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Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function.
Open accessAbstract
Occupancy of integrin receptors induces conformational changes in the receptor, resulting in exposure of novel interactive sites termed ligand-induced binding sites (LIBS). We report here that Fab fragments of certain antibodies against LIBS on integrin alpha IIb beta 3 (platelet glycoprotein IIb-IIIa) block platelet aggregation. Thus, certain LIBS or the regions surrounding them may participate in events required for platelet aggregation. In addition, certain anti-alpha IIb beta 3 LIBS Fab fragments stimulated platelet aggregation. This was due to induction of fg binding to alpha IIb beta 3, apparently by shifting a conformational equilibrium between a "resting" and an "activated" state of alpha IIb beta 3. Some of the activating anti-LIBS Fab fragments also induced high affinity fibronectin binding to alpha IIb beta 3, whereas others did not. Thus, changes in the conformation of this integrin modulate both the specificity and affinity of ligand recognition.
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Citations
Cited by
The final steps of integrin activation: the end game
Shattil, S. J., Kim, C., & Ginsberg, M. H. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2871 · Cited by 1,086
Self-citationElosegui-Artola, A., Oria, R., Chen, Y., Kosmalska, A., Pérez-González, C., Castro, N., Zhu, C., Trepat, X., & Roca-Cusachs, P. (2016) · Nature Cell Biology · doi:10.1038/ncb3336 · Cited by 858
Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
Uversky, V. N., Oldfield, C. J., & Dunker, A. K. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.747 · Cited by 847
The dynamic regulation of integrin adhesiveness
Diamond, M. S., & Springer, T. A. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00111-1 · Cited by 434
Luque, A., Gómez, M., Puzon, W., Takada, Y., Sánchez-Madrid, F., & Cabañas, C. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.19.11067 · Cited by 296
Metadata
- Authors
- Frelinger, A. L., Du, X. P., Plow, E. F., & Ginsberg, M. H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1991-09
- Volume
- 266
- Issue
- 26
- Pages
- 17106-17111
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1656991593
- Cited by
- 348
- References
- 0
- FWCI
- 4.72
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Frelinger, A. L., Du, X. P., Plow, E. F., & Ginsberg, M. H. (1991). Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(19)47346-8
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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