B cell superantigens, also called immunoglobulin superantigens, bind to the variable regions of either the heavy or light chain of immunoglobulins mirroring the lymphocyte-activating properties of classical T cell superantigens. Protein A of , protein L of and gp120 of HIV are typical immunoglobulin superantigens. Mast cells are immune cells expressing the high-affinity receptor for IgE (FcεRI) and are strategically located in the human heart, where they play a role in several cardiometabolic diseases. Here, we investigated whether immunoglobulin superantigens induced the activation of human heart mast cells (HHMCs). Protein A induced the synthesis of cysteinyl leukotriene C (LTC) from HHMCs through the interaction with IgE V3 bound to FcεRI. Protein L stimulated the production of prostaglandin D (PGD) from HHMCs through the interaction with κ light chains of IgE. HIV glycoprotein gp120 induced the release of preformed (histamine) and synthesized mediators, such as cysteinyl leukotriene C (LTC), angiogenic (VEGF-A), and lymphangiogenic (VEGF-C) factors by interacting with the V3 region of IgE. Collectively, our data indicate that bacterial and viral immunoglobulin superantigens can interact with different regions of IgE bound to FcεRI to induce the release of proinflammatory, angiogenic, and lymphangiogenic factors from human cardiac mast cells.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6514993 | PMC |
| http://dx.doi.org/10.3390/ijms20081828 | DOI Listing |
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