Article

Gene expression pattern analysis of the tight junction protein, Claudin, in the early morphogenesis of Xenopus embryos.

Department of Biological Sciences, Graduate School of Science, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan.
Mechanisms of Development (impact factor: 2.83). 01/2003; 119 Suppl 1:S27-30.
Source: PubMed

ABSTRACT To study how epithelial layers are formed during early development in Xenopus embryos, we have focused on Claudin, the major component of the tight junction. So far, 19 claudin genes have been found in the mouse, expressed in different epithelial tissues. However, though a number of cytological studies have been done for the roles of Claudins, their expression patterns and functions during early embryogenesis are largely unknown. We found three novel Xenopus claudin genes, which are referred to as claudin-4L1, -4L2, and -7L1. At the early gastrula stage, claudin-4L1, -4L2, and -7L1 mRNAs were detected in the ectoderm and in the mesoderm. At the late gastrula stage, claudin mRNAs were detected in the ectoderm through the involuting archenteron roof. At the neurula stage, claudin-4L1/4L2 and -7L1 mRNAs were differentially expressed in the neural groove and the epidermal ectoderm. At the tailbud stage, the claudin mRNAs were found in the branchial arches, the otic vesicles, the sensorial layer of the epidermis, and along the dorsal midline of the neural tube. In addition, claudin-4L1/4L2 mRNAs were detected in the pronephros and the endoderm, whereas claudin-7L1 mRNA was observed in the epithelial layer of the epidermis.

0 0
 · 
0 Bookmarks
 · 
22 Views
  • Article: Phosphorylation of ephrin-B1 via the interaction with claudin following cell-cell contact formation.
    [show abstract] [hide abstract]
    ABSTRACT: The interaction of the Eph family of receptor protein tyrosine kinase and its ligand ephrin family induces bidirectional signaling via the cell-cell contacts. Although most previous studies have focused on the function of Eph-ephrin pathways in the neural system and endothelial cells, this process also occurs in epithelial and cancer cells, of which the biological involvement is poorly understood. We show that ephrin-B1 creates an in vivo complex with adjacent claudin1 or claudin4 via the extracellular domains of these proteins. The cytoplasmic domain of ephrin-B1 was phosphorylated on tyrosine residues upon the formation of cell-cell contacts, possibly recognizing an intercellular adhesion of claudins. Phosphorylation of ephrin-B1 induced by claudins was abolished by the treatment with 4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine, an inhibitor of the Src family kinases. Moreover, overexpression of ephrin-B1 triggered consequent change in the level of cell-cell adhesion depending on its phosphorylation. These results suggest that ephrin-B1 mediated the cell-cell adhesion of epithelial and cancer cells via a novel Eph receptor-independent mechanism.
    The EMBO Journal 12/2005; 24(21):3700-11. · 9.20 Impact Factor

Keywords

-7L1 mRNAs
 
19 claudin genes
 
branchial arches
 
claudin mRNAs
 
claudin-4L1
 
claudin-4L1/4L2 mRNAs
 
claudin-7L1 mRNA
 
Claudins
 
different epithelial tissues
 
dorsal midline
 
epidermal ectoderm
 
epithelial layer
 
gastrula stage
 
involuting archenteron roof
 
major component
 
neural groove
 
neurula stage
 
novel Xenopus claudin genes
 
sensorial layer
 
tailbud stage
 

Makiko Fujita