ArticleAntioxidants & redox signaling2014
Binding to WGR domain by salidroside activates PARP1 and protects hematopoietic stem cells from oxidative stress.
Article in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 31 citations in OpenAlex.
- Natural compounds from traditional Chinese medicine regulating stem cell fate: Identification and therapeutic potential.Chinese herbal medicines · 2025Review
- PARP1 UFMylation ensures the stability of stalled replication forks.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- How ligands regulate the binding of PARP1 with DNA: Deciphering the mechanism at the molecular level.PloS one · 2023Article
- A distinct subpopulation of leukemia initiating cells in acute precursor B lymphoblastic leukemia: quiescent phenotype and unique transcriptomic profile.Frontiers in oncology · 2022Article
- Biological function, mediate cell death pathway and their potential regulated mechanisms for post-mortem muscle tenderization of PARP1: A review.Frontiers in nutrition · 2022Review
- Combined pre-conditioning with salidroside and hypoxia improves proliferation, migration and stress tolerance of adipose-derived stem cells.Journal of cellular and molecular medicine · 2020Article
- Article
- Untargeted LC-MS/MS analysis reveals metabolomics feature of osteosarcoma stem cell response to methotrexate.Cancer cell international · 2020Article
- Human leukemia cells (HL-60) proteomic and biological signatures underpinning cryo-damage are differentially modulated by novel cryo-additives.GigaScience · 2019Article
- Molecular and epigenetic regulatory mechanisms of normal stem cell radiosensitivity.Cell death discovery · 2018Review
- Article
- Persistent response of Fanconi anemia haematopoietic stem and progenitor cells to oxidative stress.Cell cycle (Georgetown, Tex.) · 2017Article
- The Fanconi anemia pathway controls oncogenic response in hematopoietic stem and progenitor cells by regulating PRMT5-mediated p53 arginine methylation.Oncotarget · 2016Article
- Salidroside reduces renal cell carcinoma proliferation by inhibiting JAK2/STAT3 signaling.Cancer biomarkers : section A of Disease markers · 2016Article
- When Anti-Aging Studies Meet Cancer Chemoprevention: Can Anti-Aging Agent Kill Two Birds with One Blow?Current pharmacology reports · 2015Article
- Effects of rhodiola crenulata on mice hearts under severe sleep apnea.BMC complementary and alternative medicine · 2015Article
- Hepatoprotective effect of Rhodiola imbricata rhizome against paracetamol-induced liver toxicity in rats.Saudi journal of biological sciences · 2014Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
aimsA component of the base excision repair pathway, poly(ADP-ribose) polymerase-1 (PARP1) functions in multiple cellular processes, including DNA repair and programmed cell death. We previously showed that Salidroside, a phenylpropanoid glycoside isolated from medicinal plants, prevented the loss of hematopoietic stem cells (HSCs) in native mice and rescued HSCs repopulating in transplanted recipients under oxidative stress. The aim of this study was to investigate the mechanism by which PARP1 activation by Salidroside maintains HSCs under oxidative stress.
resultsWe found that although there were no spontaneous defects in hematopoiesis in Parp1(-/-) mice, oxidative stress compromised the repopulating capacity of Parp1(-/-) HSCs in transplanted recipient mice. A biochemical study using truncated proteins lacking the defined functional domains of PARP1 showed that the tryptophan-glycine-arginine-rich (WGR) domain of PARP1 was critical for Salidroside binding and subsequent PARP1 activation under oxidative stress. Functionally, complementation of Parp1(-/-) HSCs with full-length PARP1WT, but not the PARP1R591K mutant in WGR domain restored Salidroside-stimulated PARP1 activation in vitro. Mechanistically, activated PARP1 by Salidroside enhanced the repopulating capacity of the stressed HSCs by accelerating oxidative DNA damage repair. INNOVATIONS AND
conclusionOur findings reveal the action of mechanism for Salidroside in PARP1 stimulation and a novel role of PARP1 activation in maintaining HSC function under oxidative stress.
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