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Fig. 7. tTG interacts directly with LRP1 by means of the catalytic domain. (A) The interaction of purified LRP1 with tTG immobilized on plastic wells. Binding assays were performed as described in Materials and Methods in the presence or absence of the LRP1 interactor RAP. Immobilized BSA and RAP were used as negative and positive binding controls, respectively. (B) The interaction of purified tTG with LRP1 and soluble VLDL receptor (sVLDLR) immobilized on plastic wells. Binding assays were performed as described in Materials and Methods with BSA used as a negative binding control. Shown in (A,B) are the means ± s.d. for two independent experiments performed in triplicate. (C) LRP1 interacts with the second (catalytic) domain of tTG. Full-length tTG and its deletion mutants (Hang et al., 2005), all containing the C-terminal c-Myc tag, were expressed in NIH3T3 fibroblasts. Cell extracts were analyzed by SDS-PAGE and immunoblotting with antibody against c-Myc for total expression levels of full-length tTG and its deletion mutants (upper panel). LRP1 was immunoprecipitated from cell extracts with the rabbit antibody Rb2629, and the resulting LRP1 immune complexes were analyzed by SDS-PAGE and immunoblotting with antibody against c-Myc (lower panel). Molecular mass markers (kDa) are shown to the right of the gels.
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