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Title: Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1

Abstract

AIMP1 (previously known as p43) is first found as a factor associated with a macromolecular tRNA synthetase complex. However, it is also secreted and acts on diverse target cells such as endothelial cells, macrophages, and fibroblasts to control angiogenesis, inflammation, and dermal regeneration, respectively. We previously showed that AIMP1 induces the death of endothelial cell but proliferation of fibroblasts and activates macrophages. In this work, we found that elastase 2-cleaved AIMP1 retained its pro-apoptotic activity to endothelial cells but lost the growth-stimulatory activity to fibroblasts. To determine the functional domains responsible for each activity, we generated several deletion fragments of AIMP1 and compared the activities to the target cells. AIMP1 promoted endothelial cell death and caspase-3 activation through its 101-114 amino acid region, fibroblast proliferation through its 6-46 amino acid region, and endothelial migration through its 114-192 amino acid region as revealed by deletion mapping. Thus, this work revealed that AIMP1 uses different regions for its diverse extracellular activities.

Authors:
 [1];  [2];  [1];  [3]
  1. Imagene Co. Biotechnology Incubating Center, Golden Helix, Seoul National University, Seoul 151-741 (Korea, Republic of)
  2. National Creative Research Initiatives Center for ARS Network, College of Pharmacy, Seoul National University, Seoul 151-741 (Korea, Republic of)
  3. National Creative Research Initiatives Center for ARS Network, College of Pharmacy, Seoul National University, Seoul 151-741 (Korea, Republic of). E-mail: sungkim@snu.ac.kr
Publication Date:
OSTI Identifier:
20798868
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 342; Journal Issue: 1; Other Information: DOI: 10.1016/j.bbrc.2006.01.117; PII: S0006-291X(06)00165-3; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; AMINO ACIDS; APOPTOSIS; CELL PROLIFERATION; DEATH; FIBROBLASTS; INFLAMMATION; LIGASES; MACROPHAGES; REGENERATION

Citation Formats

Han, Jung Min, Park, Sang Gyu, Lee, Yeonsook, and Kim, Sunghoon. Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1. United States: N. p., 2006. Web. doi:10.1016/j.bbrc.2006.01.117.
Han, Jung Min, Park, Sang Gyu, Lee, Yeonsook, & Kim, Sunghoon. Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1. United States. doi:10.1016/j.bbrc.2006.01.117.
Han, Jung Min, Park, Sang Gyu, Lee, Yeonsook, and Kim, Sunghoon. Fri . "Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1". United States. doi:10.1016/j.bbrc.2006.01.117.
@article{osti_20798868,
title = {Structural separation of different extracellular activities in aminoacyl-tRNA synthetase-interacting multi-functional protein, p43/AIMP1},
author = {Han, Jung Min and Park, Sang Gyu and Lee, Yeonsook and Kim, Sunghoon},
abstractNote = {AIMP1 (previously known as p43) is first found as a factor associated with a macromolecular tRNA synthetase complex. However, it is also secreted and acts on diverse target cells such as endothelial cells, macrophages, and fibroblasts to control angiogenesis, inflammation, and dermal regeneration, respectively. We previously showed that AIMP1 induces the death of endothelial cell but proliferation of fibroblasts and activates macrophages. In this work, we found that elastase 2-cleaved AIMP1 retained its pro-apoptotic activity to endothelial cells but lost the growth-stimulatory activity to fibroblasts. To determine the functional domains responsible for each activity, we generated several deletion fragments of AIMP1 and compared the activities to the target cells. AIMP1 promoted endothelial cell death and caspase-3 activation through its 101-114 amino acid region, fibroblast proliferation through its 6-46 amino acid region, and endothelial migration through its 114-192 amino acid region as revealed by deletion mapping. Thus, this work revealed that AIMP1 uses different regions for its diverse extracellular activities.},
doi = {10.1016/j.bbrc.2006.01.117},
journal = {Biochemical and Biophysical Research Communications},
number = 1,
volume = 342,
place = {United States},
year = {Fri Mar 31 00:00:00 EST 2006},
month = {Fri Mar 31 00:00:00 EST 2006}
}