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Distinct binding kinetics of E-, P- and L-selectins to CD44

文献类型：期刊论文

作者Li, Linda2,3,4; Ding, Qihan1,2,3; Zhou, Jin1,2,3; Wu, Yi1,2,3; Zhang, Mingkun1,2,3; Guo, Xingming4; Long, Mian1,2,3; Lu, Shouqin1,2,3; Long M(龙勉); Lv SQ(吕守芹)
刊名FEBS JOURNAL
出版日期2021-12-13
页码18
ISSN号1742-464X
关键词binding epitope binding kinetics CD44 selectin
DOI10.1111/febs.16303
通讯作者Guo, Xingming(guoxm@cqu.edu.cn) ; Long, Mian(mlong@imech.ac.cn) ; Lu, Shouqin(lsq@imech.ac.cn)
英文摘要Molecular-level selectin-cluster of differentiation 44 (CD44) interactions are far from clear because of the complexity and diversity of CD44 glycosylation and isoforms expressed on various types of cells. By combining experimental measurements and simulation predictions, the binding kinetics of three selectin members to the recombinant CD44 were quantified and the corresponding microstructural mechanisms were explored, respectively. Experimental results showed that the E-selectin-CD44 interactions mainly mediated the firm adhesion of microbeads under shear flow with the strongest rupture force. P- and L-selectins had similar interaction strength but different association and dissociation rates by mediating stable rolling and transient adhesions of microbeads, respectively. Molecular docking and molecular dynamics (MD) simulations predicted that the binding epitopes of CD44 to selectins are all located at the side face of each selectin, although the interfaces denoted as the hinge region are between lectin and epidermal growth factor domains of E-selectin, Lectin domain side of P-selectin and epidermal growth factor domain side of L-selectin, respectively. The lowest binding free energy, the largest rupture force and the longest lifetime for E-selectin, as well as the comparable values for P- and L-selectins, demonstrated in both equilibration and steered MD simulations, supported the above experimental results. These results offer basic data for understanding the functional differences of selectin-CD44 interactions.
WOS关键词MOLECULAR-DYNAMICS ; CELL-ADHESION ; LIGAND ; RECEPTOR ; PSGL-1 ; DISSOCIATION ; DOMAIN ; FIBRIN
资助项目National Key Research and Development Program of China[2016YFA0501601] ; National Natural Science Foundation of China[11972042] ; Frontier Science Key Project of Chinese Science Academy[QYZDJ-SSW-JSC018] ; Strategic Priority Research Program of Chinese Academy of Sciences[XDB22040101]
WOS研究方向Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:000729568500001
资助机构National Key Research and Development Program of China ; National Natural Science Foundation of China ; Frontier Science Key Project of Chinese Science Academy ; Strategic Priority Research Program of Chinese Academy of Sciences
源URL[http://dspace.imech.ac.cn/handle/311007/87966]  
专题力学研究所_国家微重力实验室
通讯作者Guo, Xingming; Long, Mian; Lu, Shouqin
作者单位1.Univ Chinese Acad Sci, Sch Engn Sci, Beijing, Peoples R China
2.Chinese Acad Sci, CAS Ctr Excellence Complex Syst Mech, Beijing 100190, Peoples R China
3.Chinese Acad Sci, Inst Mech, Ctr Biomech & Bioengn, Key Lab Micrograv,Natl Micrograv Lab,Beijing Key, Beijing 100190, Peoples R China
4.Chongqing Univ, Coll Bioengn, Minist Educ, Key Lab Biorheol Sci & Technol, Chongqing 400044, Peoples R China
推荐引用方式
GB/T 7714		 Li, Linda,Ding, Qihan,Zhou, Jin,et al. Distinct binding kinetics of E-, P- and L-selectins to CD44[J]. FEBS JOURNAL,2021:18.
APA Li, Linda.,Ding, Qihan.,Zhou, Jin.,Wu, Yi.,Zhang, Mingkun.,...&Long M.(2021).Distinct binding kinetics of E-, P- and L-selectins to CD44.FEBS JOURNAL,18.
MLA Li, Linda,et al."Distinct binding kinetics of E-, P- and L-selectins to CD44".FEBS JOURNAL (2021):18.

入库方式： OAI收割

来源：力学研究所

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