Knowledge Management System of Institue of Mechanics, CAS
| Probabilistic Modeling of Rosette Formation | |
Long M(龙勉) ; Chen J(陈娟); Jiang N(姜宁); Selvaraj P; McEver RP; Zhu C(朱承); Long, M (reprint author), Chinese Acad Sci, Inst Mech, Natl Micrograv Lab, Beijing 100080, Peoples R China.
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| Source Publication | Biophysical Journal
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| 2006 | |
| Volume | 91Issue:1Pages:352-363 |
| ISSN | 0006-3495 |
| Other Abstract | 英文摘要: Rosetting, or forming a cell aggregate between a single target nucleated cell and a number of red blood cells (RBCs), is a simple assay for cell adhesion-mediated by specific receptor-ligand interaction. For example, rosette formation between sheep RBC and human lymphocytes has been used to differentiate T cells from B cells. Rosetting assay is commonly used to determine the interaction of Fc gamma-receptors (Fc gamma R) expressed on inflammatory cells and IgG-coated on RBCs. Despite its wide use in measuring cell adhesion, the biophysical parameters of rosette formation have not been well characterized. Here we developed a probabilistic model to describe the distribution of rosette sizes, which is Poissonian. The average rosette size is predicted to be proportional to the apparent two-dimensional binding affinity of the interacting receptor-ligand pair and their site densities. The model has been supported by experiments of rosettes mediated by four molecular interactions: Fc gamma RIII interacting with IgG, T cell receptor and coreceptor CD8 interacting with antigen peptide presented by major histocompatibility molecule, P-selectin interacting with P-selectin glycoprotein ligand 1 (PSGL-1), and L-selectin interacting with PSGL-1. The latter two are structurally similar and are different from the former two. Fitting the model to data enabled us to evaluate the apparent effective two-dimensional binding affinity of the interacting molecular pairs: 7.19x10(-5) mu m(4) for Fc gamma RIII-IgG interaction, 4.66x10(-3) mu m(4) for P-selectin-PSGL-1 interaction, and 0.94x10(-3) mu m(4) for L-selectin-PSGL-1 interaction. These results elucidate the biophysical mechanism of rosette formation and enable it to become a semiquantitative assay that relates the rosette size to the effective affinity for receptor-ligand binding. |
| Subject Area | 力学 |
| DOI | 10.1529/biophysj.106.082909 |
| Indexed By | SCI |
| Language | 英语 |
| WOS ID | WOS:000238288200035 |
| WOS Keyword | SELECTIN GLYCOPROTEIN LIGAND-1 ; CELL-ADHESION ; P-SELECTIN ; CONCURRENT BINDING ; KINETIC RATES ; RECEPTOR ; AFFINITY ; IDENTIFICATION ; ERYTHROCYTES ; PEPTIDE |
| WOS Research Area | Biophysics |
| WOS Subject | Biophysics |
| Citation statistics | |
| Document Type | 期刊论文 |
| Identifier | http://dspace.imech.ac.cn/handle/311007/17673 |
| Collection | 力学所知识产出(1956-2008) |
| Corresponding Author | Long, M (reprint author), Chinese Acad Sci, Inst Mech, Natl Micrograv Lab, Beijing 100080, Peoples R China. |
| Recommended Citation GB/T 7714 | Long M,Chen J,Jiang N,et al. Probabilistic Modeling of Rosette Formation[J]. Biophysical Journal,2006,91,1,:352-363. |
| APA | 龙勉.,陈娟.,姜宁.,Selvaraj P.,McEver RP.,...&Long, M .(2006).Probabilistic Modeling of Rosette Formation.Biophysical Journal,91(1),352-363. |
| MLA | 龙勉,et al."Probabilistic Modeling of Rosette Formation".Biophysical Journal 91.1(2006):352-363. |
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