The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Hyaluronan Binding by Cell Surface CD44
Open accessAbstract
CD44 is the primary cell surface receptor for the extracellular matrix glycosaminoglycan hyaluronan. Here we determined the relative avidities of unlabeled hyaluronan preparations for cell surface CD44 by their ability to block the binding of fluorescein-conjugated hyaluronan to a variety of cells. We show that hyaluronan binding at the cell surface is a complex interplay of multivalent binding events affected by the size of the multivalent hyaluronan ligand, the quantity and density of cell surface CD44, and the activation state of CD44 as determined by cell-specific factors and/or treatment with CD44-specific monoclonal antibody (mAb). Using low M r hyaluronan oligomers of defined sizes, we observed monovalent binding between 6 and 18 sugars. At ∼20 to ∼38 sugars, there was an increase in avidity (∼3×), suggesting that divalent binding was occurring. In the presence of the inducing mAb IRAWB14, monovalent binding avidity was similar to that of noninduced CD44, but beginning at ∼20 residues, there was a dramatic and progressive increase in avidity with increasing oligomer size (∼22 < 26 < 30 < 34 < 38 sugars). Kinetic studies of binding and dissociation of fluorescein-conjugated hyaluronan indicated that inducing mAb treatment had little effect on the binding kinetics, but dissociation from the cell surface was greatly delayed by inducing mAb.
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Cites
CD44 and Its Interaction with Extracellular Matrix
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Self-citationRole of Lymphocyte Adhesion Receptors in Transient Interactions and Cell Locomotion
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Identification of hyaluronic acid binding sites in the extracellular domain of CD44
Peach, R., Hollenbaugh, D., Stamenkovic, I., & Aruffo, A. (1993) · The Journal of cell biology · doi:10.1083/jcb.122.1.257 · Cited by 378
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Self-citationKohda, D., Morton, C. J., Parkar, A. A., Hatanaka, H., Inagaki, F. M., Campbell, I. D., & Day, A. J. (1996) · Cell · doi:10.1016/s0092-8674(00)80151-8 · Cited by 309
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Glycosylation of CD44 negatively regulates its recognition of hyaluronan.
Katoh, S., Zheng, Z., Oritani, K., Shimozato, T., & Kincade, P. W. (1995) · The Journal of experimental medicine · doi:10.1084/jem.182.2.419 · Cited by 254
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Self-citationSkelton, T. P., Zeng, C., Nocks, A., & Stamenkovic, I. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.2.431 · Cited by 209
A versatile synthetic dimerizer for the regulation of protein–protein interactions
Amara, J. F., Clackson, T., Rivera, V. M., Guo, T., Keenan, T., Natesan, S., Pollock, R., Yang, W., Courage, N. L., Holt, D. A., et al. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.20.10618 · Cited by 206
Cited by
Hyaluronan: from extracellular glue to pericellular cue
Toole, B. P. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1391 · Cited by 2,125
Misra, S., Hascall, V. C., Markwald, R. R., & Ghatak, S. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00201 · Cited by 830
Self-citationHyaluronan-binding Proteins: Tying Up the Giant
Day, A. J., & Prestwich, G. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r100036200 · Cited by 567
Hyaluronan, a Crucial Regulator of Inflammation
Petrey, A. C., & de la Motte, C. A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00101 · Cited by 514
Hyaluronan–CD44 interactions as potential targets for cancer therapy
Misra, S., Heldin, P., Hascall, V. C., Karamanos, N. K., Skandalis, S. S., Markwald, R. R., & Ghatak, S. (2011) · The FEBS Journal · doi:10.1111/j.1742-4658.2011.08071.x · Cited by 494
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Metadata
- Authors
- Lesley, J., Hascall, V. C., Tammi, M., & Hyman, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-09
- Volume
- 275
- Issue
- 35
- Pages
- 26967-26975
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W4242063371
- Cited by
- 389
- References
- 30
- FWCI
- 4.06
- Type
- journal article
- Language
- en
- Open access
- hybrid
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