HPSE
GeneName
HPSE
Summary
HPSE, also known as Hep, Hpa, or HPA-1, is a 61 kDa endo-β-glucuronidase that is primarily located in the extracellular matrix and extracellular region. It plays a pivotal role in the degradation of heparan sulfate proteoglycans, facilitating various biological processes such as angiogenesis, cell-matrix adhesion, and the establishment of the endothelial barrier. HPSE is involved in the regulation of blood coagulation and promotes vascular endothelial growth factor production, which is essential for angiogenesis. Additionally, it has been implicated in hair follicle development and osteoblast proliferation. Its activity is linked to both intracellular and extracellular compartments, including lysosomes and membrane rafts.
Importance
HPSE is relevant to: - Angiogenesis and wound healing, making it a potential target for therapeutic interventions in tissue repair and regeneration - Cancer biology, as it can influence tumour progression through its effects on the extracellular matrix and cell migration - Vascular diseases, given its role in endothelial barrier function and regulation of blood coagulation - Dermatological research, due to its involvement in hair follicle development and skin repair mechanisms
Top Products
For researchers investigating HPSE, we highly recommend the top-selling recombinant antibody, Anti-Heparanase 1 antibody [EPR22365-230] (ab254254). This antibody has been validated in knockout models, ensuring reliable performance in Western blotting (WB). With 4 citations, it demonstrates a growing trust within the research community. Its recombinant nature provides batch-to-batch consistency, making it an excellent choice for those requiring dependable results in their studies of heparanase. The Anti-Heparanase 1 antibody ELISA Kit (ab254254), supported by 4 citations, is an excellent option for researchers looking to measure HPSE levels with confidence.
Abcam Product Citation Summary
The data indicates that the HPSE antibody (ab232817) has been utilised in Western Blot experiments specifically on human tumour tissues from patients with hepatocellular carcinoma (HCC). This suggests a focus on the role of HPSE in cancer research, particularly in liver cancer.
Abcam Product Citation Table
Function
Endoglycosidase that cleaves heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. Participates in extracellular matrix (ECM) degradation and remodeling. Selectively cleaves the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave the linkage between a glucuronic acid unit and an N-sulfo glucosamine unit carrying a 2-O-sulfo group, but not linkages between a glucuronic acid unit and a 2-O-sulfated iduronic acid moiety. It is essentially inactive at neutral pH but becomes active under acidic conditions such as during tumor invasion and in inflammatory processes. Facilitates cell migration associated with metastasis, wound healing and inflammation. Enhances shedding of syndecans, and increases endothelial invasion and angiogenesis in myelomas. Acts as a procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Increases cell adhesion to the extracellular matrix (ECM), independent of its enzymatic activity. Induces AKT1/PKB phosphorylation via lipid rafts increasing cell mobility and invasion. Heparin increases this AKT1/PKB activation. Regulates osteogenesis. Enhances angiogenesis through up-regulation of SRC-mediated activation of VEGF. Implicated in hair follicle inner root sheath differentiation and hair homeostasis.
Post-translational modifications
Proteolytically processed. The cleavage of the 65 kDa form leads to the generation of a linker peptide, and 8 kDa and 50 kDa products. The active form, the 8/50 kDa heterodimer, is resistant to degradation. Complete removal of the linker peptide appears to be a prerequisite to the complete activation of the enzyme.
N-glycosylated. Glycosylation of the 50 kDa subunit appears to be essential for its solubility.
Sequence Similarities
Belongs to the glycosyl hydrolase 79 family.
Tissue Specificity
Highly expressed in placenta and spleen and weakly expressed in lymph node, thymus, peripheral blood leukocytes, bone marrow, endothelial cells, fetal liver and tumor tissues. Also expressed in hair follicles, specifically in both Henle's and Huxley's layers of inner the root sheath (IRS) at anagen phase.
Cellular localization
- Lysosome membrane
- Peripheral membrane protein
- Secreted
- Nucleus
- Proheparanase is secreted via vesicles of the Golgi. Interacts with cell membrane heparan sulfate proteoglycans (HSPGs). Endocytosed and accumulates in endosomes. Transferred to lysosomes where it is proteolytically cleaved to produce the active enzyme. Under certain stimuli, transferred to the cell surface. Associates with lipid rafts. Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates in perinuclear lysosomal vesicles. Heparin retains proheparanase in the extracellular medium (By similarity).
Alternative names
HEP, HPA, HPA1, HPR1, HPSE1, HSE1, HPSE, Heparanase, Endo-glucoronidase, Heparanase-1, Hpa1