Ullah M, Qian NPM, Yannarelli G, Akbar A. Heat shock protein 20 promotes sirtuin 1-dependent cell proliferation in induced pluripotent stem cells . World J Stem Cells 2021; 13(6): 659-669 [PMID: 34249234 DOI: 10.4252/wjsc.v13.i6.659]
Corresponding Author of This Article
Mujib Ullah, MD, PhD, Doctor, Institute for Immunity and Transplantation, Stem Cell Biology and Regenerative Medicine, School of Medicine, Stanford University, 450 Serra Mall, Stanford, CA 94304, United States. ullah@stanford.edu
Research Domain of This Article
Cell Biology
Article-Type of This Article
Basic Study
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
World J Stem Cells. Jun 26, 2021; 13(6): 659-669 Published online Jun 26, 2021. doi: 10.4252/wjsc.v13.i6.659
Heat shock protein 20 promotes sirtuin 1-dependent cell proliferation in induced pluripotent stem cells
Mujib Ullah, Nicole Pek Min Qian, Gustavo Yannarelli, Asma Akbar
Mujib Ullah, Institute for Immunity and Transplantation, Stem Cell Biology and Regenerative Medicine, School of Medicine, Stanford University, Stanford, CA 94304, United States
Nicole Pek Min Qian, Immunology and School of Medicine, Stanford University, Stanford, CA 94304, United States
Gustavo Yannarelli, Laboratorio de Regulación Génica y Células Madre, Instituto de Medicina Traslacional, Trasplante y Bioingeniería (IMeTTyB), Universidad Favaloro-CONICET, Buenos Aires 1078, Argentina
Asma Akbar, Institute for Molecular Medicine, School of Medicine, Stanford University, Stanford, CA 94304, United States
Author contributions: Ullah M contributed to the conceptualization, data mining and experiments, coordinated the project, and wrote the paper; Ullah M, Yannarelli G, and Akbar A contributed to the data analyses and writing of the manuscript; Ullah M, Qian NMP, Yannarelli G, and Akbar A analyzed the data and wrote the manuscript, performed the manuscript review, made editing suggestions, and provided final approval; All authors have read and approved the final manuscript.
Institutional review board statement: The study was reviewed and approved by the internal review board of the University Institutional Review Board.
Conflict-of-interest statement: The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Data sharing statement: No additional data are available.
Open-Access: This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/Licenses/by-nc/4.0/
Corresponding author: Mujib Ullah, MD, PhD, Doctor, Institute for Immunity and Transplantation, Stem Cell Biology and Regenerative Medicine, School of Medicine, Stanford University, 450 Serra Mall, Stanford, CA 94304, United States. ullah@stanford.edu
Received: February 12, 2021 Peer-review started: February 12, 2021 First decision: March 17, 2021 Revised: March 27, 2021 Accepted: May 27, 2021 Article in press: May 27, 2021 Published online: June 26, 2021 Processing time: 134 Days and 7.7 Hours
ARTICLE HIGHLIGHTS
Research background
The heat shock protein 20 (HSP20) protects cells from cellular damage and dysfunctional enzyme attacks. Therefore, we used an induced pluripotent stem cell (iPSC) model to study the proliferative effects of HSP20, and investigated the effects of HSP20 on cell growth, stemness, pluripotency, and cellular activity.
Research motivation
HSPs make healthy cells stronger by protecting them against stress and injuries, making individuals more resistant to diseases. HSP20 constitutes the first line of protection for cells exposed to stressful/damaged conditions, thereby making it an ideal protein for clinical significance in different diseases.
Research objectives
This study highlighted the more recent findings illustrating the proliferative effects of HSP20 and its potential as a therapeutic agent, with the aim of determining the importance of HSP20 overexpression in iPSCs compared to their control.
Research methods
We used iPSCs, which retain their potential for cell proliferation. HSP20 overexpression effectively enhanced the proliferation of cells. Overexpression of HSP20 in iPSCs was characterized by immunocytochemistry staining and real-time polymerase chain reaction analysis. We further used cell culture, cell counting, western blotting, and flow cytometry analysis for the validation of HSP20 overexpression and its mechanism.
Research results
Our present findings revealed the role of HSP20 in promoting cell proliferation. Our results also showed that the action of HSP20 is dependent on sirtuin 1 (SIRT1).
Research conclusions
HSP20 overexpression resulted in significantly better proliferation. These findings provide adequate evidence for mechanistic study of HSP20 role in SIRT1-dependent cell proliferation in iPSCs.
Research perspectives
Resolving the detailed cellular and molecular mechanisms underlying cell proliferation is crucial. In this study, we demonstrated the role of iPSCs overexpressing HSP20 in proliferation and stemness to better understand the underlying molecular mechanisms.
