ArticleThe American journal of pathology2009
Aberrant heparan sulfate proteoglycan localization, despite normal exostosin, in central chondrosarcoma.
Article in The American journal of pathology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 49 citations in OpenAlex.
- Targeting syndecan-2 inhibits papillary thyroid cancer invasiveness and de-differentiation.BMC endocrine disorders · 2025Article
- IMP3, CDK4, MDM2 and β-catenin expression in Enchondroma and Central Chondrosarcoma: Diagnostic and prognostic utility.Clinics (Sao Paulo, Brazil) · 2024Article
- An Atlas of Heparan Sulfate Proteoglycans in the Postnatal Rat Lens.Investigative ophthalmology & visual science · 2021Article
- What Are the Potential Roles of Nuclear Perlecan and Other Heparan Sulphate Proteoglycans in the Normal and Malignant Phenotype.International journal of molecular sciences · 2021Review
- Outcome of First-Line Systemic Treatment for Unresectable Conventional, Dedifferentiated, Mesenchymal, and Clear Cell Chondrosarcoma.The oncologist · 2019Article
- Structural Features of Heparan Sulfate from Multiple Osteochondromas and Chondrosarcomas.Molecules (Basel, Switzerland) · 2018Article
- Chondrosarcoma: A Rare Misfortune in Aging Human Cartilage? The Role of Stem and Progenitor Cells in Proliferation, Malignant Degeneration and Therapeutic Resistance.International journal of molecular sciences · 2018Review
- Review
- In malignant cartilagenous tumors, immunohistochemical expression of procollagen PC1CP peptide is higher and that of PC2CP lower than in benign cartilaginous lesions.Virchows Archiv : an international journal of pathology · 2015Article
- Aberrant activation of Wnt/β-catenin signaling drives proliferation of bone sarcoma cells.Oncotarget · 2015Article
- Inhibition of mutant IDH1 decreases D-2-HG levels without affecting tumorigenic properties of chondrosarcoma cell lines.Oncotarget · 2015Article
- Genetic alterations in chondrosarcomas - keys to targeted therapies?Cellular oncology (Dordrecht, Netherlands) · 2014Review
- Heparan sulfate in the nucleus and its control of cellular functions.Matrix biology : journal of the International Society for Matrix Biology · 2014Review
- Elevated levels of Dickkopf-1 are associated with β-catenin accumulation and poor prognosis in patients with chondrosarcoma.PloS one · 2014Article
- Loss of pRB and p107 disrupts cartilage development and promotes enchondroma formation.Oncogene · 2013Article
- BMP and TGFbeta pathways in human central chondrosarcoma: enhanced endoglin and Smad 1 signaling in high grade tumors.BMC cancer · 2012Article
- Cartilage tumour progression is characterized by an increased expression of heparan sulphate 6O-sulphation-modifying enzymes.Virchows Archiv : an international journal of pathology · 2012Article
- Spinal chondrosarcoma: a review.Sarcoma · 2011Article
- No haploinsufficiency but loss of heterozygosity for EXT in multiple osteochondromas.The American journal of pathology · 2010Article
- Cartilage tumours and bone development: molecular pathology and possible therapeutic targets.Nature reviews. Cancer · 2010Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tumor suppressor genes EXT1 and EXT2 are involved in the formation of multiple osteochondromas, which can progress to become secondary peripheral chondrosarcomas. The most common chondrosarcoma subtype is primary central chondrosarcoma, which occurs in the medullar cavity of bone. The EXT1/EXT2 protein complex is involved in heparan sulfate proteoglycan (HSPG) biosynthesis, which is important for signal transduction of Indian hedgehog (IHH), WNT, and transforming growth factor (TGF)-beta. The role of EXT and its downstream targets in central chondrosarcomas is currently unknown. EXT1 and EXT2 were therefore evaluated in central chondrosarcomas at both the DNA and mRNA levels. Immunohistochemistry was used to assess HSPG (CD44v3 and SDC2), WNT (beta-catenin), and TGF-beta (PAI-1 and phosphorylated Smad2) signaling, whereas IHH signaling was studied both by quantitative polymerase chain reaction and in vitro. mRNA levels of both EXT1 and EXT2 were normal in central chondrosarcomas; genomic alterations were absent in these regions and in 30 other HSPG-related genes. Although HSPGs were aberrantly located (CD44v3 in the Golgi and SDC2 in cytoplasm and nucleus), this was not caused by mutation. WNT signaling negatively correlated with increasing histological grade, whereas TGF-beta positively correlated with increasing histological grade. IHH signaling was active, and inhibition decreased cell viability in one of six cell lines. Our data suggest that, despite normal EXT in central chondrosarcomas, HSPGs and HSPG-dependent signaling are affected in both central and peripheral chondrosarcomas.
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