Insulin-Like Growth Factor Binding Protein-3 Binds to Histone 3
Insulin-like growth factor (IGF) binding protein-3 (IGFBP-3) is an essential protein that regulates cellular processes such as cell proliferation, apoptosis, and differentiation. It is known to bind with several proteins to carry out various cellular functions. In this study, we report for the first...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2021-01-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | https://www.mdpi.com/1422-0067/22/1/407 |
_version_ | 1797542569005023232 |
---|---|
author | Apurva Bhardwaj Kumar Alok Pathak Anuraag Shrivastav Shailly Varma Shrivastav |
author_facet | Apurva Bhardwaj Kumar Alok Pathak Anuraag Shrivastav Shailly Varma Shrivastav |
author_sort | Apurva Bhardwaj |
collection | DOAJ |
description | Insulin-like growth factor (IGF) binding protein-3 (IGFBP-3) is an essential protein that regulates cellular processes such as cell proliferation, apoptosis, and differentiation. It is known to bind with several proteins to carry out various cellular functions. In this study, we report for the first time that IGFBP-3 is a histone 3 (H3) binding protein. Sub-cellular fractionation was performed to separate into cytosolic fraction, nucleic acid binding protein fraction and insoluble nuclear fraction. Using ligand blot analysis, we identified a ~15 kDa protein that can interact with IGFBP-3 in the insoluble nuclear fraction. The 15 kDa protein was confirmed as histone 3 by far-Western blot analysis and co-immunoprecipitation experiments. A dot-blot experiment further validated the binding of IGFBP-3 with H3. The intensity of IGFBP-3 on dot-blot showed a proportional increase with H3 concentrations between 2.33 pmol–37.42 pmol. Our results support the presence of protein-protein interaction between IGFBP-3 and H3. The physical binding between IGFBP-3 and H3 could indicate its yet another cellular role in regulating the chromatin remodeling for gene transcription. |
first_indexed | 2024-03-10T13:32:25Z |
format | Article |
id | doaj.art-eb82eb51b7b142aab44bdb4b050a44fa |
institution | Directory Open Access Journal |
issn | 1661-6596 1422-0067 |
language | English |
last_indexed | 2024-03-10T13:32:25Z |
publishDate | 2021-01-01 |
publisher | MDPI AG |
record_format | Article |
series | International Journal of Molecular Sciences |
spelling | doaj.art-eb82eb51b7b142aab44bdb4b050a44fa2023-11-21T07:48:00ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672021-01-0122140710.3390/ijms22010407Insulin-Like Growth Factor Binding Protein-3 Binds to Histone 3Apurva Bhardwaj0Kumar Alok Pathak1Anuraag Shrivastav2Shailly Varma Shrivastav3Department of Biology, The University of Winnipeg, Winnipeg, MB R3B 2G3, CanadaResearch Institute of Oncology and Hematology, CancerCare Manitoba, Winnipeg, MB R3E 0V9, CanadaDepartment of Biology, The University of Winnipeg, Winnipeg, MB R3B 2G3, CanadaDepartment of Biology, The University of Winnipeg, Winnipeg, MB R3B 2G3, CanadaInsulin-like growth factor (IGF) binding protein-3 (IGFBP-3) is an essential protein that regulates cellular processes such as cell proliferation, apoptosis, and differentiation. It is known to bind with several proteins to carry out various cellular functions. In this study, we report for the first time that IGFBP-3 is a histone 3 (H3) binding protein. Sub-cellular fractionation was performed to separate into cytosolic fraction, nucleic acid binding protein fraction and insoluble nuclear fraction. Using ligand blot analysis, we identified a ~15 kDa protein that can interact with IGFBP-3 in the insoluble nuclear fraction. The 15 kDa protein was confirmed as histone 3 by far-Western blot analysis and co-immunoprecipitation experiments. A dot-blot experiment further validated the binding of IGFBP-3 with H3. The intensity of IGFBP-3 on dot-blot showed a proportional increase with H3 concentrations between 2.33 pmol–37.42 pmol. Our results support the presence of protein-protein interaction between IGFBP-3 and H3. The physical binding between IGFBP-3 and H3 could indicate its yet another cellular role in regulating the chromatin remodeling for gene transcription.https://www.mdpi.com/1422-0067/22/1/407IGFBP-3histone 3protein-protein interaction |
spellingShingle | Apurva Bhardwaj Kumar Alok Pathak Anuraag Shrivastav Shailly Varma Shrivastav Insulin-Like Growth Factor Binding Protein-3 Binds to Histone 3 International Journal of Molecular Sciences IGFBP-3 histone 3 protein-protein interaction |
title | Insulin-Like Growth Factor Binding Protein-3 Binds to Histone 3 |
title_full | Insulin-Like Growth Factor Binding Protein-3 Binds to Histone 3 |
title_fullStr | Insulin-Like Growth Factor Binding Protein-3 Binds to Histone 3 |
title_full_unstemmed | Insulin-Like Growth Factor Binding Protein-3 Binds to Histone 3 |
title_short | Insulin-Like Growth Factor Binding Protein-3 Binds to Histone 3 |
title_sort | insulin like growth factor binding protein 3 binds to histone 3 |
topic | IGFBP-3 histone 3 protein-protein interaction |
url | https://www.mdpi.com/1422-0067/22/1/407 |
work_keys_str_mv | AT apurvabhardwaj insulinlikegrowthfactorbindingprotein3bindstohistone3 AT kumaralokpathak insulinlikegrowthfactorbindingprotein3bindstohistone3 AT anuraagshrivastav insulinlikegrowthfactorbindingprotein3bindstohistone3 AT shaillyvarmashrivastav insulinlikegrowthfactorbindingprotein3bindstohistone3 |