ArticleCancers2020
Two Secreted Proteoglycans, Activators of Urothelial Cell-Cell Adhesion, Negatively Contribute to Bladder Cancer Initiation and Progression.
Article in Cancers, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- Reversible homodimerization of a small leucine-rich proteoglycan PRELP modulates the interactions with TGFβ1 and IGFI-R.The Journal of biological chemistry · 2026Article
- Protective effects of PRELP protein in a mouse model of pulmonary fibrosis.Respiratory research · 2026Article
- PRELP negatively regulates IL-17A-mediated proliferation and the inflammatory response in psoriasis.Signal transduction and targeted therapy · 2026Article
- Construction and evaluation of a bladder cancer prognosis model based on super-enhancer-associated genes.Discover oncology · 2026Article
- Proteoglycans in Breast Cancer: Friends and Foes.Biomolecules · 2025Review
- Imidacloprid contributes to bladder cancer progression: preliminary evidence based on network toxicology, machine learning and molecular docking.BMC pharmacology & toxicology · 2025Article
- PRELP functions via multiple interactions with intrinsically weak affinity relying on ECM anchoring and remodeling.Scientific reports · 2025Article
- Mechanistic Insights into Tumorigenesis from Serum Proteins.medRxiv : the preprint server for health sciences · 2025Article
- PRELP inhibits colorectal cancer progression by suppressing epithelial-mesenchymal transition and angiogenesis via the inactivation of the FGF1/PI3K/AKT pathway.Apoptosis : an international journal on programmed cell death · 2025Article
- Analysis of metastasis‑related risk factors and clinical relevance in adult soft‑tissue sarcoma.Oncology letters · 2024Article
- Investigating the role of disulfidptosis related genes in radiotherapy resistance of lung adenocarcinoma.Frontiers in medicine · 2024Article
- Correlation of the tumor escape phenotype with loss of PRELP expression in melanoma.Journal of translational medicine · 2023Article
- The critical role of circular RNAs in drug resistance in gastrointestinal cancers.Medical oncology (Northwood, London, England) · 2023Review
- PRELP secreted from mural cells protects the function of blood brain barrier through regulation of endothelial cell-cell integrity.Frontiers in cell and developmental biology · 2023Article
- Tumor Suppressive Role of theJournal of personalized medicine · 2022Article
- Repression of the PRELP gene is relieved by histone deacetylase inhibitors through acetylation of histone H2B lysine 5 in bladder cancer.Clinical epigenetics · 2022Article
- Article
- A four-miRNA signature in serum as a biomarker for bladder cancer diagnosis.American journal of translational research · 2022Article
- Article
- Comprehensive investigation of proteoglycan gene expression in breast cancer: Discovery of a unique proteoglycan gene signature linked to the malignant phenotype.Proteoglycan researchArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
22 authors at 9 institutions in 4 countries.
Funding
Abstract
Osteomodulin (OMD) and proline/arginine-rich end leucine repeat protein (PRELP) are secreted extracellular matrix proteins belonging to the small leucine-rich proteoglycans family. We found that OMD and PRELP were specifically expressed in umbrella cells in bladder epithelia, and their expression levels were dramatically downregulated in all bladder cancers from very early stages and various epithelial cancers. Our in vitro studies including gene expression profiling using bladder cancer cell lines revealed that OMD or PRELP application suppressed the cancer progression by inhibiting TGF-β and EGF pathways, which reversed epithelial-mesenchymal transition (EMT), activated cell-cell adhesion, and inhibited various oncogenic pathways. Furthermore, the overexpression of OMD in bladder cancer cells strongly inhibited the anchorage-independent growth and tumorigenicity in mouse xenograft studies. On the other hand, we found that in the bladder epithelia, the knockout mice of OMD and/or PRELP gene caused partial EMT and a loss of tight junctions of the umbrella cells and resulted in formation of a bladder carcinoma in situ-like structure by spontaneous breakdowns of the umbrella cell layer. Furthermore, the ontological analysis of the expression profiling of an OMD knockout mouse bladder demonstrated very high similarity with those obtained from human bladder cancers. Our data indicate that OMD and PRELP are endogenous inhibitors of cancer initiation and progression by controlling EMT. OMD and/or PRELP may have potential for the treatment of bladder cancer.
Indexed as
Identifiers
What OpenQuestion holds
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.