Blood Vessel Epicardial Substance (Bves) Regulates Epidermal Tight Junction Integrity through Atypical Protein Kinase C

doi:10.1074/jbc.M112.372078

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Title:	Blood Vessel Epicardial Substance (Bves) Regulates Epidermal Tight Junction Integrity through Atypical Protein Kinase C
Authors:	Wu, Yu-Ching;Liu, Chia-Yang;Chen, Yau-Hung;Chen, Ruei-Feng;Huang, Chang-Jen;Wang, I-Jong
Contributors:	淡江大學化學學系
Keywords:	Cell Permeabilization;Cell-Cell Interaction;Epidermis;Membrane Function;Tight Junctions;aPKC;Epidermal Barrier;Tight Junction;zBves
Date:	2012-11-01
Issue Date:	2013-01-08 13:10:45 (UTC+8)
Publisher:	American Society for Biochemistry and Molecular Biology
Abstract:	Bves is widely observed in the cell junction of the skin, epicardium, intestine, and cornea of both developmental embryos and mature adults. However, it is not clear how Bves confers its role in intercellular adhesion. Here, we identified the zebrafish bves (zBves) and found that the epidermal barrier function could be disrupted after knockdown of Bves, and these zBves morphants were sensitive to osmotic stress. A loss of zBves would affect the partitioning defective protein (PAR) junctional complex identified by the rescue experiment with tjp-2/ZO-2 or the PAR complex (par-3, par-6, and prkci/atypical (a)PKC) mRNAs, in which the survival rate of embryos increased 11, 24, 25, and 28%, respectively, after injection with junctional components; the tjp-2 and aPKC mRNA-rescued embryos also had 24 and 45% decreases in the defective rate. Immunofluorescent studies demonstrated that the aggregation of aPKC around the cell junctions had disintegrated in zBves morphants. However, the expression and assembly of zBves were not influenced by aPKC-MO. These results indicate that a loss of zBves affects the proteins involved in the pathway of the PAR junctional complex, especially aPKC, and both aPKC and Bves are indispensable to claudin expression.
Relation:	The Journal of Biological Chemistry 287(47), pp.39887-39897
DOI:	10.1074/jbc.M112.372078
Appears in Collections:	[Graduate Institute & Department of Chemistry] Journal Article

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