1,25-Dihydroxyvitamin D3 increases secretion of insulin-like growth factor binding protein-4 (IGFBP-4) by human osteoblast-like cells in vitro and elevates IGFBP-4 serum levels in vivo

1993 ◽  
Vol 77 (5) ◽  
pp. 1190-1197 ◽  
Author(s):  
S. H. Scharla
Keyword(s):  
Growth Factor ◽  
Binding Protein ◽  
Serum Levels ◽  
Insulin Like Growth Factor ◽  
Human Osteoblast ◽  
Dihydroxyvitamin D3 ◽  
Factor Binding ◽  
1,25 Dihydroxyvitamin D3

scholarly journals Insulin-Like Growth Factor Binding Protein-3 Exerts Its Anti-Metastatic Effect in Aerodigestive Tract Cancers by Disrupting the Protein Stability of Vimentin

Cancers ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 1041
Author(s):  
Huong Thuy Le ◽  
Ho Jin Lee ◽  
Jaebeom Cho ◽  
Hye-Young Min ◽  
Ji-Sun Lee ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protein Stability ◽  
Binding Protein ◽  
Migration And Invasion ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Local Invasion ◽  
Igfbp 3

The proapoptotic, antiangiogenic, and antimetastatic activities of insulin-like growth factor binding protein-3 (IGFBP-3) through IGF-dependent or -independent mechanisms have been suggested in various types of human cancers. However, a mechanistic explanation of and downstream targets involved in the antimetastatic effect of IGFBP-3 is still lacking. In this study, by applying various in vitro and in vivo models, we show that IGFBP-3 suppresses migration and invasion of human head and neck squamous carcinoma (HNSCC) and non-small cell lung cancer (NSCLC) cells. Silencing IGFBP-3 expression elevated the migration and invasion of NSCLC and HNSCC cells in vitro and their local invasion and metastasis in vivo, whereas overexpression of IGFBP-3 decreased such prometastatic changes. Local invasion of 4-nitroquinoline-1-oxide (4-NQO)-induced HNSCC tumors was consistently significantly potentiated in Igfbp3 knockout mice compared with that in wild-type mice. Mechanistically, IGFBP-3 disrupted the protein stability of vimentin via direct binding and promoting its association with the E3 ligase FBXL14, causing proteasomal degradation. The C-terminal domain of IGFBP-3 and the head domain of vimentin are essential for their interaction. These results provide a molecular framework for IGFBP-3′s IGF-independent antimetastatic and antitumor activities.

scholarly journals Insulin-Like-Growth-Factor-Binding-Protein-3 (IGFBP-3) Contrasts Melanoma Progression In Vitro and In Vivo

PLoS ONE ◽  
2014 ◽  
Vol 9 (6) ◽  
pp. e98641 ◽  
Author(s):  
Antimo Naspi ◽  
Vincenzo Panasiti ◽  
Franco Abbate ◽  
Vincenzo Roberti ◽  
Valeria Devirgiliis ◽  
...  
Keyword(s):  
Growth Factor ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Melanoma Progression ◽  
Igfbp 3
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