Words similar to co-immunoprecipitate
Example sentences for: co-immunoprecipitate
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Studies have shown that the sitosterolemic patients hyperabsorb all sterols (cholesterol and phytosterols) and fail to excrete phytosterols into bile [ 3 4 5 6 7 ] . Positional mapping of the STSL locus to human chromosome 2p21 led to the identification of two genes, ATP binding cassette (ABC) half-transporters G5 and G8 that were mutated in affected individuals [ 8 9 10 11 12 ] . The protein products of these two genes (sterolin-1 and sterolin-2 respectively) are thought to form heterodimers to constitute a functional transporter, based primarily on the genetic evidence that affected individuals are either completely mutated in sterolin-1 or sterolin-2, but not both [ 12 ] . More recently, evidence from in vitro expression of these proteins has been presented that these two proteins co-immunoprecipitate, supporting this conclusion [ 13 ] . ABCG5 and ABCG8 appear to be present in all mammalian genomes examined to date and are highly conserved between species, indicating that these genes may have a similar function in other species.
Similarly, GPI-linked proteins such as CD 109, TM4SF proteins such as CD81, and other transmembrane proteins such as CD147/EMMPRIN can be found at substantial levels in light membrane fractions [ 44 45 ] , and our unpublished results), and these also did not co-immunoprecipitate with CD98 (Fig.
However, the Src inhibitor, PP1 or the expression of a dominant-negative Src mutant, will reduce GPCR-mediated transphosphorylation of the EGFR and GPCR-mediated ERK activation to varying degrees (partial to total), suggesting that at least two different tyrosine kinases can be involved [ 18 ] . Src was found to co-immunoprecipitate with the phosphorylated EGFR in COS-7 cells exposed to either LPA or EGF [ 14 ] . These authors reported that the autophosphorylation of Y350 in the EGFR does not occur after LPA exposure, suggesting that c-Src is the principal tyrosine kinase in this instance and not the EGFR's intrinsic tyrosine kinase.
Though caveolin is present in the same fractions as CD98-integrin complexes, it does not co-immunoprecipitate with CD98 under these conditions (not shown) and thus is not part of integrin-CD98 complexes.
Src has also been found to co-immunoprecipitate with the agonist-stimulated β 2 -AR during the period of ERK activation [ 8 ] . Our previous work [ 11 13 ] suggested that a Src-like protein tyrosine kinase was primarily responsible for tyrosine phosphorylation of the δ-OR and ERK activation induced by DTLET when the receptor was expressed in CHO or HEK-293 cells, because both responses were blocked by the presence of 50 μM PP1.
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