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      Is Open Access

      Monoclonal antibody 10A5 recognizes an antigen unique to the water-insoluble 25/45 membrane fraction of the rat ocular lens

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          Abstract

          The water-insoluble 25/45 fraction and non-sedimenting membrane fraction (NSMF) are two membrane preparations isolated from the ocular lens. The fractions are postulated to represent distinct subdomains of the lens with unique functions. However, attempts to distinguish between the two fractions by detecting proteins present in one fraction but absent from other have been unsuccessful. In this study, we exploited the ability of the mouse immune system to detect antigenic differences between the 25/45 fraction and NSMF isolated from the lenses of 20-day-old rats. We generated a monoclonal antibody (MAb 10A5) that reacts with a ganglioside-like antigen that is present in the 25/45 fraction but absent from the NSMF. Restriction of the antigen to the 25/45 fraction in 20-day-old animals supports the hypothesis that the 25/45 fraction and NSMF represent different subdomains within the ocular lens.

          Electronic supplementary material

          The online version of this article (doi:10.1186/2193-1801-2-500) contains supplementary material, which is available to authorized users.

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          Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane

          Patrick Lajoie, Jacky Goetz, James W. Dennis … (2009)
          The plasma membrane is organized into various subdomains of clustered macromolecules. Such domains include adhesive structures (cellular synapses, substrate adhesions, and cell–cell junctions) and membrane invaginations (clathrin-coated pits and caveolae), as well as less well-defined domains such as lipid rafts and lectin-glycoprotein lattices. Domains are organized by specialized scaffold proteins including the intramembranous caveolins, which stabilize lipid raft domains, and the galectins, a family of animal lectins that cross-link glycoproteins forming molecular lattices. We review evidence that these heterogeneous microdomains interact to regulate substratum adhesion and cytokine receptor dynamics at the cell surface.
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            Glycosphingolipids in cellular interaction, differentiation, and oncogenesis.

            S Hakomori (1980)
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              Gangliosides as components of lipid membrane domains.

              Sandro Sonnino, Laura Mauri, Vanna Chigorno … (2007)
              Cell membrane components are organized as specialized domains involved in membrane-associated events such as cell signaling, cell adhesion, and protein sorting. These membrane domains are enriched in sphingolipids and cholesterol but display a low protein content. Theoretical considerations and experimental data suggest that some properties of gangliosides play an important role in the formation and stabilization of specific cell lipid membrane domains. Gangliosides are glycolipids with strong amphiphilic character and are particularly abundant in the plasma membranes, where they are inserted into the external leaflet with the hydrophobic ceramide moiety and with the oligosaccharide chain protruding into the extracellular medium. The geometry of the monomer inserted into the membrane, largely determined by the very large surface area occupied by the oligosaccharide chain, the ability of the ceramide amide linkage to form a network of hydrogen bonds at the water-lipid interface of cell membranes, the Delta(4) double bond of sphingosine proximal to the water-lipid interface, the capability of the oligosaccharide chain to interact with water, and the absence of double bonds into the double-tailed hydrophobic moiety are the ganglioside features that will be discussed in this review, to show how gangliosides are responsible for the formation of cell lipid membrane domains characterized by a strong positive curvature.
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                Author and article information

                Contributors
                : jwhitman@atsu.edu
                : aalviar@phoenixchildrens.com
                : cfleschner@atsu.edu
                : mstuart@atsu.edu
                Journal
                Journal ID (nlm-ta): Springerplus
                Journal ID (iso-abbrev): Springerplus
                Title: SpringerPlus
                Publisher: Springer International Publishing (Cham )
                ISSN (Electronic): 2193-1801
                Publication date (Electronic): 2 October 2013
                Publication date PMC-release: 2 October 2013
                Publication date Collection: 2013
                Volume: 2
                Electronic Location Identifier: 500
                Affiliations
                [ ]Northeast Regional Medical Center, Otolaryngology/Facial Plastic Surgery Residency Program, 315 S Osteopathy Ave, Kirksville, MO 63501 USA
                [ ]Phoenix Children’s Hospital/Maricopa Medical Center Pediatric Residency Program, 1919 E Thomas Rd, Phoenix, AZ 85016 USA
                [ ]Department of Biochemistry, A T Still University, Kirksville College of Osteopathic Medicine, 800 W Jefferson St, Kirksville, MO 63501 USA
                [ ]Department of Microbiology/Immunology, A T Still University, Kirksville College of Osteopathic Medicine, 800 W Jefferson St, Kirksville, MO 63501 USA
                Article
                Publisher ID: 557
                DOI: 10.1186/2193-1801-2-500
                PMC ID: 3793078
                SO-VID: 9ff1fb3f-24d4-4a61-be2d-09bc274a253d
                Copyright © © Whitman et al.; licensee Springer. 2013
                License:

                This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 13 May 2013
                Date accepted : 1 October 2013
                Categories
                Subject: Research
                Custom metadata
                issue-copyright-statement © The Author(s) 2013

                ScienceOpen disciplines: Uncategorized
                Keywords: ocular lens,plasma membrane domains,monoclonal antibodies,gangliosides
                Data availability:
                ScienceOpen disciplines: Uncategorized
                Keywords: ocular lens, plasma membrane domains, monoclonal antibodies, gangliosides

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