Anti-HYAL3 antibody

Supplementary info

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

Activity summary

HYAL3 also known as hyaluronoglucosaminidase 3 functions mechanically as an enzyme that catalyzes the degradation of hyaluronan. This protein helps break down hyaluronic acid by cleaving its glycosidic bonds. HYAL3 is expressed in human tissues like lungs liver placenta and skeletal muscle. Its molecular mass is approximately 55 kDa. Researchers recognize HYAL3 as part of a family of hyaluronidase enzymes that play a significant role in maintaining the extracellular matrix.

Biological function summary

Hyaluronoglucosaminidase 3 influences the turnover of hyaluronan in the extracellular environment. Although scientists have not fully clarified its specific biological role due to its relatively weak catalytic activity compared to other hyaluronidases HYAL3 contributes to cellular processes like proliferation differentiation and migration. It participates in a complex with other hyaluronidases such as HYAL1 and HYAL2 which also process hyaluronan and hold a more direct enzymatic role in hyaluronan metabolism.

Pathways

The enzyme hyaluronoglucosaminidase 3 engages in the extracellular matrix (ECM) remodeling pathway. This pathway influences tissue architecture during development and repair. HYAL3 along with hyaluronidases like HYAL1 and HYAL2 regulates hyaluronic acid balance as it affects ECM stability and cell movement. It indirectly supports processes within the Wnt signaling pathway due to its modulatory effects on the ECM further linking it with cellular proliferation and migration.

Associated diseases and disorders

Studies show that HYAL3 may connect to cancer progression and osteoarthritis. In cancer altered expression of HYAL3 and its related hyaluronidase proteins like HYAL2 may facilitate tumor growth and invasion through ECM remodeling. In osteoarthritis HYAL3's influence on hyaluronan degradation could alter joint structure and function potentially disrupting normal joint movements. These associations with various proteins in disease contexts suggest the importance of HYAL3 in pathophysiological conditions.