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Title: N-Acetylgalactosaminyltransferase 14, a novel insulin-like growth factor binding protein-3 binding partner

Abstract

Insulin-like growth factor binding protein-3 (IGFBP-3) is known to inhibit cell proliferation and induce apoptosis in IGF-dependent and IGF-independent manners, but the mechanism underlying IGF-independent effects is not yet clear. In a yeast two-hybrid assay, IGFBP-3 was used as the bait to screen a human fetal liver cDNA library for it interactors that may potentially mediate IGFBP-3-regulated functions. N-Acetylgalactosaminyltransferase 14 (GalNAc-T14), a member of the GalNAc-Tases family, was identified as a novel IGFBP-3 binding partner. This interaction involved the ricin-type beta-trefoil domain of GalNAc-T14. The interaction between IGFBP-3 and GalNAc-T14 was reconfirmed in vitro and in vivo, using GST pull-down, co-immunoprecipitation and mammalian two-hybrid assays. Our findings may provide new clues for further study on the mechanism behind the IGF-independent effects of IGFBP-3 promoting apoptosis. The role of GalNAc-T14 as an intracellular mediator of the effects of IGFBP-3 need to be verified in future studies.

Authors:
 [1];  [2];  [3];  [1];  [1];  [1];  [3];  [1];  [4]
  1. Institute of Basic Medical Sciences, Taiping Road 27, Beijing 100850 (China)
  2. (China)
  3. College of Life Sciences, Hebei University, Baoding, Hebei 100072 (China)
  4. Institute of Basic Medical Sciences, Taiping Road 27, Beijing 100850 (China). E-mail: xudg@nic.bmi.ac.cn
Publication Date:
OSTI Identifier:
20991362
Resource Type:
Journal Article
Resource Relation:
Journal Name: Biochemical and Biophysical Research Communications; Journal Volume: 357; Journal Issue: 2; Other Information: DOI: 10.1016/j.bbrc.2007.03.153; PII: S0006-291X(07)00598-0; Copyright (c) 2007 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; APOPTOSIS; CELL PROLIFERATION; GROWTH FACTORS; HYBRIDIZATION; IN VITRO; IN VIVO; INSULIN; LIVER; YEASTS

Citation Formats

Wu, Chen, College of Life Sciences, Hebei University, Baoding, Hebei 100072, Yao, Guangyin, Zou, Minji, Chen, Guangyu, Wang, Min, Liu, Jingqian, Wang, Jiaxi, and Xu, Donggang. N-Acetylgalactosaminyltransferase 14, a novel insulin-like growth factor binding protein-3 binding partner. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2007.03.153.
Wu, Chen, College of Life Sciences, Hebei University, Baoding, Hebei 100072, Yao, Guangyin, Zou, Minji, Chen, Guangyu, Wang, Min, Liu, Jingqian, Wang, Jiaxi, & Xu, Donggang. N-Acetylgalactosaminyltransferase 14, a novel insulin-like growth factor binding protein-3 binding partner. United States. doi:10.1016/j.bbrc.2007.03.153.
Wu, Chen, College of Life Sciences, Hebei University, Baoding, Hebei 100072, Yao, Guangyin, Zou, Minji, Chen, Guangyu, Wang, Min, Liu, Jingqian, Wang, Jiaxi, and Xu, Donggang. Fri . "N-Acetylgalactosaminyltransferase 14, a novel insulin-like growth factor binding protein-3 binding partner". United States. doi:10.1016/j.bbrc.2007.03.153.
@article{osti_20991362,
title = {N-Acetylgalactosaminyltransferase 14, a novel insulin-like growth factor binding protein-3 binding partner},
author = {Wu, Chen and College of Life Sciences, Hebei University, Baoding, Hebei 100072 and Yao, Guangyin and Zou, Minji and Chen, Guangyu and Wang, Min and Liu, Jingqian and Wang, Jiaxi and Xu, Donggang},
abstractNote = {Insulin-like growth factor binding protein-3 (IGFBP-3) is known to inhibit cell proliferation and induce apoptosis in IGF-dependent and IGF-independent manners, but the mechanism underlying IGF-independent effects is not yet clear. In a yeast two-hybrid assay, IGFBP-3 was used as the bait to screen a human fetal liver cDNA library for it interactors that may potentially mediate IGFBP-3-regulated functions. N-Acetylgalactosaminyltransferase 14 (GalNAc-T14), a member of the GalNAc-Tases family, was identified as a novel IGFBP-3 binding partner. This interaction involved the ricin-type beta-trefoil domain of GalNAc-T14. The interaction between IGFBP-3 and GalNAc-T14 was reconfirmed in vitro and in vivo, using GST pull-down, co-immunoprecipitation and mammalian two-hybrid assays. Our findings may provide new clues for further study on the mechanism behind the IGF-independent effects of IGFBP-3 promoting apoptosis. The role of GalNAc-T14 as an intracellular mediator of the effects of IGFBP-3 need to be verified in future studies.},
doi = {10.1016/j.bbrc.2007.03.153},
journal = {Biochemical and Biophysical Research Communications},
number = 2,
volume = 357,
place = {United States},
year = {Fri Jun 01 00:00:00 EDT 2007},
month = {Fri Jun 01 00:00:00 EDT 2007}
}