Cited by 639Proteoglycans and glycosaminoglycans researchWound Healing and TreatmentsAdvanced Glycation End Products research

Glycosaminoglycans and their proteoglycans: host‐associated molecular patterns for initiation and modulation of inflammation

Taylor, Kristen R., Gallo, Richard L.·2006·The FASEB Journal

Abstract

Glycosaminoglycans, linear carbohydrates such as heparan sulfate and hyaluronan, participate in a variety of biological processes including cell‐matrix interactions and activation of chemokines, enzymes and growth factors. This review will discuss progress in immunology and the science of wound repair that has revealed the importance of glycosaminoglycans, and their proteoglycans, in the inflammatory process. Heparan sulfate enables growth factor function and modifies enzyme/inhibitor functions, such as antithrombin III and heparin cofactor II. Heparan sulfate also interacts with cytokines/chemokines and participates in leukocyte selectin binding to promote the recruitment of leukocytes. Chondroitin sulfate/ dermatan sulfate regulates growth factor activity and is an alternate modulator of heparin cofactor II. In addition, dermatan sulfate induces ICAM‐1 expression on endothelial cells and also recruits leukocytes via selectin interactions. Hyaluronan alternatively participates in leukocyte recruitment via interaction with CD44, while activating various inflammatory cells, such as macrophages, through CD44‐dependent signaling. Hyaluronan also signals through Toll‐like receptor 4 to induce dendritic cell maturation and promote cytokine release by dendritic cells and endothelial cells. Taken together, the field of glycosaminoglycan biology provides new clues and explanations of the process of inflammation and suggests new therapeutic approaches to human disease.—Taylor, K. R., Gallo, R. L. Glycosaminoglycans and their proteoglycans: host‐associated molecular patterns for initiation and modulation of inflammation. FASEB J. 20, 9–22 (2006)

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Crossref · 10.1096/fj.05-4682rev

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  • These integrins were also co-expressed with members of the glycosaminoglycan and proteoglycan family (SDCBP, LUM), laminin beta 1 (LAMB1), and with several proteases and other enzymes involved in ECM remodeling and cell-cell or cell-matrix interactions.

    “They were also co-expressed with members of the glycosaminoglycan and proteoglycan family (syndecan binding protein (SDCBP), lumican (LUM)), known to play an important role in the initiation of inflammatory phenomena, as well as in the recruitment, rolling, and subsequent extravasation of lymphocytes [24], the laminin beta 1 (LAMB1), and with several proteases and other enzymes involved in ECM”

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Authors
Taylor, K. R., & Gallo, R. L.
Affiliations
University of California San Diego (US)
Venue
The FASEB Journal
Publisher
Wiley
Published
2006-01
Volume
20
Issue
1
Pages
9-22
ISSN
  • 0892-6638 (ISSN-L)
  • 1530-6860
OpenAlex
W1972420702
Cited by
639
References
130
Citations by year
2026: 16 · 2025: 16 · 2024: 14 · 2023: 15 · 2022: 20 · 2021: 25 · 2020: 35 · 2019: 29 · 2018: 29 · 2017: 34 · 2016: 45 · 2015: 34 · 2014: 41 · 2013: 39 · 2012: 39
FWCI
3.19
Type
journal article
Language
en
Open access
closed
Locations
  • The FASEB Journal (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
  • Health Sciences › Medicine › Rehabilitation › Wound Healing and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
Keywords
glycosaminoglycans, proteoglycans, inflammation, heparan sulfate, hyaluronic acid, chondroitin sulfate, dermatan sulfate, wound healing, leukocyte recruitment, selectins, CD44, ICAM-1, heparin cofactor II, antithrombin III, growth factor activation, TLR4, dendritic cell maturation, macrophages, cytokine production
MeSH terms
Animals, Gene Expression Regulation, Glycosaminoglycans, Inflammation, Proteoglycans

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