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

Journal Article · · Biochemical and Biophysical Research Communications
 [1];  [2];  [1];  [1];  [1];  [2];  [1];  [1]
  1. Institute of Basic Medical Sciences, Taiping Road 27, Beijing 100850 (China)
  2. College of Life Sciences, Hebei University, Baoding, Hebei 100072 (China)

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.

OSTI ID:
20991362
Journal Information:
Biochemical and Biophysical Research Communications, Vol. 357, 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); ISSN 0006-291X
Country of Publication:
United States
Language:
English