Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin.

Tyrosine replacement in P-selectin glycoprotein ligand-1 affects distinct kinetic and mechanical properties of bonds with P- and L-selectin.
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P-选择素糖蛋白配体-1 中的酪氨酸取代会影响与 P-和 L-选择素键的独特动力学和机械特性。

DOI:
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发表时间:
1999
影响因子:
11.1
通讯作者:
R. McEver
R. McEver
中科院分区:
综合性期刊1区
文献类型:
--
作者:
V. Ramachandran;M. U. Nollert;H. Qiu;W. Liu;R. Cummings;C. Zhu;R. McEver

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选择素是一种粘附分子,它能使白细胞在血管壁上聚集和滚动。滚动需要选择配体键的快速形成和断裂,选择配体键必须具有机械强度以抵抗剪切流中施加的力的过早解离。P-选择素和l -选择素结合到P-选择素糖蛋白配体1 (PSGL-1)的n端区域,这是白细胞上的一种粘蛋白。为了确定PSGL-1上的决定因素,这些决定因素有助于与选择素结合的动力学和力学特性,我们比较了表达P-选择素或l -选择素的转染前b细胞在表达野生型PSGL-1或目标n端残基取代的PSGL-1构建物的转染细胞单层上的旋转。滚动通过P-或l -选择素需要在PSGL-1上的特定位置(必需o -聚糖的附着位点)上一个Thr或Ser,但只需要附近三个Tyr残基中的一个,这些残基是形成Tyr- so(3)的位点。在野生型PSGL-1和仅含一个Tyr的三种PSGL-1构建体上,通过P-或l -选择素的粘附强度和细胞数量相似。然而,细胞在单tyr形式的PSGL-1上滚动得更加不规则。分析瞬时系索对PSGL-1极限密度的影响,发现l -选择素在所有剪切条件下都比野生型PSGL-1更快地从单个tyr解离。与此形成鲜明对比的是,p -选择素在高剪切下比野生型PSGL-1更快地从单个tyr中解离,而在低剪切下则不然。因此,PSGL-1中的酪氨酸替换会影响与P-选择素和l -选择素键的不同动力学和力学性质。
Selectins are adhesion molecules that initiate tethering and rolling of leukocytes on the vessel wall. Rolling requires rapid formation and breakage of selectin-ligand bonds that must have mechanical strength to resist premature dissociation by the forces applied in shear flow. P- and L-selectin bind to the N-terminal region of P-selectin glycoprotein ligand-1 (PSGL-1), a mucin on leukocytes. To define determinants on PSGL-1 that contribute to the kinetic and mechanical properties of bonds with selectins, we compared rolling of transfected preB cells expressing P- or L-selectin on transfected cell monolayers expressing wild-type PSGL-1 or PSGL-1 constructs with substitutions in targeted N-terminal residues. Rolling through P- or L-selectin required a Thr or Ser at a specific position on PSGL-1, the attachment site for an essential O-glycan, but required only one of three nearby Tyr residues, which are sites for Tyr-SO(3) formation. The adhesive strengths and numbers of cells rolling through P- or L-selectin were similar on wild-type PSGL-1 and on each of the three PSGL-1 constructs containing only a single Tyr. However, the cells rolled more irregularly on the single-Tyr forms of PSGL-1. Analysis of the lifetimes of transient tethers on limiting densities of PSGL-1 revealed that L-selectin dissociated faster from single-Tyr than wild-type PSGL-1 at all shears examined. In sharp contrast, P-selectin dissociated faster from single-Tyr than wild-type PSGL-1 at higher shear but not at lower shear. Thus, tyrosine replacements in PSGL-1 affect distinct kinetic and mechanical properties of bonds with P- and L-selectin.
DOI: --
发表时间: 1994-06
期刊: The Journal of biological chemistry
影响因子: --
作者:
S. Natsuka;K. M. Gersten;K. Zenita;R. Kannagi;J. Lowe
通讯作者: S. Natsuka;K. M. Gersten;K. Zenita;R. Kannagi;J. Lowe
DOI: 10.1073/pnas.95.12.6797
发表时间: 1998-06-09
影响因子: 11.1
作者:
Shao, JY;Ting-Beall, HP;Hochmuth, RM
通讯作者: Hochmuth, RM
DOI: 10.1126/science.2551036
发表时间: 1989-09-15
期刊: SCIENCE
影响因子: 56.9
作者:
KISHIMOTO, TK;JUTILA, MA;BUTCHER, EC
通讯作者: BUTCHER, EC
DOI: 10.1073/pnas.95.20.11631
发表时间: 1998-09-29
影响因子: 11.1
作者:
Alon, R;Chen, SQ;Springer, TA
通讯作者: Springer, TA