Open Access
Tumor Biology, volume 37, issue 9, pages 12697-12711
The alpha-fetoprotein (AFP) third domain: a search for AFP interaction sites of cell cycle proteins
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Division of Translational Medicine, Wadsworth Center, New York State Department of Health, Albany, USA
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Publication type: Journal Article
Publication date: 2016-07-22
General Medicine
Abstract
The carboxy-terminal third domain of alpha-fetoprotein (AFP-3D) is known to harbor binding and/or interaction sites for hydrophobic ligands, receptors, and binding proteins. Such reports have established that AFP-3D consists of amino acid (AA) sequence stretches on the AFP polypeptide that engages in protein-to-protein interactions with various ligands and receptors. Using a computer software program specifically designed for such interactions, the present report identified AA sequence fragments on AFP-3D that could potentially interact with a variety of cell cycle proteins. The cell cycle proteins identified were (1) cyclins, (2) cyclin-dependent kinases, (3) cell cycle-associated proteins (inhibitors, checkpoints, initiators), and (4) ubiquitin ligases. Following detection of the AFP-3D to cell cycle protein interaction sites, the computer-derived AFP localization AA sequences were compared and aligned with previously reported hydrophobic ligand and receptor interaction sites on AFP-3D. A literature survey of the association of cell cycle proteins with AFP showed both positive relationships and correlations. Previous reports of experimental AFP-derived peptides effects on various cell cycle proteins served to confirm and verify the present computer cell cycle protein identifications. Cell cycle protein interactions with AFP-CD peptides have been reported in cultured MCF-7 breast cancer cells subjected to mRNA microarray analysis. After 7 days in culture with MCF-7 cells, the AFP-derived peptides were shown to downregulate cyclin E, SKP2, checkpoint suppressors, cyclin-dependent kinases, and ubiquitin ligases that modulate cyclin E/CdK2 transition from the G1 to the S-phase of the cell cycle. Thus, the experimental data on AFP-CD interaction with cell cycle proteins were consistent with the “in silico” findings.
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Citations by publishers
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SAGE
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1 publication, 14.29%
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3
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- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
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Mizejewski G. The alpha-fetoprotein (AFP) third domain: a search for AFP interaction sites of cell cycle proteins // Tumor Biology. 2016. Vol. 37. No. 9. pp. 12697-12711.
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Mizejewski G. The alpha-fetoprotein (AFP) third domain: a search for AFP interaction sites of cell cycle proteins // Tumor Biology. 2016. Vol. 37. No. 9. pp. 12697-12711.
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TY - JOUR
DO - 10.1007/s13277-016-5131-x
UR - https://doi.org/10.1007%2Fs13277-016-5131-x
TI - The alpha-fetoprotein (AFP) third domain: a search for AFP interaction sites of cell cycle proteins
T2 - Tumor Biology
AU - Mizejewski, G.J.
PY - 2016
DA - 2016/07/22 00:00:00
PB - SAGE
SP - 12697-12711
IS - 9
VL - 37
SN - 1010-4283
SN - 1423-0380
ER -
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@article{2016_Mizejewski,
author = {G.J. Mizejewski},
title = {The alpha-fetoprotein (AFP) third domain: a search for AFP interaction sites of cell cycle proteins},
journal = {Tumor Biology},
year = {2016},
volume = {37},
publisher = {SAGE},
month = {jul},
url = {https://doi.org/10.1007%2Fs13277-016-5131-x},
number = {9},
pages = {12697--12711},
doi = {10.1007/s13277-016-5131-x}
}
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MLA
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Mizejewski, G.J.. “The alpha-fetoprotein (AFP) third domain: a search for AFP interaction sites of cell cycle proteins.” Tumor Biology, vol. 37, no. 9, Jul. 2016, pp. 12697-12711. https://doi.org/10.1007%2Fs13277-016-5131-x.