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人皮肤成纤维细胞对纤维蛋白凝胶的收缩不需要纤连蛋白和纤维蛋白溶解。

Fibronectin and fibrinolysis are not required for fibrin gel contraction by human skin fibroblasts.

作者信息

Tuan T L, Grinnell F

机构信息

Department of Cell Biology and Anatomy, University of Texas Southwestern Medical Center, Dallas 75235.

出版信息

J Cell Physiol. 1989 Sep;140(3):577-83. doi: 10.1002/jcp.1041400324.

Abstract

Human skin fibroblasts contracted fibrin gels in a time- and cell-dependent manner. Under optimal conditions, gel contraction amounted to more than 50% in 2 hr. Fibronectin did not promote contraction, and fibrinolysis was not required for contraction, although gels contracted without serum or aprotinin were lysed. Before contraction, fibrin was present in loosely packed, randomly organized fibrils. After contraction, the fibrils were more densely packed and aligned in the plane of cell spreading. Cycloheximide treatment of fibroblasts inhibited gel contraction in serum-free medium but not in serum-containing medium. Fibronectin could not substitute for serum in overcoming the cycloheximide effect. Binding sites for fibrin were distributed randomly over the cells' surfaces based on electron microscopic observations. Often small groups of fibrils were localized in indentations at the cell surface. Finally, peptides containing the arg-gly-asp-ser sequence inhibited gel contraction.

摘要

人皮肤成纤维细胞以时间和细胞依赖性方式收缩纤维蛋白凝胶。在最佳条件下,2小时内凝胶收缩率超过50%。纤连蛋白不促进收缩,收缩也不需要纤维蛋白溶解,尽管无血清或抑肽酶时收缩的凝胶会被溶解。收缩前,纤维蛋白以松散堆积、随机排列的纤维形式存在。收缩后,纤维堆积更密集,并在细胞铺展平面内排列。用环己酰亚胺处理成纤维细胞可抑制无血清培养基中的凝胶收缩,但在含血清培养基中则不然。纤连蛋白不能替代血清来克服环己酰亚胺的作用。基于电子显微镜观察,纤维蛋白的结合位点随机分布在细胞表面。通常有小群纤维位于细胞表面的凹陷处。最后,含有精氨酸-甘氨酸-天冬氨酸-丝氨酸序列的肽可抑制凝胶收缩。

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