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pubmed-article:9581863pubmed:abstractTextEven though the involvement of the 67-kDa laminin receptor (67LR) in tumor invasiveness has been clearly demonstrated, its molecular structure remains an open problem, since only a full-length gene encoding a 37-kDa precursor protein (37LRP) has been isolated so far. A pool of recently obtained monoclonal antibodies directed against the recombinant 37LRP molecule was used to investigate the processing that leads to the formation of the 67-kDa molecule. In soluble extracts of A431 human carcinoma cells, these reagents recognize the precursor molecule as well as the mature 67LR and a 120-kDa molecule. The recovery of these proteins was found to be strikingly dependent upon the cell solubilization conditions: the 67LR is soluble in NP-40-lysis buffer whereas the 37LRP is NP-40-insoluble. Inhibition of 67LR formation by cerulenin indicates that acylation is involved in the processing of the receptor. It is likely a palmitoylation process, as indicated by sensitivity of NP-40-soluble extracts to hydroxylamine treatment. Immunoblotting assays performed with a polyclonal serum directed against galectin3 showed that both the 67- and the 120-kDa proteins carry galectin3 epitopes whereas the 37LRP does not. These data suggest that the 67LR is a heterodimer stabilized by strong intramolecular hydrophobic interactions, carried by fatty acids bound to the 37LRP and to a galectin3 cross-reacting molecule.lld:pubmed
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pubmed-article:9581863pubmed:articleTitleFormation of the 67-kDa laminin receptor by acylation of the precursor.lld:pubmed
pubmed-article:9581863pubmed:affiliationDivision of Experimental Oncology E, Istituto Nazionale Tumori, Milan, Italy.lld:pubmed
pubmed-article:9581863pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9581863pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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