Distribution of Laminin Variants and Their Integrin Receptors in Human Secondary Lymphoid Tissue: Colocalization suggests that the α6β4-integrin is a receptor for laminin-5 in lymphoid follicles

References

• Aberdam D., Aguzzi A., Baudoin C., Galliano M. F., Ortonne J. P., Menguzzi G. Developmental expression of nicein adhesion protein (laminin-5) subunits suggests multiple morphogenic roles. Cell. Adh. and Comm 1994; 2: 115–129
   PubMed Web of Science ®Google Scholar
• Baudoin C., Miquel C., Blanchet-Bardon C., Gambini C., Meneguzzi G., Ortonne J. P. Herlitz junctional epidermolysis bullosa keratinocytes display heterogeneous defects of nicein/kalinin gene expression. J. Clin. Invest 1994; 93: 862–869
   PubMed Web of Science ®Google Scholar
• Beck K., Hunter I., Engel J. Structure and function of laminin: Anatomy of a multidomain glycoprotein. Faseb J 1990; 4: 148–160
   PubMed Web of Science ®Google Scholar
• Brown J. C., Spragg J. H., Wheeler G. N., Taylor P. W. Identification of the BI and B2 subunits of the placental laminin and rat parietal-yolk-sac laminin using antisera specific for murine laminin-β-galactosidase proteins. Biochem. J 1990; 270: 463–468
   PubMed Web of Science ®Google Scholar
• Burgeson R. E., Chiquet M., Deutzman R., Ekblom P., Engel J., Kleinman H., Martin G. R., Meneguzzi G., Paulsson M., Sanes J., Timpl R., Tryggvason K., Yamada Y., Yurchenco P. D. A new nomenclature for laminins. Matrix Biol 1994; 14: 209–211
   PubMed Web of Science ®Google Scholar
• Carter W., Ryan M., Gahr P. Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes. Cell 1991; 65: 599–610
   PubMed Web of Science ®Google Scholar
• De Sousa M., Tilney N. L., Kupiec-Weglinski J. W. Recognition of self within self: specific lymphocyte positioning and the extracellular matrix. Immunol. Today 1991; 12: 262–266
   PubMedGoogle Scholar
• Delwel G. O., De Melker A. A., Hogervorst F., Jaspars L. H., Fles D. L.A., Kuikman I., Lindblom A., Paulsson M., Timpl R., Sonnenberg A. Distinct and overlapping ligand specificities of the α3β1 and α6β1 integrins: recognition of laminin isoforms. Mol. Biol. Cell 1994; 5: 203–215
   PubMed Web of Science ®Google Scholar
• Delwel G. O., Hogervorst F., Kuikman I., Paulsson M., Timpl R., Sonnenberg A. Expression and function of the cytoplasmic variants of the integrin α6 subunit in transfected K562 cells. Activation-dependent adhesion and interaction with isoforms of laminin. J. Biol. Chem 1993; 268: 25865–25875
   PubMed Web of Science ®Google Scholar
• Delwel G. O., Sonnenberg A. Laminin isoforms and their integrin receptors. “In Adhesion recepters as therapeutic target.”, M. A. Horton. CRC Press, Boca Raton 1996; 36
   Google Scholar
• Engel J. Laminin and other strange proteins. Biochemistry 1992; 31: 10643–10651
   PubMed Web of Science ®Google Scholar
• Gloghini A., Carbone A. Dendritic reticulum cell-related immunostaining for laminin in follicular and diffuse B-cell lymphomas. Virchotivs Arch iv. A Pathol. Anat 1990; 416: 197–204
   PubMed Web of Science ®Google Scholar
• Hemler M. E., Ware C. F., Strominger J. L. Characterization of a novel differentiation antigen complex recognized by a monoclonal antibody (A-1A5): unique activation-specific molecular forms on stimulated T cells. J. Immunol 1983; 131: 334–340
   PubMed Web of Science ®Google Scholar
• Heusermann U., Zurborn K., Schroeder L., Stutte H. The origin of the dendritic reticulum cell; an experimental enzyme-histochemical and electron microscopic study on the rabbit spleen. Cell Tissue Res 1980; 202: 279–294
   Google Scholar
• Hsu S. M., Raine L., Fanger H. Use of avidin-biotinperoxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures. J. Histochem. Cytochem 1981; 29: 577–580
   PubMed Web of Science ®Google Scholar
• Imhof B. A., Ruiz P., Hesse B., Palacios R., Dunon D. EA-I, a novel adhesion molecule involved in the homing of progenitor T lymphocytes to the thymus. J. Cell. Biol 1991; 114: 1069–1078
