Abstract
Selected outer membrane polypeptides from Gram-negative bacteria are associated with lipopolysaccharide endotoxin (LPS) upon extraction of the organism by the trichloracetic acid method (1). This endotoxin associated protein (EP) when purified is known to be a potent polyclonal activator of B lymphocytes from mice and humans and can act as a potent adjuvant as well (2–4). However, the mechanism by which EP acts as an immunomodulator has not been elucidated. On the other hand, some of the early events initiated by the cross-linking of surface immunoglobulin on B cells have been described which are believed to be important for inducing DNA synthesis. Anti-sIg antibodies stimulate the turnover of phosphatidyl inositol (PI) leading to an increase in diacylglycerol (DAG) and inositol triphosphate (IP3) which, in turn, induce the activation of protein kinase C (PKC) and the release of intracellular Ca++, respectively (5). In contrast, LPS acts like a DAG analogue directly causing the translocation and activation of PKC without changes in PI or Ca++ ions (5).
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© 1992 Springer Science+Business Media New York
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Sultzer, B.M., Bandekar, J., Castagna, R., Abu-Lawi, K. (1992). Immunomodulation of C3H/HeJ Cells by Endotoxin Associated Protein and Lipopolysaccharide Endotoxin. In: Friedman, H., Klein, T.W., Yamaguchi, H. (eds) Microbial Infections. Advances in Experimental Medicine and Biology, vol 319. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-3434-1_5
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DOI: https://doi.org/10.1007/978-1-4615-3434-1_5
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