蛋白激酶C
封堵器
肽
紧密连接
磷酸化
细胞生物学
并行传输
增强子
五肽重复序列
生物化学
化学
棕榈酰化
生物
生物物理学
酶
磁导率
转录因子
膜
基因
半胱氨酸
作者
Joël Brunner,Domitille Schvartz,Aurélie Gouiller,Alexandre Hainard,Gerrit Borchard
标识
DOI:10.1016/j.bbrep.2022.101375
摘要
The myristoylated pentapeptide, L-R5, contains an amino acid sequence of the zeta inhibitory peptide (ZIP) portion (pseudosubstrate) of protein kinase C zeta (PKC ζ). As PKC ζ is involved in the modulation of epithelial tight junctions (TJs) through the phosphorylation of TJ proteins, L-R5 was suggested to interact with the enzyme resulting in the enhancement of paracellular permeability. This study shows that L-R5 does not bind to the enzyme but interacts directly with TJ proteins. We show here that the binding of PKC ζ to occludin and its successive phosphorylation is prevented by L-R5, which leads to TJ disruption and enhanced epithelial permeability. Although L-R5 did not show any in vitro cytotoxicity, a proteomics study revealed that L-R5 interferes with other regulatory pathways, e.g., apoptosis and immune response. We suggest that structural modification of the peptide may increase the specificity TJ protein-peptide interaction.
科研通智能强力驱动
Strongly Powered by AbleSci AI