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N-Acetylgalactosaminyltransferase 14, a novel insulin-like growth factor binding protein-3 binding partner
- Source :
-
Biochemical & Biophysical Research Communications . Jun2007, Vol. 357 Issue 2, p360-365. 6p. - Publication Year :
- 2007
-
Abstract
- 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. [Copyright &y& Elsevier]
- Subjects :
- *HYPOGLYCEMIC agents
*PANCREATIC secretions
*CYTOKINES
*CARRIER proteins
Subjects
Details
- Language :
- English
- ISSN :
- 0006291X
- Volume :
- 357
- Issue :
- 2
- Database :
- Academic Search Index
- Journal :
- Biochemical & Biophysical Research Communications
- Publication Type :
- Academic Journal
- Accession number :
- 24782272
- Full Text :
- https://doi.org/10.1016/j.bbrc.2007.03.153