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因子XIIIa介导的成纤维细胞层中纤连蛋白的交联。细胞纤连蛋白与血浆纤连蛋白以及氨基末端纤连蛋白片段的交联。

Factor XIIIa-mediated cross-linking of fibronectin in fibroblast cell layers. Cross-linking of cellular and plasma fibronectin and of amino-terminal fibronectin fragments.

作者信息

Barry E L, Mosher D F

机构信息

Department of Physiological Chemistry, University of Wisconsin, Madison 53706.

出版信息

J Biol Chem. 1989 Mar 5;264(7):4179-85.

PMID:2917995
Abstract

Factor XIIIa cross-links plasma fibronectin as it is being assembled into the extracellular matrix of cultured human skin fibroblasts (Barry, E. L. R., and Mosher, D. F. (1988) J. Biol. Chem. 262, 10464-10469). We have further characterized this process. Fibroblasts were metabolically labeled with proline in the presence or absence of ascorbate and Factor XIIIa. Endogenous fibronectin in the extracellular matrix was cross-linked by Factor XIIIa. There was no evidence for cross-linking of collagenous proteins. Fibro-blast cell layers were incubated with iodinated 27-kDa heparin-binding or 70-kDa collagen- and heparin-binding amino-terminal fibronectin fragments. Factor XIIa cross-linked the fragments into high molecular weight aggregates. The amounts of cross-linked fragments reaches a steady state after 1 to 2 h, whereas intact fibronectin continues to be cross-linked for 24 h. When fibroblast cell layers were pulsed with iodinated fibronectin or amino-terminal fragments and Factor XIIIa was included in the chase media, the high molecular weight aggregates were formed in a step-wise manner. The smallest cross-linking steps were to high molecular weight extracellular matrix molecules forming approximately 270-, 300-, and 440-kDa complexes for the 27-kDa fragment, 70-kDa fragment, and intact fibronectin, respectively. When iodinated fibronectin was bound to fibroblast cell layers and chased into the matrix pool in the absence of Factor XIIIa, it could also be cross-linked into high molecular weight complexes when Factor XIIIa was added to the media. These results, therefore, indicate that both cellular and plasma fibronectin and amino-terminal fragments are cross-linked specifically by Factor XIIIa, that the cross-linking is probably to other fibronectin molecules rather than to collagenous proteins, and that both assembling and assembled fibronectin are substrates for Factor XIIIa.

摘要

当血浆纤连蛋白组装进入培养的人皮肤成纤维细胞的细胞外基质时,凝血因子XIIIa会使其发生交联(巴里,E.L.R.,和莫舍,D.F.(1988年)《生物化学杂志》262卷,10464 - 10469页)。我们进一步对这一过程进行了表征。在有或没有抗坏血酸和凝血因子XIIIa存在的情况下,用脯氨酸对成纤维细胞进行代谢标记。细胞外基质中的内源性纤连蛋白被凝血因子XIIIa交联。没有证据表明胶原蛋白质发生了交联。将成纤维细胞层与碘化的27 kDa肝素结合或70 kDa胶原和肝素结合的氨基末端纤连蛋白片段一起孵育。凝血因子XIIa将这些片段交联成高分子量聚集体。交联片段的量在1至2小时后达到稳定状态,而完整的纤连蛋白会持续交联24小时。当成纤维细胞层用碘化纤连蛋白或氨基末端片段进行脉冲处理,且在追踪培养基中加入凝血因子XIIIa时,高分子量聚集体会逐步形成。最小的交联步骤是形成高分子量的细胞外基质分子,对于27 kDa片段、70 kDa片段和完整的纤连蛋白,分别形成约270 kDa、300 kDa和440 kDa的复合物。当碘化纤连蛋白与成纤维细胞层结合并在没有凝血因子XIIIa的情况下追踪到基质池中时,当向培养基中加入凝血因子XIIIa时,它也可以交联成高分子量复合物。因此,这些结果表明,细胞和血浆纤连蛋白以及氨基末端片段都被凝血因子XIIIa特异性交联,这种交联可能是与其他纤连蛋白分子而非胶原蛋白质发生交联,并且正在组装和已组装的纤连蛋白都是凝血因子XIIIa的底物。

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