Article (Scientific journals)
Formation of the 67-kDa laminin receptor by acylation of the precursor.
Buto, S.; Tagliabue, E.; Ardini, E. et al.
1998In Journal of Cellular Biochemistry, 69 (3), p. 244-51
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Keywords :
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
Abstract :
[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.
Disciplines :
Oncology
Biochemistry, biophysics & molecular biology
Author, co-author :
Buto, S.
Tagliabue, E.
Ardini, E.
Magnifico, A.
Ghirelli, C.
van den Brule, F.
Castronovo, Vincenzo ;  Université de Liège - ULiège > 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.
Language :
English
Title :
Formation of the 67-kDa laminin receptor by acylation of the precursor.
Publication date :
1998
Journal title :
Journal of Cellular Biochemistry
ISSN :
0730-2312
eISSN :
1097-4644
Publisher :
Wiley Liss, Inc.
Volume :
69
Issue :
3
Pages :
244-51
Peer reviewed :
Peer Reviewed verified by ORBi
Funders :
AIRF/FIRC
Available on ORBi :
since 28 September 2009

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