| 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
(IF:3.665[JCR-2018],3.845[5-Year]) |
| 2006
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| Volume | 91Issue:1Pages:352-363 |
| ISSN | 0006-3495
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| 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
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| DOI | 10.1529/biophysj.106.082909
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| Indexed By | SCI
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| Language | 英语
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| WOS ID | WOS:000238288200035
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| WOS Keyword | SELECTIN GLYCOPROTEIN LIGAND-1
; CELL-ADHESION
; P-SELECTIN
; CONCURRENT BINDING
; KINETIC RATES
; RECEPTOR
; AFFINITY
; IDENTIFICATION
; ERYTHROCYTES
; PEPTIDE
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| WOS Research Area | Biophysics
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| WOS Subject | Biophysics
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| Citation statistics |
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| Document Type | 期刊论文
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| Identifier | http://dspace.imech.ac.cn/handle/311007/17673
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| Collection | 力学所知识产出(1956-2008)
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| 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.
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| 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.
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| MLA |
龙勉,et al."Probabilistic Modeling of Rosette Formation".Biophysical Journal 91.1(2006):352-363.
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