Hyaluronan as an Immune Regulator in Human Diseases
By P. Noble, Jiurong Liang, D. Jiang. Physiological Reviews, 2011
1,034 citations recorded by the source corpus.
Accumulation and turnover of extracellular matrix components are the hallmarks of tissue injury. Fragmented hyaluronan stimulates the expression of inflammatory genes by a variety of immune cells at the injury site. Hyaluronan binds to a number of cell surface proteins on a variety of cell types. Hyaluronan fragments signal through both Toll-like receptor (TLR) 4 and TLR2 as well as CD44 to stimulate inflammatory genes in inflammatory cells. Hyaluronan is also present on the cell surface of epithelial cells and provides protection against tissue damage by interacting with TLR2 and TLR4 on these parenchymal cells. Hyaluronan and hyaluronan-binding proteins regulate inflammation, tissue injury and repair through regulating inflammatory cell recruitment, release of inflammatory cytokines, and stem cell migration. This review focuses on the role of hyaluronan as an immune regulator in human diseases.
Subfields: Cell Biology, Immunology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/ddcf30b593b7606c91f92ae89fbcaccbd2f87e89
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Citations in the corpus
- The ominous triad of adipose tissue dysfunction: inflammation, fibrosis, and impaired angiogenesis. (2017, neutral): “HA is also a potent inducer of the innate immune response through binding and activation of immune cell TLR2 and -4 (51).”
- Hyaluronic Acid in the Third Millennium (2018, background): “According to the first theory, LMW hyaluronan acts as an agonist for TLR2 and TLR4, thus provoking an inflammatory reaction [51,114].”
- Biological roles of glycans (2016, background): “Innate immune cells also recognize glycans released from tissue damage in vertebrates such as hyaluronan fragments (467, 914, 915) and some matrix proteoglycans”
- An Introduction to Proteoglycans and Their Localization (2012, background): “Hyaluronan is now also considered a regulator of immune function (Jiang et al. 2011), interacting with tolllike receptors, as can biglycan.”