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We found that DSL and RCA I blotted PrPSc in all samples.
RCA I, recognized a smaller cluster of spots than both DSL and 6H4.
We next used DSL and RCA I to probe guanidinium protocol-purified PrPSc.
From this screening two lectins with affinity for PrPSc emerged, namely DSL and RCA I. DSL recognizes repeating N-acetyllactosamine [Gal β(1→4) GlcNAc] oligomers, whereas RCA I binds to terminal galactose (Gal) or N-acetylgalactosamine (GalNAc).
These data further confirm that DSL and RCA I recognize specifically PrPSc subpopulations and not other copurifying host glycoproteins.
In agreement with that, DSL and RCA I were previously reported to bind PrP in ELISAs [16], [17].
Similar(48)
RCA-I is a tetramer containing two non-covalently bonded ricin-like dimers.
Crude ricin extracts contain many other proteins such as the less toxic agglutinin or RCA-I and other superantigens [30].
Hence, the aforementioned effects of RCA-I on TNBC cell motilities were indeed specific for RCA-I.
We speculate that RCA-I inhibited the motilities of TNBC cells by blocking the metastasis-associated surface glycans and, hence, RCA-I might also have therapeutic potential.
As shown in Figure 5a, the invasion capability of all three cell lines was inhibited by RCA-I, particularly at the highest RCA-I concentration.
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