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• W97100671 abstract "Chemokines are low molecular weight cytokines that induce extravasation, chemotaxis, and activation of a wide variety of leukocytes. Members of the different chemokine families are defined by the orientation of specific critical cysteine residues, and are designated as C-X-C (e.g. interleukin-8), C-C (e.g. regulated upon activation normally T cell expressed and secreted, RANTES), or C (lymphotactin). All chemokines bind to members of a G-protein coupled serpentine receptor superfamily that span the leukocyte cell surface membrane seven times and mediate the biological activities of the individual ligands. Most chemokines possess two major binding surfaces: a high affinity site responsible for specific ligand/receptor interactions and a lower affinity site, also called the heparin-binding or glycosaminoglycan-binding domain, believed to be responsible for the establishment and presentation of chemokine gradients on the surface of endothelial cells and within the extracellular matrix. Although chemokines are clearly beneficial in wound healing, hemopoiesis, and the clearance of infectious organisms, the continued expression of chemokines is associated with chronic inflammation. Therefore, this class of cytokines are attractive targets for the creation of antagonists that abrogate one or more chemokine functions. It is envisioned that such antagonists could serve as a new class of anti-inflammatory drugs. In this commentary, we will discuss two different but related strategies for antagonizing chemokine-induced functions, namely, disruption of the low and high affinity binding sites." @default.
• W97100671 created "2016-06-24" @default.
• W97100671 creator A5035200799 @default.
• W97100671 creator A5059808129 @default.
• W97100671 date "1997-12-01" @default.
• W97100671 modified "2023-10-17" @default.
• W97100671 title "New Strategies for Chemokine Inhibition and Modulation" @default.
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• W97100671 doi "https://doi.org/10.1016/s0006-2952(97)00182-2" @default.
• W97100671 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9393669" @default.

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