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TIMP1 binds LRP1. 27 / 28
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"Indeed, we and others have reported that TIMP-1 directly bound to LRP-1 at the plasma membrane of mouse cortical neurons, leading to cell morphology changes XREF_BIBR, XREF_BIBR."
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"ELISA to analyse binding of TIMP-1 to LRP-1."
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"The results confirmed that all TIMPs bind to LRP1 ( xref ) with binding affinities ranging from 23 nM to 33 nM for various TIMPs ( xref )."
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"The K D values we measured for TIMP-1 binding to LRP1 is similar to the reported binding affinity for TIMP-1 to cluster II of LRP1 XREF_BIBR, XREF_BIBR while the K D values we measured for TIMP-3 binding to LRP1 is similar to earlier reports 54."
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"TIMP-1 complex binds to LRP with high affinity and that the binding determinant for LRP appears to reside on MMP-9."
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"To gain insight into the interaction between TIMP-1 and LRP-1, we considered conformational changes that occur when a ligand binds to its receptor."
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"In this study, we combined NMA and MD simulations with biological experiments to gain insight into the TIMP-1 and LRP-1 interaction."
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"The data obtained using in silico simulations and biological experiments highlight the relevance of protein dynamics in the TIMP-1 and LRP-1 interaction and associated biological effects."
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"The K D values we measured for TIMP-1 binding to LRP1 is similar to the reported binding affinity for TIMP-1 to cluster II of LRP1 xref , xref while the K D values we measured for TIMP-3 binding to LRP1 is similar to earlier reports xref ."
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"We have thus hypothesised that the alteration of these properties could modify the TIMP-1 and LRP-1 interaction and associated cellular effects."
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"We have thus combined NMA and MD simulations with biological experiments to characterise the TIMP-1 and LRP-1 interaction."
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"We next examined the binding of TIMP-1, TIMP-2, TIMP-3, and TIMP-4 to LRP1 by measuring equilibrium binding to LRP1 using SPR."
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"Although Hahn-Dantona et al. failed to demonstrate a direct interaction between TIMP-1 and LRP-1 in their in vitro study [XREF_BIBR], our unpublished data reveal that LRP-1 could bind and endocytose TIMP-1 in neurons, in an MMP independent way."
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"Consequently, the use of molecular docking tools is not appropriate for studying the TIMP-1 and LRP-1 interaction."
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"Intriguingly, although both TIMP-1 mutants bound to LRP-1, F12A and K47A mutations prevented the biological effects associated with the TIMP-1 and LRP-1 interaction."
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"Thus, proMMP-9 and TIMP-1 directly interacts with LRP-1, leading to its endocytic uptake and degradation by lysosomal proteases [XREF_BIBR]."
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"The results of these experiments reveal that, in addition to proMMP-1 (XREF_FIG), both active MMP-1 (XREF_FIG) and the MMP-1 and TIMP-1 complex (XREF_FIG) also bind to LRP1."
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"Interestingly, MMP-1 and TIMP-1 complexes bind to LRP1 with approximately 30-fold increased affinity (K D = 0.6 +/- 0.2 nM) over that of proMMP-1 (K D = 19 +/- 1 nM) or active MMP-1 (K D = 25 +/- 2 nM)."
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"Characterising TIMP-1 and LRP-1 interaction could thus be of physiological relevance in the treatment of certain neurodegenerative disorders."
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"Binding of monomeric and trimeric proMMP-9 to LRP-1, LRP-2 and TIMP-1."
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"In an ELISA assay, TIMP-1 bound to LRP-1 with a K D, App of 16nM, in agreement with previous reports 40."
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"The characterisation of the TIMP-1 and LRP-1 interaction could be physiologically relevant in some neurodegenerative disorders."
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"TIMP-1 complex binds to LRP with high affinity and that the binding determinant for LRP appears to reside on MMP-9."
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"The activity of MMPs are regulated by their TIMP inhibitors, and while proMMP-1, active MMP-1 and TIMP-1 bind to LRP1 with K D values of 19 nM, 25 nM, and 23 nM, respectively, our data reveal that the MMP-1 and TIMP-1 complex binds with approximately 30-fold higher affinity to LRP1 (K D = 0.6 nM) than either component alone."
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"Interestingly, the MMP-1 and TIMP-1 complex bound to LRP1 with 30-fold higher affinity (K D = 0.6 nM) than either component alone, revealing that LRP1 prefers the protease : inhibitor complex as a ligand."
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"We have thus hypothesised that alteration of these protein dynamics could modify the TIMP-1 and LRP-1 interaction."
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"Taken together, these results suggest that TIMP-1 binding to LRP-1 is followed by a TIMP-1 conformational change, which is required for its endocytosis and cellular effects."
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