Mechanisms regulating the binding activity of CD44 to hyaluronic acid.

@article{Liu1998MechanismsRT,
  title={Mechanisms regulating the binding activity of CD44 to hyaluronic acid.},
  author={D. Liu and T Liu and R. Li and Man Sun Sy},
  journal={Frontiers in bioscience : a journal and virtual library},
  year={1998},
  volume={3},
  pages={
          d631-6
        }
}
  • D. Liu, T. Liu, +1 author M. Sy
  • Published 1 July 1998
  • Biology, Chemistry
  • Frontiers in bioscience : a journal and virtual library
CD44 is a cell surface glycoprotein present on many cell types. Many CD44 isoforms have been identified. All CD44 isoforms utilize identical transmembrane and cytoplasmic domains. The hematopoietic form of CD44 (CD44H) is the major CD44 protein present on normal human lymphocytes and monocytes. One of the ligands for CD44 is hyaluronic acid (HA), a polymer consisting of repeat units of disaccharide; N-acetyl-D-glucosamine and N-acetyl-D-glucuronic acid. Since HA is present ubiquitously in… 
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Induction of interactions between CD44 and hyaluronic acid by a short exposure of human T cells to diverse pro‐inflammatory mediators
TLDR
The role of inflammatory mediators in regulating the adhesion of T cells from human peripheral blood to immobilized hyaluronan under static or shear stress conditions is studied and it is found that the CD44‐dependent adhesion requires a T‐cell activation of 2–3 hr and is regulated by the cross‐linking of CD3, cytokines and chemokines.
Chapter 5 – The Hyaluronan Receptor: CD44
PKC-induced stiffening of hyaluronan/CD44 linkage; local force measurements on glioma cells.
Recent advances in the regulation of CD44 expression and its role in inflammation and autoimmune diseases.
TLDR
This review will focus on the recent advances in the molecular mechanisms regulating CD44 expression, ligand binding, as well as the contribution of CD44 to the development of inflammation and autoimmune disorders.
Chapter 7 – Signal Transduction Associated with Hyaluronan
Tumor Necrosis Factor-α Induces Functionally Active Hyaluronan-adhesive CD44 by Activating Sialidase through p38 Mitogen-activated Protein Kinase in Lipopolysaccharide-stimulated Human Monocytic Cells*
TLDR
It is shown that LPS-induced CD44-mediated HA (CD44-HA) binding in monocytes is regulated by endogenously produced tumor necrosis factor (TNF)-α and IL-10, and that lysosomal sialidase activation may be required for the acquisition of the HA-binding form of CD44 in L PS- and TNF-α-stimulated monocytic cells.
Hyaluronan-Binding T Regulatory Cells in Peripheral Blood of Breast Cancer Patients
TLDR
It was shown that the majority of peripheral blood Tregs were able to adhere to immobilized hyaluronan, and these cells exerted superior suppressor activity, suggesting a key role in regulatory functions of these cells.
Two Novel Functions of Hyaluronidase-2 (Hyal2) Are Formation of the Glycocalyx and Control of CD44-ERM Interactions*
TLDR
It is surmise that Hyal2, through direct interactions with CD44 and possibly some pericellular hyaluronidase activity requiring acidic foci, suppresses the formation or the stability of the glycocalyx, modulates ERM-related cytoskeletal interactions, and diminishes cell motility.
The High and Low Molecular Weight Forms of Hyaluronan Have Distinct Effects on CD44 Clustering*
TLDR
The results suggest that native HA binding to CD44 selectively induces CD44 clustering, which could be inhibited by oHA, and it is demonstrated that HA regulates cell adhesion in a manner specifically dependent on its size.
Cancer Growth and Metastasis
TLDR
A family of chimeric proteins in which the extracellular ligand-binding domain of the hyaluronan receptor CD44 is fused in-frame to the cytoplasmic “death domain” of the pro-apoptotic protein Fas is described, helping validate a broadly applicable gene therapy approach inWhich the presence of particular multivalent ligands within the tumor microenvironment can be exploited for therapeutic gain.
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References

SHOWING 1-10 OF 65 REFERENCES
Defective phosphorylation and hyaluronate binding of CD44 with point mutations in the cytoplasmic domain
TLDR
It is demonstrated that serines 325 and 327 within the cytoplasmic domain of CD44 are required for the constitutive phosphorylation ofCD44 in T cells, and that cells expressing mutated CD44 containing a serine to glycine substitution at position 325 are defective in HA binding, CD44-mediated adhesion of T cells to smooth muscle cells, as well as ligand-induced receptor modulation.
CD44 and its interaction with extracellular matrix.
Requirements for hyaluronic acid binding by CD44: a role for the cytoplasmic domain and activation by antibody
TLDR
The CD44-negative T lymphoma AKR1 (CD44.2 genotype) was transfected with a CD44.1 cDNA, indicating that the cytoplasmic domain of CD44 is necessary for binding of HA from solution but is not required for binding to immobilized HA, although it may contribute to adhesion following ligand recognition.
Role of CD44 cytoplasmic domain in hyaluronan binding
TLDR
Results suggest that changes in the distribution of CD44 on the cell surface, induced by molecular interactions either from within the cell or from outside, may regulate its role as a receptor, and conclude that dimerization ofCD44 abrogates the requirement for the cytoplasmic domain.
Variant cell lines selected for alterations in the function of the hyaluronan receptor CD44 show differences in glycosylation
TLDR
The results suggest that two genetic events must occur to obtain an active CD44-HA receptor from an inactive receptor, and indicate that carbohydrate side chains of CD44 and/or other molecules on the cell surface that interact with CD44 are potentially involved in regulating the HA-binding function ofCD44 on thecell surface.
Glycosylation of CD44 negatively regulates its recognition of hyaluronan
TLDR
Differential glycosylation of this molecule is sufficient to influence its recognition function, and the ligand-binding ability of a purified CD44-immunoglobulin fusion protein dramatically increased after neuraminidase treatment.
Glycosylation of CD44 is implicated in CD44-mediated cell adhesion to hyaluronan
TLDR
Observations indicate that changes in glycosylation of CD44 can have profound effects on its interaction with hyaluronic acid and suggest that gly cosylation may provide an important regulatory mechanism ofCD44 function.
CD44 is the principal cell surface receptor for hyaluronate
A Novel Ligand for CD44 Is Serglycin, a Hematopoietic Cell Lineage-specific Proteoglycan
TLDR
It is concluded that the serglycin secreted from secretory granules of hematopoietic cells is a novel ligand for CD44, and could regulate lymphoid cell adherence and activation.
Regulation of human CD44H and CD44E isoform binding to hyaluronan by phorbol myristate acetate and anti-CD44 monoclonal and polyclonal antibodies.
TLDR
Data underscore the importance of the CD44 cytoplasmic domain in the function of the extracellular portion of CD44H, and demonstrate a role for ligation of human CD44 isoforms at multiple distinct sites in regulation of expression ofCD44 binding to HA.
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