The Loss of the Expression of α Catenin, the 102 kD Cadherin Associated Protein, in Central Nervous Tissues during Development

Abstract

A monoclonal antibody specific for a catenin, the 102 kD cadherin-associated protein, has been characterized and used to describe the expression and distribution pattern of a catenin in adult mice and mouse embryos. This monoclonal antibody recognized an epitope in the middle part of the (Y catenin molecule of various vertebrate species, and bound to neither vinculin nor crN catenin, which are cytoskeletal proteins with sequence similarity to (Y catenin. At the early mouse embryo stage (neurulae stage) a catenin was expressed and concentrated at cell-to-cell contact sites together with various types of cadherins in all tissues. In embryos at 12.5 days of gestation, the a catenin expression was gradually diminished selectively in central nervous tissues such as brain and spinal cord, and in most of the adult central nervous tissues the a catenin expression was hardly detected. In adult non-nervous tissues most of the cells examined expressed a catenin. Especially in well-polarized tissues such as epithelial cells, a catenin appeared to be highly concentrated at cell-to-cell adherens junctions where cadherins act as adhesion molecules.This loss of a catenin expression in central nervous tissues was observed not only in mice but also in other vertebrate species such as fish and newt, suggesting that this phenomenon has important implications from the view point of nervous tissue development.

An α- E-catenin gene trap mutation defines its function in preimplantation development

“…2). The LacZ expression observed is in agreement with and extends previously reported expression data of ␣-E-catenin (19,30).…”

Tricellulin regulates junctional tension of epithelial cells at tricellular contacts via Cdc42

“…Rabbit pAbs against mouse Tuba were raised against GST fusion proteins with fragments encoding amino acids 1376-1518 and 561-710. Mouse anti-ZO-1 mAb T8-754 (Itoh et al, 1991) and rat anti-a-catenin mAb a-18 (Nagafuchi and Tsukita, 1994) were kindly provided by Masahiko Itoh (Dokkyo Medical University, Tochigi, Japan) and Akira Nagafuchi (Nara Medical University, Nara, Japan), respectively. The following secondary antibodies were used: Alexa-Fluor-488-conjugated donkey anti-rat-, anti-mouse-and anti-rabbit-IgG (Invitrogen); Cy3-or Cy5-conjugated goat anti-rat-, anti-mouse-and anti-rabbit-IgG (Jackson Immunoresearch Laboratories); and horseradish-peroxidase-conjugated anti-rat-, antimouse-and anti-rabbit-IgG (GE Healthcare).…”

Involvement of p120 Carboxy-Terminal Domain in Cadherin Trafficking

“…The following primary antibodies were used for the immunofluorescent staining and Western blot analyses: mouse anti-p120, mouse anti-β-catenin and mouse anti-plakoglobin mAbs (BD Transduction Laboratories), rat anti-mouse E-cadherin mAb (ECCD-2) (Shirayoshi et al, 1986), rat anti-α-catenin mAb (α18) (Nagafuchi and Tsukita, 1994), mouse anti-HA tag mAb (12C5A, Roche), rat anti-mouse LAMP-1 mAb (1D4B; Southern Biotechnology Associates, Inc.), rabbit anti-E-cadherin pAb (Nagafuchi et al, 1987), anti-GFP polyclonal antibody (pAb) (Molecular Probes), anti-α-tubulin mAb (DM1A; Sigma-Aldrich). FITC-or Cy3-conjugated donkey anti-rabbit, anti-mouse and anti-rat IgGs (Jackson Immunoresearch) were used as secondary antibodies for the immunofluorescent staining.…”

“…SDS-PAGE and immunoblotting was performed as previously described (Nagafuchi and Tsukita, 1994). Samples were solubilized in SDS sample buffer and then separated by SDS-PAGE.…”