Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers.
Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers.
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转谷氨酰胺酶介导的内皮细胞单层对纤连蛋白的加工。
DOI：
10.1021/bi00175a024
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Barsigian,C
中科院分区：
文献类型：
--
作者：
Martinez,J;Chalupowicz,DG;Roush,RK;Sheth,A;Barsigian,C
摘要：我们研究了[125I]纤维连接蛋白与人脐静脉内皮细胞的相互作用。内皮细胞单层交联[125I]纤维连接蛋白已预吸附到明胶涂层的盘子。底物固定的[125I]纤维连接蛋白的交联是由细胞相关组织转谷氨酰胺酶介导的，在内皮细胞播种后的前30分钟内发生得更快，但在细胞完全扩散后也持续了几个小时。[125I]纤维连接蛋白的加工与内皮细胞的基底外侧表面有关，当[125I]纤维连接蛋白呈现在融合单层的顶端表面时，不会发生交联。转谷氨酰胺酶活性对于HUVEC在纤维连接蛋白/明胶基质上的附着和扩散不是必需的。非肽基转谷氨酰胺酶灭活剂的存在使细胞更容易被胰蛋白酶分离，并破坏了纤维连接蛋白与内皮下细胞外基质的联系。因此，内皮细胞通过细胞基表面组织转谷氨酰胺酶的表达，将纤维连接蛋白加工成交联多聚体。这一过程可能有助于稳定细胞外基质，并将细胞牢固地固定在基底膜上。血管内皮细胞外基质在介导内皮细胞生化事件中发挥重要作用，影响多种生物过程（Hynes, 1990; Ruoslahti, 1988; Albelda et al., 1989; Ingber, 1990）。人内皮细胞和成纤维细胞在涂有纤维连接蛋白、层粘连蛋白、iv型胶原蛋白、玻璃体连接蛋白或血管性血液病因子等基质成分的组织培养皿上的附着和扩散主要是由细胞受体（称为整合素）与每种基质蛋白的特定功能域的相互作用介导的。就纤维连接蛋白而言，这种关联主要是通过其细胞结合域与as (f)整合素的相互作用来实现的，这种相互作用涉及调节细胞骨架的组织、决定细胞形态和控制细胞生长（Hynes, 1990; Ruoslahti, 1988; Albelda et ah, 1989; Ingber, 1990）。纤维连接蛋白分子是一种二聚体糖蛋白，每个亚基的分子质量为230-250kDa
Revised Manuscript Received November 29, 1993® abstract: We studied the interaction of [125I] fibronectin with human umbilical vein endothelial cells. Endothelial cell monolayers cross-linked [125I] fibronectin which had been preadsorbed to gelatin-coated dishes. The cross-linking of the substrate-immobilized [125I] fibronectin was mediated by cell-associated tissue transglutaminase and occurred more rapidly during the first 30 min after endothelial cell seeding but also continued for several hours after the cells were fully spread. The processing of the [125I] fibronectin was associated with the basolateral surface of the endothelial cell, as demonstrated by the finding that cross-linking did not occur when [125I] fibronectin was presented to the apical surface of confluent monolayers. Transglutaminase activity was not necessary for attachment and spreading of HUVEC on a fibronectin/gelatin matrix. The presence of a nonpeptidyl transglutaminase inactivator rendered the cells more susceptible to detachment by trypsin and destabilized the association of fibronectin with the subendothelial extracellular matrix. Thus, endothelial cells process fibronectin into cross-linked multimers due to the expression of tissue transglutaminase at the basal surface of the cell. This process may serve to stabilize the extracellular matrix and to firmly anchor the cells to the basement membrane.The extracellular matrix of vascular endothelium plays an essential role in mediating biochemical events in endothelial cells which influence a variety of biological processes (Hynes, 1990; Ruoslahti, 1988; Albelda et al., 1989; Ingber, 1990). The attachment and spreading of human endothelial cells and fibroblasts on tissue culture dishes coated with matrix components such as fibronectin, laminin, type-IV collagen, vitronectin, or von Willebrand factor are largely mediated by the interaction of cellular receptors, known as integrins, with specific functional domains of each matrix protein. In the case of fibronectin, this association is principally accomplished by the interaction of its cell-binding domain with the as (f integrin, an interaction which is involved in regulating organization of the cytoskeleton, in determining cell mor-phology, and in controlling cell growth (Hynes, 1990; Ruoslahti, 1988; Albelda et ah, 1989; Ingber, 1990). The fibronectin molecule is a dimeric glycoprotein, each subunit having a molecular mass of 230-250kDa and
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成纤维细胞层中因子 XIIIa 介导的纤连蛋白交联。
DOI：
--
发表时间：
1989
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Barry,EL;Mosher,DF
通讯作者：
Mosher,DF
影响因子：
6.4
作者：
ENGVALL, E;RUOSLAHTI, E
通讯作者：
RUOSLAHTI, E
悬浮液中兔肝细胞对兔纤连蛋白的结合和交联。
DOI：
--
发表时间：
1988
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Fellin,FM;Barsigian,C;Rich,E;Martinez,J
通讯作者：
Martinez,J
纤维蛋白原和纤连蛋白结合从转谷氨酰胺酶介导的肝细胞表面交联中解离。
DOI：
--
发表时间：
1988
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Barsigian,C;Fellin,FM;Jain,A;Martinez,J
通讯作者：
Martinez,J
NIL.8 仓鼠细胞中纤连蛋白的生物合成和加工。
影响因子：
4.8
作者：
M. Choi;R. Hynes
通讯作者：
R. Hynes