aminoacyl tRNA synthetases form a macromolecular protein complex with three non-enzymatic cofactors. Among these factors, p43 is also secreted to work as a cytokine on endothelial as well as immune cells. Here we investigated the activity of p43 in angiogenesis and determined the related mediators. It promoted the migration of endothelial cells at low dose but induced their apoptosis at high dose. p43 at low concentration activated extracellular signal-regulating kinase, which resulted in the induction and activation of matrix metalloproteinase 9. In contrast, p43 at high concentration activated Jun N-terminal kinase, which mediated apoptosis of endothelial cells. These results suggest that p43 is a novel cytokine playing a dose-dependent biphasic role in angiogenesis.


* This work was supported by a grant from the National Creative Research Initiatives from the Ministry of Science and Technology, Korea.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| Current address: Graduate School of Biotechnology, Korea University, Seoul 131-701, Korea.

** To whom correspondence should be addressed: San 56-1, Shillim-dong, Kwanak-gu, Center for ARS Network, College of Pharmacy, Seoul National University, Seoul 151-746, Korea. Tel.: 82-2-880-8180; Fax: 82-2-875-2621; E-mail: sungkim@snu.ac.kr.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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
Proc. Natl. Acad. Sci. USAHome page
S. G. Park, P. Schimmel, and S. Kim
Aminoacyl tRNA synthetases and their connections to disease
PNAS, August 12, 2008; 105(32): 11043 - 11049.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
J. M. Han, B.-J. Park, S. G. Park, Y. S. Oh, S. J. Choi, S. W. Lee, S.-K. Hwang, S.-H. Chang, M.-H. Cho, and S. Kim
AIMP2/p38, the scaffold for the multi-tRNA synthetase complex, responds to genotoxic stresses via p53
PNAS, August 12, 2008; 105(32): 11206 - 11211.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K.-J. Kim, M. C. Park, S. J. Choi, Y. S. Oh, E.-C. Choi, H. J. Cho, M. H. Kim, S.-H. Kim, D. W. Kim, S. Kim, et al.
Determination of Three-dimensional Structure and Residues of the Novel Tumor Suppressor AIMP3/p18 Required for the Interaction with ATM
J. Biol. Chem., May 16, 2008; 283(20): 14032 - 14040.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
E. Kim, S. H. Kim, S. Kim, D. Cho, and T. S. Kim
AIMP1/p43 Protein Induces the Maturation of Bone Marrow-Derived Dendritic Cells with T Helper Type 1-Polarizing Ability
J. Immunol., March 1, 2008; 180(5): 2894 - 2902.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Pathol.Home page
J. M. Han, S. G. Park, B. Liu, B.-J. Park, J. Y. Kim, C. H. Jin, Y. W. Song, Z. Li, and S. Kim
Aminoacyl-tRNA Synthetase-Interacting Multifunctional Protein 1/p43 Controls Endoplasmic Reticulum Retention of Heat Shock Protein gp96: Its Pathological Implications in Lupus-Like Autoimmune Diseases
Am. J. Pathol., June 1, 2007; 170(6): 2042 - 2054.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
V. Shalak, L. Guigou, M. Kaminska, M.-P. Wautier, J.-L. Wautier, and M. Mirande
Characterization of p43(ARF), a Derivative of the p43 Component of Multiaminoacyl-tRNA Synthetase Complex Released during Apoptosis
J. Biol. Chem., April 13, 2007; 282(15): 10935 - 10943.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. M. Han, M. J. Lee, S. G. Park, S. H. Lee, E. Razin, E.-C. Choi, and S. Kim
Hierarchical Network between the Components of the Multi-tRNA Synthetase Complex: IMPLICATIONS FOR COMPLEX FORMATION
J. Biol. Chem., December 15, 2006; 281(50): 38663 - 38667.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. G. Park, Y. S. Kang, J. Y. Kim, C. S. Lee, Y. G. Ko, W. J. Lee, K.-U. Lee, Y. I. Yeom, and S. Kim
Hormonal activity of AIMP1/p43 for glucose homeostasis
PNAS, October 3, 2006; 103(40): 14913 - 14918.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
E. Kim, S. H. Kim, S. Kim, and T. S. Kim
The Novel Cytokine p43 Induces IL-12 Production in Macrophages via NF-{kappa}B Activation, Leading to Enhanced IFN-{gamma} Production in CD4+ T Cells
J. Immunol., January 1, 2006; 176(1): 256 - 264.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
S. G. Park, H. J. Kim, Y. H. Min, E.-C. Choi, Y. K. Shin, B.-J. Park, S. W. Lee, and S. Kim
From The Cover: Human lysyl-tRNA synthetase is secreted to trigger proinflammatory response
PNAS, May 3, 2005; 102(18): 6356 - 6361.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Pathol.Home page
S. G. Park, H. Shin, Y. K. Shin, Y. Lee, E.-C. Choi, B.-J. Park, and S. Kim
The Novel Cytokine p43 Stimulates Dermal Fibroblast Proliferation and Wound Repair
Am. J. Pathol., February 1, 2005; 166(2): 387 - 398.
[Abstract] [Full Text] [PDF]


Home page
J. Cell Sci.Home page
S. W. Lee, B. H. Cho, S. G. Park, and S. Kim
Aminoacyl-tRNA synthetase complexes: beyond translation
J. Cell Sci., September 1, 2004; 117(17): 3725 - 3734.
[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 © 2002 by the American Society for Biochemistry and Molecular Biology.