Reference : Formation of the 67-kDa laminin receptor by acylation of the precursor.
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
Human health sciences : Oncology
http://hdl.handle.net/2268/24098
Formation of the 67-kDa laminin receptor by acylation of the precursor.
English
Buto, S. [> > > >]
Tagliabue, E. [> > > >]
Ardini, E. [> > > >]
Magnifico, A. [> > > >]
Ghirelli, C. [> > > >]
van den Brule, F. [> > > >]
Castronovo, Vincenzo mailto [Université de Liège - ULg > Département des sciences biomédicales et précliniques > Biologie générale et cellulaire - GIGA-R : Labo de recherche sur les métastases >]
Colnaghi, M. I. [> > > >]
Sobel, M. E. [> > > >]
Menard, S. [> > > >]
1998
Journal of Cellular Biochemistry
Wiley Liss, Inc.
69
3
244-51
Yes (verified by ORBi)
International
0730-2312
1097-4644
[en] Acylation ; Antigens, Differentiation/chemistry ; Cell Line ; Chromatography, Affinity ; Dimerization ; Epitopes/chemistry ; Fatty Acids/antagonists & inhibitors/biosynthesis ; Galectin 3 ; Humans ; Hydroxylamine/chemistry ; Laminin/metabolism ; Protein Precursors/chemistry/metabolism ; Receptors, Laminin/biosynthesis/chemistry/metabolism ; Solubility
[en] Even 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.
AIRF/FIRC
http://hdl.handle.net/2268/24098

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