A 135-kd membrane protein of intercellular adherens junctions.

Abstract

We report here on a new 135-kd membrane protein which is specifically associated with intercellular adherens-type junctions. This surface component was identified by a monoclonal antibody, ID-7.2.3, raised against detergent-extracted components of membranes of chicken cardiac muscle rich in intercalated discs. The antibodies stain extensively adherens junctions in intact cardiac muscle and in lens, as well as in cultured cells derived from these tissues. In living cultured cells only very little immunolabelling was obtained with ID-7.2.3 antibodies, probably due to the limited accessibility of the antibodies to the intercellular gap. However, upon the removal of extracellular Ca2 + ions a dissociation of the junction occurred, leading to the rapid exposure of the 135-kd protein. Immunoelectron microscopic labelling of EGTAtreated, or detergent-permeabilized cells indicated that the antigen is found along the plasma membrane and highly enriched in contact areas. Double immunolabelling for both the 135-kd protein and vinculin pointed to the close association of the two in intercellular junctions and to the apparent absence of the former protein from the vinculin-rich focal contacts of cultured cells and from dense plaque of smooth muscle. Immunoblotting indicated that the 135-kd protein is present in many tissues but is particularly enriched in heart, lens and brain.

Structure and distribution of N‐cadherin in developing zebrafish embryos: Morphogenetic effects of ectopic over‐expression

“…Cells were labeled using affinity purified R-851 antibodies and rhodamine-conjugated goat anti rabbit antibodies (Jackson Labs, Bar Harbor, ME) as described (Volk and Geiger, 1984).…”

The cytoplasmic domain of adherens‐type junctions

“…readily exchange with the cytoplasmic diffusible pool [Geiger et al, 1984;Kreis et al, 19851. This feature suggests that the assembly of the AJ complex and/or its modulation depends on the availability of potent binding sites for cytoplasmic junctional molecules at the endofacial surfaces of the junction itself rather than on an active and directional transport mechanism.…”

Adherens Junction: Molecular Architecture and Regulation

“…Early studies to search for the molecules responsible for the calcium-dependent junctions resulted in the identification of a group of type-I transmembrane proteins, and its founding member was termed cadherin (Yoshida and Takeichi 1982;Yoshida-Noro et al 1984). Related molecules identified were also called by various names, such as uvomorulin (Peyrieras et al 1983), LCAM (Gallin et al 1983), and ACAM (Volk and Geiger 1984). Later studies revealed that the cadherins form a superfamily, and therefore, the original cadherins are now called "classic" cadherins.…”