發(fā)布時(shí)間：2018-02-15 12:32

  本文關(guān)鍵詞： 白細(xì)胞整合素LFA- 趨化因子CXCL 親和態(tài)躍遷 受體配體相互作用 細(xì)胞黏附　出處：《醫(yī)用生物力學(xué)》2017年06期 　論文類型：期刊論文

【摘要】：目的探究剪應(yīng)力下趨化因子誘導(dǎo)的白細(xì)胞上整合素LFA-1激活過程。方法采用平行平板流動(dòng)腔系統(tǒng)在10~30 mPa剪應(yīng)力下,觀察分析可溶性及固定趨化因子CXCL12對(duì)Jurkat細(xì)胞在ICAM-1上瞬時(shí)黏附行為的影響,提取特征參數(shù)。結(jié)果 CXCL12僅能介導(dǎo)Jurkat細(xì)胞的短暫栓縛(0.13~0.20 s)。只有固定的CXCL12才能有效激活Jurkat細(xì)胞上LFA-1與ICAM-1鍵合,從而提高栓縛事件的發(fā)生率,并大大延長(zhǎng)細(xì)胞的栓縛時(shí)間(0.8~1.2 s)。激活的LFA-1/ICAM-1解離速率呈現(xiàn)明顯雙態(tài)性:k_1(1.09~1.24 s~(-1)),k_2(0.28~0.7 s~(-1)),剪應(yīng)力主要通過調(diào)節(jié)k_2及k_2對(duì)整個(gè)黏附時(shí)間的貢獻(xiàn)率β來控制細(xì)胞的瞬時(shí)黏附行為。結(jié)論剪應(yīng)力通過G蛋白偶聯(lián)受體與CXCL12的作用可在0.2 s內(nèi)快速激活整合素LFA-1,進(jìn)而調(diào)控白細(xì)胞的黏附過程。研究結(jié)果有助于深化趨化因子-力偶聯(lián)調(diào)控整合素激活機(jī)制的認(rèn)識(shí)。
[Abstract]:Objective to investigate the activation process of integrin LFA-1 on leukocytes induced by chemokines under shear stress. The effects of soluble and immobilized chemokine CXCL12 on transient adhesion of Jurkat cells on ICAM-1 were observed and analyzed. Results CXCL12 could only mediate the transient binding of Jurkat cells 0.13 ~ 0.20 s 路s ~ (-1). Only fixed CXCL12 could effectively activate the binding of LFA-1 and ICAM-1 on Jurkat cells, thus increasing the incidence of binding events. The activated LFA-1/ICAM-1 dissociation rate was significantly bimodal: K11.09 / 1.24 s-1 / L ~ (-1). The shear stress was mainly controlled by adjusting the contribution rate 尾 of k2 and kSn2 to the whole adhesion time. The effect of shear stress on the transient adhesion behavior of the cells was studied by adjusting the effect of K _ 2 and K _ S _ 2 on the transient adhesion behavior of the cells to the whole adhesion time (尾), and to control the transient adhesion behavior of the cells by adjusting the ratio of K _ 2 and K _ S _ 2 contribution to the whole adhesion time. It is suggested that shear stress can rapidly activate integrin LFA-1 and regulate the adhesion process of leukocytes in 0.2 s through the interaction of G protein-coupled receptors with CXCL12. The results of this study are helpful to deepen the understanding of chemokine-coupled regulation mechanism of integrin activation.
【作者單位】： 華南理工大學(xué)生物科學(xué)與工程學(xué)院生物力學(xué)研究所;
【基金】：國(guó)家自然科學(xué)基金項(xiàng)目(11432006,11672109,11272125,31170887)
【分類號(hào)】：R318.01

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