Recombinant Human HYAL2 protein (GST tag N-Terminus)

補足情報

This supplementary information is collated from multiple sources and compiled automatically.

HYAL2 also known as hyaluronoglucosaminidase 2 is an enzyme that helps break down hyaluronic acid a large polysaccharide present in the extracellular matrix. With a molecular mass of about 60 kDa HYAL2 plays an important mechanical role in the catabolism of hyaluronic acid by cleaving it into smaller fragments. HYAL2 is mainly expressed in tissue such as heart kidney and spleen exhibiting various physiological functions across different organisms.

Biological function summary

Hyaluronoglucosaminidase 2 contributes to the degradation of hyaluronic acid by acting at the cell surface. It operates as part of a complex with CD44 a cell surface receptor involved in cell adhesion and signaling. This interaction allows HYAL2 to localize hyaluronic acid degradation to the cell membrane which influences cellular responses like migration and proliferation. By controlling the size of hyaluronic acid fragments HYAL2 modulates immune responses and tissue remodeling.

Pathways

Several essential processes involve hyaluronoglucosaminidase 2 including the hyaluronan metabolic pathway and the extracellular matrix remodeling pathways. In the hyaluronan metabolic pathway HYAL2 works alongside related enzymes such as HYAL1 to ensure the breakdown and turnover of hyaluronic acid. The regulated degradation of hyaluronic acid by these enzymes is necessary for proper cellular homeostasis and impacts cellular processes such as wound healing and angiogenesis.

Research links hyaluronoglucosaminidase 2 to conditions like cancer and pulmonary hypertension. It relates to cancer because HYAL2's role in hyaluronic acid catabolism can influence tumor progression and metastasis. For pulmonary hypertension alterations in hyaluronic acid levels can affect vascular architecture and function. Additionally interactions with proteins such as CD44 and HYAL1 suggest potential pathways through which HYAL2 could contribute to these diseases influencing therapeutic strategies.