Abstract
The mechanism whereby cytolytic lymphocytes protect themselves from killing mediated by their own cytotoxic protein, perforin, was studied. Perforin attached to killer lymphocyte surface in reversible manner even in the presence of Ca2+ while it bound to target cell surface in irreversible way. Moreover, the association rate constant for perforin-killer lymphocytes was different from that for perforin-target cells. These facts suggested that perforin binds to different molecule between on the killer cell membrane and target cell membrane. On the other hand, in killer lymphocytes treated with tunicamycin, an inhibitor of glycosylation, their resistance against perforin was significantly decreased. N-Glycosidase F-treated killer lymphocytes also lost their resistance ability against perforin. These findings suggested that certain carbohydrates of some glycoproteins at the cell surface are essentially important for protection of killer cell from perforin. Furthermore, some oligosaccharides such as 4-O-ß-Dgalactopyranosyl-D-galactopyranose and 4-O-ß-D-galactopyranosyl-D-fructose deactivated the perforin activity. These oligosaccharides had a same set of functions for hydrogen bond donor and acceptor.
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Eto, N. et al. (2002). Putative Protection Mechanism of CTL from Killing by Their Own Perforin. In: Shirahata, S., Teruya, K., Katakura, Y. (eds) Animal Cell Technology: Basic & Applied Aspects. Animal Cell Technology: Basic & Applied Aspects, vol 12. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0728-2_65
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DOI: https://doi.org/10.1007/978-94-017-0728-2_65
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