Ask about this productRelated genes to: HPSE antibody
- Gene:
- HPSE NIH gene
- Name:
- heparanase
- Previous symbol:
- -
- Synonyms:
- HPA, HSE1, HPSE1
- Chromosome:
- 4q21.23
- Locus Type:
- gene with protein product
- Date approved:
- 1999-09-28
- Date modifiied:
- 2016-10-05
Related products to: HPSE antibody
Related articles to: HPSE antibody
- Desmoplasia, a dense fibrotic reaction, is a hallmark of pancreatic ductal adenocarcinoma (PDAC) and fuels chemoresistance through multiple mechanisms. Here, we evaluated heparanase (HPSE), an endoglycosidase that remodels extracellular matrix (ECM) and drives fibrogenesis, as a potential target in PDAC. Immunohistochemical analysis of human PDAC tissues showed elevated HPSE expression, along with increased levels of fibroblast growth factors 1 and 2 (FGF1/2), reflecting their liberation by HPSE-catalyzed heparan sulfate cleavage. High expression of all three proteins was associated with worse overall and disease-free survival. In vitro coculture assays showed that the HPSE inhibitor PI-88 suppressed PDAC cell-induced activation of pancreatic stellate cells (PSCs) and prevented ECM stiffening without inducing cytotoxicity. Mechanistically, tumor-derived HPSE activated ERK signaling and promoted FGF1/2 production in PSCs, both of which were effectively suppressed by PI-88. In orthotopic mouse models, gemcitabine treatment upregulated HPSE and FGF1/2, whereas gemcitabine-resistant tumors exhibited further increases in these factors, accompanied by enhanced PSC activation and collagen deposition. Importantly, triple therapy with PI-88, gemcitabine, and Abraxane significantly suppressed tumor growth and prolonged survival relative to all mono- and doublet regimens. Immune profiling revealed that this combination reduced PSC activation, contracted M2 macrophage and regulatory T cell populations, and expanded M1 macrophages, CD8⁺ T cells, and NK cells. In conclusion, these data underscore HPSE as a key driver of fibrosis and chemoresistance in PDAC and support HPSE inhibition as a promising strategy to enhance therapeutic efficacy. - Source: PubMed
Publication date: 2026/05/08
Chen Chang-JungWang Hao-ChenHuang Wen-YenChang Stanley Shi-ChungChang AlarngLin Chieh-LiangYang Chih-YaShan Yan-Shen - Heparanase uniquely cleaves heparan sulfate, the main component of the outer layer of endothelial cell plasma membranes, promoting tumour invasion and dissemination. However, it can also enhance tumour immune surveillance and clearance. heparanase's versatility extends to pro-thrombotic properties, such as the promotion of tissue factor release. Interestingly, elevated heparanase levels have been found in ovarian cancer (OC), which has a notably high incidence of venous thrombosis. Previously, single-nucleotide polymorphisms (SNPs) of HPSE were shown to modulate mRNA and protein levels, possibly predicting disease outcomes. - Source: PubMed
Publication date: 2026/05/05
de Melo Inês GuerraTavares ValériaSavva-Bordalo JoanaRei MarianaLiz-Pimenta JoanaPereira DeolindaMedeiros Rui - Heparanase-1 (HPSE) is the only mammalian endo-β-D-glucuronidase that cleaves heparan sulfate (HS) polysaccharides on cell surfaces and in extracellular matrices. HPSE contributes to diverse pathological conditions, particularly in the processes driving injury to the luminal glycocalyx overlying vascular endothelial cells. Existing methods for assaying the activity of HPSE are insensitive and lack specificity. Here, we present a new method, Single Heparan Sulfate Substrate-Based Isotope Dilution Mass Spectrometry (SHS-IDMS), that permits the quantitative measurement of HPSE activity in complex biological matrices like plasma. The method involves the use of a structurally defined-HS 12-mer substrate that yields a consistent disaccharide product upon HPSE digestion. The disaccharide product is quantified using LC-MS/MS and a 13C-labeled disaccharide calibrant. The method demonstrates strong linearity, high sensitivity, and resistance to interference by heparanase-2 (HPSE-2). Using this method, we detected significant, quantitative differences in HPSE activity using 20 μL plasma samples from children with sepsis compared to samples from healthy children. Moreover, we found that plasma HPSE activity correlated with circulating levels of syndecan-1 and angiopoietin-2, supporting the hypothesis that HPSE may contribute to endothelial glycocalyx injury and pathological endothelial activation under septic conditions. The new method will advance research in the biology of this important enzyme. - Source: PubMed
Wang ZhangjieRichter RobertSu GuoweiXu YongmeiBecker YannicHaller HermannLiu Jian - The aim was to evaluate the effects of liberal and restrictive intraoperative fluid strategies on the gene-level markers of endothelial glycocalyx biology during major urological surgery. Specifically, (ANP) representing the ANP axis, the core proteoglycan (syndecan-1), and key genes of glycosaminoglycan metabolism, (heparanase) and (hyaluronan synthase-2), were examined. - Source: PubMed
Publication date: 2026/04/10
Kivanc DemetOztan GozdeSenturk Ciftci HayriyeKaradeniz Sedat TanjuOguz Suleyman RustuKulaksiz Mammadov BurcuSavran Karadeniz Meltem - Sepsis is a life-threatening condition and a leading cause of in-hospital mortality, characterized by dysregulated inflammatory responses. Using murine models, this study investigated whether Shenfu Injection (SFI), a clinically approved botanical formulation, protects against sepsis by preserving glycocalyx integrity and modulating noncanonical inflammasome signaling mediated by murine caspase-11. - Source: PubMed
Publication date: 2026/04/01
Zhang ChangChen HuanWang ZhongtaiWang XiangyuLi ZhaozhengLiang FangShi JianLu BenTang Yiting