ArticleThe Journal of biological chemistry2009
Zinc protoporphyrin regulates cyclin D1 expression independent of heme oxygenase inhibition.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 38 citations in OpenAlex.
- Proteomic analysis of the effect of hemin in breast cancer.Scientific reports · 2023Article
- Metalloporphyrins as Tools for Deciphering the Role of Heme Oxygenase in Renal Immune Injury.International journal of molecular sciences · 2023Review
- BACH1-Hemoxygenase-1 axis regulates cellular energetics and survival following sepsis.Free radical biology & medicine · 2022Article
- Zinc protoporphyrin binding to telomerase complexes and inhibition of telomerase activity.Pharmacology research & perspectives · 2021Article
- Metalloprotoporphyrin Inhibition of HCV NS3-4A Protease: Structure-Activity Relationships.Drug design, development and therapy · 2020Article
- JNK inhibition blocks piperlongumine-induced cell death and transcriptional activation of heme oxygenase-1 in pancreatic cancer cells.Apoptosis : an international journal on programmed cell death · 2019Article
- Heme oxygenase inhibition in cancers: possible tools and targets.Contemporary oncology (Poznan, Poland) · 2018Review
- Blocking heme oxygenase-1 by zinc protoporphyrin reduces tumor hypoxia-mediated VEGF release and inhibits tumor angiogenesis as a potential therapeutic agent against colorectal cancer.Journal of biomedical science · 2016Article
- Article
- Characterization of docosahexaenoic acid (DHA)-induced heme oxygenase-1 (HO-1) expression in human cancer cells: the importance of enhanced BTB and CNC homology 1 (Bach1) degradation.The Journal of nutritional biochemistry · 2014Article
- Topical hypochlorite ameliorates NF-κB-mediated skin diseases in mice.The Journal of clinical investigation · 2013Article
- Restoration of type I interferon expression by heme and related tetrapyrroles through inhibition of NS3/4A protease.The Journal of infectious diseases · 2013Article
- Analysis of lead toxicity in human cells.BMC genomics · 2012Article
- Curcumin ameliorates hydrogen peroxide-induced epithelial barrier disruption by upregulating heme oxygenase-1 expression in human intestinal epithelial cells.Digestive diseases and sciences · 2012Article
- Exacerbation of oxidative stress-induced cell death and differentiation in induced pluripotent stem cells lacking heme oxygenase-1.Stem cells and development · 2012Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Zinc protoporphyrin IX (ZnPP), an endogenous heme analogue that inhibits heme oxygenase (HO) activity, represses tumor growth. It can also translocate into the nucleus and up-regulate heme oxygenase 1 (HMOX1) gene expression. Here, we demonstrate that tumor cell proliferation was inhibited by ZnPP, whereas tin protoporphyrin (SnPP), another equally potent HO-1 inhibitor, had no effect. Microarray analysis on 128 tumorigenesis related genes showed that ZnPP suppressed genes involved in cell proliferation and angiogenesis. Among these genes, CYCLIN D1 (CCND1) was specifically inhibited as were its mRNA and protein levels. Additionally, ZnPP inhibited CCND1 promoter activity through an Sp1 and Egr1 overlapping binding site (S/E). We confirmed that ZnPP modulated the S/E site, at least partially by associating with Sp1 and Egr1 proteins rather than direct binding to DNA targets. Furthermore, administration of ZnPP significantly inhibited cyclin D1 expression and progression of a B-cell leukemia/lymphoma 1 tumor in mice by preferentially targeting tumor cells. These observations show HO independent effects of ZnPP on cyclin D1 expression and tumorigenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.