Anti-HYAL1 monoclonal antibody, clone FQS6653

Hyaluronan ( HA) is a glycosaminoglycan that associates with various molecules to assemble a specific HA-rich extracellular matrix. Low and intermediate-molecular-weight HA induces cytokines, chemokines, and other mediators of inflammation and extracellular matrix (ECM) degradation. Hyaluronidases are a group of enzymes that degrade HA. As a model of patients with allergic diseases, we used egg albumin to induce high levels of IgE in rats and examined changes in the expression of hyaluronidase genes (Hyal1 and Hyal2) using reverse transcription-polymerase chain reaction (RT-PCR). The expression of Hyal2 was not affected by the overproduction of IgE induced with egg albumin, whereas the expression of the Hyal1 gene was suppressed. High-molecular-weight HA might be degraded by Hyal2 into intermediate-molecular-weight HA, which can trigger inflammation.

A highly sensitive and selective fluorescence strategy for hyaluronidase assay was developed by coupling silicon nanoparticles (SiNPs) as fluorescence indicators with hyaluronic-acid-functionalized gold nanoparticles (HA-AuNPs) as quenchers. With the formation of a core-shell HA-AuNPs@SiNPs nanoprobe by self-assembly, the fluorescence of SiNPs could be quenched by HA-AuNPs through fluorescence resonance energy transfer (FRET). The addition of hyaluronidase leads to cleavage of HA into small fragments, and SiNPs are released. As a result, an immediately fluorescent recovery appears when HAase is introduced. The proposed fluorescence method showed a linear response ranged for HAase from 0.01 to 10 U/mL, and a detection limit of 0.004 U/mL (S/N = 3) was obtained. Furthermore, it can be employed as an enzyme activatable nanoprobe for cell imaging applied in diagnostic and related biological studies.