Introduction adhesive proteins

Reichardt, L.E, Introduction extracellular matrix molecules, in Guidebook to the Extracellular Matrix, Anchor, and Adhesion Proteins, 2nd ed., Oxford University Press, New York, 1999, p. 335. 

The introduction of retro-, retro-inverso-, and PMRI-peptides with free and blocked C-and N-termini has been successful in numerous biological systems such as neurotransmitters, inhibitors of proteases and protein kinases, sweeteners, antimicrobial peptides, hormones, adhesion molecules, antigenic epitopes, immuno-modulators, and immunological probes. Table 1 provides an exhaustive list of retro-, retro-inverso-, PMRI-, and end-group-modified re/ro-mvmo-pseudopeptides derived from bioactive peptides. 

Adhesion of different immune cells to one another or to epithelial cells has also been studied using planar bilayer models. For example, lymphocyte function-associated protein-1 (LFA-1) promotes cell adhesion in inflammation [i.e., a reaction that can be mimicked by binding to purified ICAM-1 in supported membranes (70)]. Similarly, purified LFA-3 reconstituted into supported bilayers mediates efficient CD2-dependent adhesion and differentiation of lymphoblasts (71). This work was followed by a study in which transmembrane domain-anchored and GPl-anchored isoforms of LFA-3 were compared (72). Because this research occurred before the introduction of polymer cushions and because the bilayers were formed by the simple vesicle fusion technique, the transmembrane domain isoform was immobile, whereas the GPl isoform was partially mobile. By comparing results with these two isoforms at different protein densities in the supported bilayer, the authors showed that diffusible proteins at a sufficient minimal density in the supported membrane were required to form strong cell adhesion contacts in this system. 

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