Cell localization and redistribution of the 67 kD laminin receptor and alpha 6 beta 1 integrin subunits in response to laminin stimulation: an immunogold electron microscopy study.
Romanov, V.; Sobel, M. E.; pinto da Silva, P.et al.
1994 • In Cell Adhesion and Communication, 2 (3), p. 201-9
[en] The 67 kDa laminin receptor (67LR), one of several cell surface laminin-binding proteins, is involved in the interactions between cancer cells and laminin during tumor invasion and metastasis. A 37 kDa polypeptide (37LRP), previously identified as the 67LR precursor, is abundantly present in the cytoplasm and has been implicated in polysome formation. To better understand the cellular localization of the 67LR and its precursor, transmission electron microscopic studies of human melanoma A2058 cells were carried out using immunogold labeling and a variety of antibodies: (a) affinity purified antibodies directed against 37LRP cDNA-derived synthetic peptides; (b) anti-67LR monoclonal antibodies raised against intact human small cell lung carcinoma cells; and (c) monoclonal antibodies against the subunits of the integrin laminin receptor, alpha 6 beta 1. Double-labeling immunocyto-chemistry revealed that anti-67LR monoclonal antibodies as well as anti-37 LRP antibodies recognized antigens that were localized in the cytoplasm in electron dense structures. As expected, cell membrane labeling was also observed. Surprisingly, alpha 6 and beta 1 integrin subunits were detected in the same cytoplasmic structures positive for the 67LR and the 37LRP. After addition of soluble laminin to A2058 cells in suspension, the number of labeled cytoplasmic structures increased especially in the vicinity of the plasma membrane, and were exported onto the cell surface. Neither fibronectin nor BSA induced such an effect. The data demonstrate that the 67 LR and the 37 LRP antibodies detect colocalized antigens that are in cytoplasmic structures with alpha 6 beta 1 integrin.(ABSTRACT TRUNCATED AT 250 WORDS)
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Romanov, V.
Sobel, M. E.
pinto da Silva, P.
Menard, S.
Castronovo, Vincenzo ; Université de Liège - ULiège > Département des sciences biomédicales et précliniques > Biologie générale et cellulaire - GIGA-R : Labo de recherche sur les métastases
Language :
English
Title :
Cell localization and redistribution of the 67 kD laminin receptor and alpha 6 beta 1 integrin subunits in response to laminin stimulation: an immunogold electron microscopy study.
Auth D., Brawerman G. (1992) A 33-kDa polypeptide with homology to the laminin receptor: Component of translation machinery. Proc. Natl. Acad. Sci. USA 89:4368-4372.
Bendayan M. (1982) Double immunocytochemical labeling applying the protein A-gold technique. J. Histochem. Cytochem. 30:81-85.
Bendayan M., Zollinger M. (1983) Ultrastructural localization of antigenic sites on osmium-fixed tissues applying the protein A gold technique. J. Histochem. Cytochem. 31:101-109.
Bottini C., Miotti S., Fiorucci S., Facheris P., Menard S., Colnaghi M.I. (1993) Polarization of the α6β4 integrin in ovarian carcinomas. Int. J. Cancer 54:261-267.
Castronovo V. (1993) Laminin receptors and laminin binding proteins during tumor invasion and metastasis. Invasion Metastasis. 13:1-30.
Castronovo V., Claysmith A.P., Barker K.T., Cioce V., Krutzsch H.C., Sobel M.E. (1991) Biosynthesis of the 67 kDa high affinity laminin receptor. Biochem. Biophys.Res. Commun. 177:177-183.
Castronovo V., Colin C., Claysmith A.P., Chen P.H., Lifrange E., Lambotte R., Krutzsch H., Liotta L.A., Sobel M.E. (1990) Immunodetection of the metastasis-associated laminin receptor in human breast cancer cells obtained by fine-needle aspiration biopsy. Am. J. Pathol. 137:1373-1381.
Castronovo V., Taraboletti G., Sobel M.E. (1991) Laminin receptor complimentary DNA-deduced synthetic peptide inhibits cancer cell attachment to endothelium. Cancer Res. 51:5672-5678.
