ArticleProceedings of the National Academy of Sciences of the United States of America1996
Homophilic adhesion mediated by the neural cell adhesion molecule involves multiple immunoglobulin domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 123 citations in OpenAlex.
- Nerve bundle formation during the promotion of peripheral nerve regeneration: collagen VI-neural cell adhesion molecule 1 interaction.Neural regeneration research · 2022Article
- Altering Cell-Cell Interaction in Prenatal Alcohol Exposure Models: Insight on Cell-Adhesion Molecules During Brain Development.Frontiers in molecular neuroscience · 2021Review
- Structural Characterization and Function Prediction of Immunoglobulin-like Fold in Cell Adhesion and Cell Signaling.Journal of chemical information and modeling · 2018Article
- Understanding the Functional Roles of Multiple Extracellular Domains in Cell Adhesion Molecules with a Coarse-Grained Model.Journal of molecular biology · 2017Article
- Glycosylphosphatidylinositol-Anchored Immunoglobulin Superfamily Cell Adhesion Molecules and Their Role in Neuronal Development and Synapse Regulation.Frontiers in molecular neuroscience · 2017Review
- Magnetic tweezers-based force clamp reveals mechanically distinct apCAM domain interactions.Biophysical journal · 2012Article
- Single-molecule force spectroscopy of the Aplysia cell adhesion molecule reveals two homophilic bonds.Biophysical journal · 2012Article
- Sequences at the interface of the fifth immunoglobulin domain and first fibronectin type III repeat of the neural cell adhesion molecule are critical for its polysialylation.The Journal of biological chemistry · 2011Article
- Structure and mutagenesis of neural cell adhesion molecule domains: evidence for flexibility in the placement of polysialic acid attachment sites.The Journal of biological chemistry · 2010Article
- Elasticity and rupture of a multi-domain neural cell adhesion molecule complex.Biophysical journal · 2009Article
- Pharmacology of cell adhesion molecules of the nervous system.Current neuropharmacology · 2007Article
- Multiple-bond kinetics from single-molecule pulling experiments: evidence for multiple NCAM bonds.Biophysical journal · 2005Article
- Architecture and adhesive activity of the Haemophilus influenzae Hsf adhesin.Journal of bacteriology · 2005Article
- Mouse Na+/K+-ATPase beta1-subunit has a K+-dependent cell adhesion activity for beta-GlcNAc-terminating glycans.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Mechanism of homophilic adhesion by the neural cell adhesion molecule: use of multiple domains and flexibility.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- NCAM mimetic peptides: Pharmacological and therapeutic potential.Journal of molecular neuroscience : MN · 2004Review
- Functional analysis of the structural basis of homophilic cadherin adhesion.Biophysical journal · 2003Article
- Intracellular signaling by the neural cell adhesion molecule.Neurochemical research · 2003Review
- Expression of CD56/neural cell adhesion molecule correlates with the presence of lytic bone lesions in multiple myeloma and distinguishes myeloma from monoclonal gammopathy of undetermined significance and lymphomas with plasmacytoid differentiation.The American journal of pathology · 2002Article
- Multiple cadherin extracellular repeats mediate homophilic binding and adhesion.The Journal of cell biology · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The neural cell adhesion molecule (N-CAM) mediates homophilic binding between a variety of cell types including neurons, neurons and glia, and neurons and muscle cells. The mechanism by which N-CAM on one cell interacts with N-CAM on another, however, is unknown. Attempts to identify which of the five immunoglobulin-like domains (Ig I-V) and the two fibronectin type III repeats (FnIII 1-2) in the extracellular region of N-CAM are involved in this process have led to ambiguous results. We have generated soluble recombinant proteins corresponding to each of the individual immunoglobulin domains and the combined FnIII 1-2 and prepared polyclonal antibodies specific for each. The purified proteins and antibodies were used in aggregation experiments with fluorescent microspheres and chicken embryo brain cells to determine possible contributions of each domain to homophilic adhesion. The recombinant domains were tested for their ability to bind to purified native N-CAM, to bind to each other, and to inhibit the aggregation of N-CAM on microspheres and the aggregation of neuronal cells. Each of the immunoglobulin domains bound to N-CAM, and in solution all of the immunoglobulin domains inhibited the aggregation of N-CAM-coated microspheres. Soluble Ig II, Ig III, and Ig IV inhibited neuronal aggregation; antibodies against whole N-CAM, the Ig III domain, and the Ig I domain all strongly inhibited neuronal aggregation, as well as the aggregation of N-CAM-coated microspheres. Of all the domains, the third immunoglobulin domain alone demonstrated the ability to self-aggregate, whereas Ig I bound to Ig V and Ig II bound to Ig IV. The combined FnIII 1-2 exhibited a slight ability to self-aggregate but did not bind to any of the immunoglobulin-like domains. These results suggest that N-CAM-N-CAM binding involves all five immunoglobulin domains and prompt the hypothesis that in homophilic cell-cell binding mediated by N-CAM these domains may interact pairwise in an antiparallel orientation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.