HPSE Protein, Rat (His-Myc)

HPSE Protein functions as an endoglycosidase, playing a crucial role in the cleavage of heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans. This enzymatic activity contributes to extracellular matrix (ECM) degradation and remodeling, selectively cleaving linkages within glucuronic acid units and N-sulfo glucosamine units carrying specific sulfation patterns. While predominantly inactive at neutral pH, HPSE becomes active under acidic conditions, such as during tumor invasion and inflammatory processes. This protein is implicated in various cellular processes, including facilitating cell migration associated with metastasis, wound healing, and inflammation. It enhances shedding of syndecans, promotes endothelial invasion and angiogenesis in myelomas, and acts as a procoagulant by increasing the generation of activation factor X in the presence of tissue factor and activation factor VII. Notably, HPSE also plays a role in cell adhesion to the ECM, independent of its enzymatic activity, and induces AKT1/PKB phosphorylation, thereby increasing cell mobility and invasion. Additionally, HPSE is involved in the regulation of osteogenesis, promotes angiogenesis through up-regulation of SRC-mediated activation of VEGF, and is implicated in hair follicle inner root sheath differentiation and hair homeostasis.