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- W1567350729 abstract "Abstract The yolk protein, vitellogenin, is sequestered by the developing oocyte by receptor-mediated endocytosis, the process by which cells bind and internalize extracellular proteins. Endocytosis of a variety of proteins follows a similar pathway, whereby internalization of receptor-bound ligand takes place over clathrin-coated regions of the cell membrane. The protein crosslinking enzyme, transglutaminase, has been reported to be essential for the receptor-mediated endocytosis of insulin and α2-macroglobulin. In this study, the presence of transglutaminase activity was demonstrated in the Xenopus laevis ovary and was effectively inhibited by poly L-lysine, an inhibitor of vitellogenin uptake, and dansylcadaverine, a known inhibitor of transglutaminase activity. Two other less poteint inhibitors of transglutaminase, methylamine and bacitracin produced partial inhibition of the ovarian enzyme. Furthermore, dansylcadaverine and methylamine were found to inhibit the appearance of vitellogenin in the yolk platelets of the oocyte." @default.
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- W1567350729 date "1981-03-01" @default.
- W1567350729 modified "2023-09-23" @default.
- W1567350729 title "Evidence for the involvement of transglutaminase in the uptake of vitellogenin by Xenopuslaevis oöcytes" @default.
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- W1567350729 doi "https://doi.org/10.1016/0006-291x(81)91735-6" @default.
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