Castronovo V., Taraboletti G., Sobel M.E. (1992) Functional domains of the 67-kDa laminin receptor precursor. J. Biol. Chem. 267:17743-17747.
Cooper D.N.W., Barondes S.H. (1990) Evidence for export of a muscle lectin from cytosol to extracellular matrix and for novel secretory mechanism. J. Cell Biol. 110:1681-1691.
Davis S.C., Tzagoloff A., Ellis S.R. (1992) Characterization of a yeast mitochondrial ribosomal protein structurally related to the mammalian 68-kD high affinity laminin receptor. J. Biol. Chem. 267:5508-5514.
Keppel E., Schaller H.C. (1991) A 33 kDa protein with sequence homology to the “laminin binding protein” is associated with the cytoskeleton in hydra and in mammalian cells. J. Cell. Sci. 100:789-797.
Lesot R., Kuhl U., Von der Mark K. (1983) Isolation of a laminin binding protein from muscle cell membrane. EMBO J. 2:861-865.
Liotta L.A. (1986) Tumor invasion and metastasis: role of the extracellular matrix: Rhoads memorial award lecture. Cancer Res. 46:1-7.
Martignone S., Menard S., Bufalino R., Cascinelli N., Pellegrini R., Tagliabue E., Andreola S., Rilke F., Colnaghi M.I. (1993) Prognostic significance of the 67-kilodalton laminin receptor expression in human breast carcinomas. J. Natl. Cancer Inst. 85:398-402.
Martignone S., Pellegrini R., Villa E., Tandon N.N., Mastroianni A., Tagliabue E., Menard S., Colnaghi M.I. (1992) Characterization of two monoclonal antibodies directed against the 67 kDa high affinity laminin receptor and application for the study of breast carcinoma progression. Clin. Exp. Metastasis. 10:379-386.
McCafferty P., Neve R.L., Drager U.C. (1990) A dorsoventral asymmetry in the embryonic retina defined by protein conformation. Proc. Natl. Acad. Sci. USA 87:8570-8574.
Newman G.R. (1989) LR white embedding medium for colloidal gold methods. Colloidal Gold. M. A , Academic Press, M. A. Hayat ed., New York; 2:48-75.
Nicholson G.L. (1989) Metastatic tumor cell interactions with endothelium, basement membrane and tissue. Curr. Opin. Cell Biol. 1:1009-1019.
Pellegrini R., Bazzini P., Tosi E., Tagllabue E., Conforti G., Dejana E., Menard S., Colnaghi M.I. (1992) Production and characterization of two monoclonal antibodies directed against the integrin pi chain. Tumori. 78:1-4.
Singer I.I., Scott S., Kawka D.W., Kazazis D.M. (1989) Adhesomes: Specific granules containing receptors for laminin, C3bi/fibrinogen, fibronectin, and vitronectin in human polymorphonuclear leukocytes and monocytes. J. Cell Biol. 109:3169-3182.
Sonnenberg A., Modderman P.W., Hogervorst F. (1988) Laminin receptor on platelets is the integrin VLA-6. Nature 336:487-489.
Terranova V.P., Rao C.N., Kalebic T., Margulies I.M., Liotta L.A. (1983) Laminin receptor on human breast carcinoma cells. Proc. Natl. Acad. Sci. USA 80:444-448.
Timpl R., Rhode H., Gehron-Robey G., Renard M.N., Foidart J.M., Martin G.R. (1979) Laminin, a glycoprotein from basement membranes. J. Biol. Chem. 254:9933-9937.
Todaro G.J., Frybng C., De Larco J.E. (1990) Transforming growth factors produced by certain human tumor cells: polypeptides that interact with epidermal growth factor receptors. Proc. Natl. Acad. Sci. USA 77:5258-5262.
Wang K.S., Kuhn R.J., Strauss E.G., Ou S., Strauss J.H. (1992) High-affinity laminin receptor is a receptor for Sindbis virus in mammalian cells. J. Virol. 66:4992-5001.
Wewer U.M., Taraboletti G., Sobel M.E., Albrechtsen R., Liotta L.A. (1987) Role of laminin receptor in tumor cell migration. Cancer Res. 47:5691-5698.