Biochemical analysis of ligand-induced receptor patching and capping using a novel immunolactoperoxidase iodination technique.

Bourguignon, Lilly Y.W.

doi:10.1083/jcb.83.3.649

Cited by 16 publications

(4 citation statements)

References 20 publications

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“…Thus, a highly clustered distribution of the H-2 antigen is not expected. The T-200 glycoprotein on mouse thymocytes has been shown to cocap with H-2K antigens (5). However, we have observed no interaction between Con A binding glycoproteins and the antigens, as evidenced by their ability, to cap independently.…”

Section: Discussioncontrasting

confidence: 38%

Distribution and mobility of murine histocompatibility H-2Kk antigen in the cytoplasmic membrane.

Damjanovich¹,

Trón²,

Szöllősi³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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The topographical distributions and mobilities of the murine histocompatibility antigen H-2Kk and of concanavalin A (Con A) binding sites have been studied on a murine lymphoma cell line. The spatial distribution of H-2Kk antigens, the average distance between H-2Kk antigens and Con A binding sites, and the separation of different determinants on the H-2K antigen itself were determined by using fluorescence resonance energy-transfer measurements with a dual-laser flow sorter. From the lack of energy transfer between bound monoclonal anti-H-2Kk antibodies conjugated with fluorescein (donor) and rhodamine (acceptor), we conclude that the H-2Kk antigen exists without appreciable clustering on the cell surface. Substantial energy transfer between appropriately labeled Con A and antibodies bound to the H-2Kk antigen shows that the two populations are interspersed. Donor/ acceptor pairs of monoclonal antibodies binding to different determinants on the same H-2Kk antigen exhibited a degree of energy transfer indicative of a mean separation of 8.6 nm between the sites. Time-resolved phosphorescence anisotropy measurements with anti-H-2Kk antibodies labeled with eosin or erythrosin yielded rotational mobility information for the antigen-antibody complexes on the cell membrane. The rotational correlation time of 10-20 ,us and the finite residual anisotropy are compatible with an uniaxial mode of rotation of monomeric antigen around its transmembrane portion and, thus, provide additional evidence for an unclustered distribution. Capping by rabbit anti-mouse IgG immobilized the antigen-antibody complex. Fluorescence recovery after photobleaching was used to calculate an apparent lateral diffusion coefficient of 5 ± 3 X 10-10 cm2s-1 for the H-2Kk an-' tigen labeled with fluoresceinated IgG or its corresponding Fab fragment.The K and D regions of the H-2 major histocompatibility gene complex (MHC) of the mouse encode the class I antigens expressed on the surface of most somatic cells. The class I antigens consist of a highly polymorphic integral membrane glycoprotein of Mr 45,000 associated with an invariant f82-microglobulin, a Mr 11,600 protein not coded for by the MHC. These antigens and other MHC gene products guide thymic lymphocytes in distinguishing self from nonself. The H-2K and H-2D regions provide the alloantigens that control (i) allograft rejection (1-3), (ii) induction of lytic (killer) T cells (1-4), and (iii) differentiation of restricted T cells that lyse cells bearing both a foreign (e.g., viral) antigen and a H-2K or H-2D antigen presented by the initial stimulating cells (4). Models for the mechanism by which the latter process occurs provide for the recognition of a complex between MHC products and foreign antigen on the target cell (altered self; refs. 2, 5-7) or both antigens separately (dual recognition; refs. 8 and 9). These models require a finite mobility and redistribution of the class I antigens on the cell surface. Considerations of a similar nature apply to other cell-cell interactions ...

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Section: Discussioncontrasting

confidence: 38%

Distribution and mobility of murine histocompatibility H-2Kk antigen in the cytoplasmic membrane.

Damjanovich¹,

Trón²,

Szöllősi³

et al. 1983

Proc. Natl. Acad. Sci. U.S.A.

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“…For these experiments, addition of the antibody to the cell surface was maintained at 4°C to limit antibody-mediated protein cross-linking (fig. S8) (29,30). We selected CD45, a highly abundant tyrosine phosphatase on T cell surfaces involved in antigen receptor signaling (31), as an initial target.…”

Section: Microenvironment Mapping On Cell Membranesmentioning

confidence: 99%

Microenvironment mapping via Dexter energy transfer on immune cells

Geri

Oakley

Reyes‐Robles

et al. 2020

Science

281

278

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Many disease pathologies can be understood through the elucidation of localized biomolecular networks, or microenvironments. To this end, enzymatic proximity labeling platforms are broadly applied for mapping the wider spatial relationships in subcellular architectures. However, technologies that can map microenvironments with higher precision have long been sought. Here, we describe a microenvironment-mapping platform that exploits photocatalytic carbene generation to selectively identify protein-protein interactions on cell membranes, an approach we term MicroMap (μMap). By using a photocatalyst-antibody conjugate to spatially localize carbene generation, we demonstrate selective labeling of antibody binding targets and their microenvironment protein neighbors. This technique identified the constituent proteins of the programmed-death ligand 1 (PD-L1) microenvironment in live lymphocytes and selectively labeled within an immunosynaptic junction.

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“…Patching and capping involves ligand-receptor binding causing association of receptor complexes (patching), followed by grouping of patches into large aggregates at one pole of cell (capping). Patching and capping of fluorescence antibody will appear as a concentrated spot of fluorescence on cell surface (Bourguignon, 1979). Antibody induced patching (Gaunt et ai, 1983) and capping (Trimmer and Vacquier, 1988), and shedding (Shaha, 1994) has been reported previously in sperm.…”

Section: Resultsmentioning

confidence: 78%

Selection of sex-specific aptamer probes to sperm

2008

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The author has granted a nonexclusive license allowing Library and Archives Canada to reproduce, publish, archive, preserve, conserve, communicate to the public by telecommunication or on the Internet, loan, distribute and sell theses worldwide, for commercial or noncommercial purposes, in microform, paper, electronic and/or any other formats.L'auteur a accorde une licence non exclusive permettant a la Bibliotheque et Archives Canada de reproduce, publier, archiver, sauvegarder, conserver, transmettre au public par telecommunication ou par I'lnternet, preter, distribuer et vendre des theses partout dans le monde, a des fins commerciales ou autres, sur support microforme, papier, electronique et/ou autres formats.Bien que ces formulaires aient inclus dans la pagination, il n'y aura aucun contenu manquant.

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Biochemical analysis of ligand-induced receptor patching and capping using a novel immunolactoperoxidase iodination technique.

Cited by 16 publications

References 20 publications

Distribution and mobility of murine histocompatibility H-2Kk antigen in the cytoplasmic membrane.

Distribution and mobility of murine histocompatibility H-2Kk antigen in the cytoplasmic membrane.

Microenvironment mapping via Dexter energy transfer on immune cells

Selection of sex-specific aptamer probes to sperm

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