Schwarzbauer J E
Department of Molecular Biology, Princeton University, NJ 08544.
Bioessays. 1991 Oct;13(10):527-33. doi: 10.1002/bies.950131006.
Fibronectin (FN) is a multi-functional extracellular matrix protein required for cell adhesion and migration, blood clotting, wound healing, and oncogenic transformation. The functional complexity is paralleled by structural diversity in that multiple forms of FN are generated by cell type-specific alternative splicing. In the rat, up to 12 different combinations of the three alternatively spliced segments (EIIIA, EIIIB, and the V region) are produced. What effects do these segments have on FN function? Recently, progress has been made in the identification of specific activities for the three variants of the V region, V120, V95, and V0. FN-mediated cell adhesion, FN synthesis and secretion, and incorporation into blood clots are differentially affected by these isoforms. These results suggest that cellular behavior is modulated by environmental cues provided by different types and proportions of alternatively spliced FN variants.
纤连蛋白（FN）是一种多功能细胞外基质蛋白，在细胞黏附与迁移、血液凝固、伤口愈合以及致癌转化过程中发挥着重要作用。其功能的复杂性与结构多样性并存，因为多种形式的FN是由细胞类型特异性可变剪接产生的。在大鼠体内，三个可变剪接片段（EIIIA、EIIIB和V区域）最多可产生12种不同的组合。这些片段对FN功能有何影响？最近，在鉴定V区域的三个变体V120、V95和V0的特定活性方面取得了进展。这些异构体对FN介导的细胞黏附、FN的合成与分泌以及融入血凝块的过程产生了不同的影响。这些结果表明，细胞行为受到不同类型和比例的可变剪接FN变体所提供的环境线索的调节。
