3/13/2023 0 Comments Cayla vimrStructural basis of CAM-mediated cell adhesion. We also discuss how unravelling of the 3D structure of CAMs provides novel pharmacological tools for dissection of CAMs-induced signalling pathways and offers therapeutic opportunities for a range of neurological disorders. Different pharmacological approaches to study the functions of CAMs are presented, including the use of specific antibodies, recombinant proteins, and synthetic peptides. We outline the structural basis of CAM-mediated cell adhesion and CAM-induced signalling. This review discusses the progress in CAM pharmacology focusing on cadherins and CAMs belonging to the Ig superfamily, such as NCAM and L1 (see for a detailed description of neural CAMs of the Ig-superfamily). Therefore, it has become important to develop pharmacological tools that can target homophilic and/or heterophilic interactions of CAMs and thus modulate cellular responses induced by CAM binding. However, it is not always possible to obtain the relevant constructs for a particular protein, and many animal systems are not easily amenable to genetic modifications. One strategy used to address CAM function is to study cells with genetic knock-out or knock-in of CAMs. Because of this diversity CAMs not only play a pivotal role in the function of the nervous system under normal conditions, but also are involved in numerous pathological processes such as inflammation, neurodegeneration, and cancer. These include neurite outgrowth and axonal pathfinding, synapse formation and remodelling, modulation of cell motility and survival, to mention a few. CAM-induced intracellular signalling is triggered via homophilic (CAM-CAM) and heterophilic (CAM - other counter-receptors) interactions resulting in a variety of cellular responses. ![]() CAMs are not only 'mechanical' regulators of cell adhesion, but also signal transducing receptors. The first three classes are ubiquitously expressed in the nervous system. CAMs can be divided into four classes: integrins, cadherins, members of the immunoglobulin (Ig) superfamily, and selectins. We also discuss how unravelling of the 3D structure of CAMs provides novel pharmacological tools for dissection of CAM-induced signalling pathways and offers therapeutic opportunities for a range of neurological disorders.Ĭell adhesion molecules (CAMs) are glycoproteins found on the cell surface that mediate cell-cell and cell-extracellular matrix (ECM) adhesion. Different pharmacological approaches to study functions of CAMs are presented including the use of specific antibodies, recombinant proteins, and synthetic peptides. Structural basis of CAM-mediated cell adhesion and CAM-induced signalling are outlined. We here describe the progress in the CAM pharmacology focusing on cadherins and CAMs of the immunoglobulin (Ig) superfamily, such as NCAM and L1. CAM-induced intracellular signalling is triggered via homophilic (CAM-CAM) and heterophilic (CAM - other counter-receptors) interactions, which both can be targeted pharmacologically. ![]() The majority of CAMs are signal transducing receptors. They also are involved in numerous pathological processes such as inflammation, degenerative disorders, and cancer, making them attractive targets for drug development. Cell adhesion molecules (CAMs) play a pivotal role in the development and maintenance of the nervous system under normal conditions.
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