ArticleThe Journal of biological chemistry2019
Hyaluronidase-4 is produced by mast cells and can cleave serglycin chondroitin sulfate chains into lower molecular weight forms.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Serglycin Across the Disease Spectrum: A Multifunctional Proteoglycan in Inflammation and Cancer.Current issues in molecular biology · 2026Article
- Review
- Glycosaminoglycans, Instructive Biomolecules That Regulate Cellular Activity and Synaptic Neuronal Control of Specific Tissue Functional Properties.International journal of molecular sciences · 2025Review
- Structure and functional impact of glycosaminoglycan modification of HSulf-2 endosulfatase revealed by atomic force microscopy and mass spectrometry.Scientific reports · 2023Article
- Arthritis and Duchenne muscular dystrophy: the role of chondroitin sulfate and its associated proteoglycans in disease pathology and as a diagnostic marker.American journal of physiology. Cell physiology · 2023Review
- Characterization of Hyaluronidase 4 Involved in the Catabolism of Chondroitin Sulfate.Molecules (Basel, Switzerland) · 2022Article
- Identification of key apoptosis-related genes and immune infiltration in the pathogenesis of psoriasis.Hereditas · 2022Article
- Proteoglycans and their functions in esophageal squamous cell carcinoma.World journal of clinical oncology · 2021Review
- New Insights Into Human Hyaluronidase 4/Chondroitin Sulphate Hydrolase.Frontiers in cell and developmental biology · 2021Review
- Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mast cells represent a heterogeneous cell population that is well-known for the production of heparin and the release of histamine upon activation. Serglycin is a proteoglycan that within mast cell α-granules is predominantly decorated with the glycosaminoglycans heparin or chondroitin sulfate (CS) and has a known role in granule homeostasis. Heparanase is a heparin-degrading enzyme, is present within the α-granules, and contributes to granule homeostasis, but an equivalent CS-degrading enzyme has not been reported previously. In this study, using several approaches, including epitope-specific antibodies, immunohistochemistry, and EM analyses, we demonstrate that human HMC-1 mast cells produce the CS-degrading enzymes hyaluronidase-1 (HYAL1) and HYAL4. We observed that treating the two model CS proteoglycans aggrecan and serglycin with HYAL1 and HYAL4
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