绒毛
生物
画笔边框
体内
肌动蛋白
细胞生物学
生物化学
遗传学
小泡
膜
作者
Évelyne Ferrary,Michel Cohen‐Tannoudji,Gérard Pehau‐Arnaudet,Alexandre Lapillonne,Rafika Athman,Tereza Ruiz,Lilia Boulouha,Fatima El Marjou,Anne Doye,Jean‐Jacques Fontaine,Claude Antony,Charles Babinet,Daniel Louvard,Frédéric Jaisser,Sylvie Robine
标识
DOI:10.1083/jcb.146.4.819
摘要
Villin is an actin-binding protein localized in intestinal and kidney brush borders. In vitro, villin has been demonstrated to bundle and sever F-actin in a Ca2+-dependent manner. We generated knockout mice to study the role of villin in vivo. In villin-null mice, no noticeable changes were observed in the ultrastructure of the microvilli or in the localization and expression of the actin-binding and membrane proteins of the intestine. Interestingly, the response to elevated intracellular Ca2+ differed significantly between mutant and normal mice. In wild-type animals, isolated brush borders were disrupted by the addition of Ca2+, whereas Ca2+ had no effect in villin-null isolates. Moreover, increase in intracellular Ca2+ by serosal carbachol or mucosal Ca2+ ionophore A23187 application abolished the F-actin labeling only in the brush border of wild-type animals. This F-actin disruption was also observed in physiological fasting/refeeding experiments. Oral administration of dextran sulfate sodium, an agent that causes colonic epithelial injury, induced large mucosal lesions resulting in a higher death probability in mice lacking villin, 36 ± 9.6%, compared with wild-type mice, 70 ± 8.8%, at day 13. These results suggest that in vivo, villin is not necessary for the bundling of F-actin microfilaments, whereas it is necessary for the reorganization elicited by various signals. We postulate that this property might be involved in cellular plasticity related to cell injury.
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