   PubMed Web of Science ®Google Scholar
• Jaspars E. H., van der Linden J. C., Scheffer G. L., Scheper R. J., Meijer C. J.L.M. Monoclonal antibody 4C7 recognizes an endothelial basement membrane component that is selectively expressed in capillaries of lymphoid follicles. J. Pathol 1993; 170: 121–128
   PubMed Web of Science ®Google Scholar
• Jaspars L. H., Bloemena E., Bonnet P., van der Valk P., Meijer C. J.L.M. Distribution of extracellular matrix components and their receptors in human lymphoid tissue and B-cell non-Hodgkin lymphomas. Histopathology 1994; 26: 113–121
   Web of Science ®Google Scholar
• Kantor R. R.S., Mattes M. J., Lloyd K. O., Old L. J., Albino A. P. Biochemical analysis of two cell surface glycoprotein complexes. very common antigen 1 and very common antigen 2. J. Biol. Chem 1987; 262: 15158–15165
   PubMed Web of Science ®Google Scholar
• Kosco M. Germinal centers and the immune response. Res. Immunol 1991; 142: 219–282
   PubMedGoogle Scholar
• Kubota Y., Kleinman H., Martin G., Lawley T. Role of laminine and basement membrane in the morphological differentiation of human endothelial cells into capillary-like structures. J. Cell Biol 1988; 107: 1589–1598
   PubMed Web of Science ®Google Scholar
• Lawley T. J., Kubota Y. Induction of morphologic differentiation of endothelial cells in culture. J. Invest. Domatol 1989; 93: 59S–61S
   PubMed Web of Science ®Google Scholar
• Leanderson T., Kallenberg E., Gray D. Expansion. selection and mutation of antigen-specific B cells in germinal centers. Immunol. Rev 1992; 126: 47–61
   PubMed Web of Science ®Google Scholar
• Li Y. Y., Tak Cheung H. T. Basement membrane and its components on lymphocyte adhesion, migration and proliferation. J. Immunol 1992; 149: 3174–3181
   PubMed Web of Science ®Google Scholar
• Marinkovich M. P., Lunstrum G. P., Burgeson R. E. The anchoring filament protein kalinin is synthesized and sercreted as a high molecular weight precursor. J. Biol. Chem 1992; 267: 17900–17906
   PubMed Web of Science ®Google Scholar
• Niessen C. M., Hogervorst F., Jaspars L. H., De Melker A. A., Delwel G. O., Hulsman E. H.M., Kuikman I, Sonnenberg A. The α64bT4 integrin is a receptor for both laminin and kalinin. Esp. Cell Res 1994; 211: 360–367
   PubMed Web of Science ®Google Scholar
• Paulsson M., Deutzmann R., Timpl R., Dalzoppo D., Odermatt E., Engel J. Evidence for coiled-coil α-helical regions in the long arm of laminin. EMBO J 1985; 4: 309–316
   PubMed Web of Science ®Google Scholar
• Paulsson M., Saladin K., Engvall E. Structure of laminin variants. The 300-kDa chains of murine and bovine heart laminin are related to the human placenta merosin heavy chain and replace the A chain in some laminin variants. J. Biol. Chem 1991; 266: 17545–17551
   PubMed Web of Science ®Google Scholar
• Rademakers L. Follicular dendritic cells in germinal centre development. Res. Immunol 1991; 142: 257–260
   PubMedGoogle Scholar
• Rouselle P., Lunstrum G. P., Keene D. R., Burgeson R. E. Kalinin: an epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments. J. Cell Biol 1991; 114: 567–576
   PubMed Web of Science ®Google Scholar
• Ruiz P., Wiles M. V., Imhof B. A. α6 integrins participate in pro-T cell homing to the thymus. Eur J. Immunol 1995; 25: 2034–2041
   PubMed Web of Science ®Google Scholar
• Schwartzendruber D. Desmosomes in germinal centers of mouse spleen. Exp. Cell Res 1965; 40: 429–431
   PubMed Web of Science ®Google Scholar
• Shimizu Y., van Seventer G. A., Horgan K. J., Shaw S. Costimulation of proliferative responses of resting Cd4 + T cells by the interaction of VLA-4 and VLA-5 with fibronectin or VLA-6 with laminin. J. Immunol 1990; 145: 59–67
   PubMed Web of Science ®Google Scholar
• Sonnenberg A., Modderman P. W., Hogervorst F. Laminin receptor on platelets is the integrin VLA-6. Nature 1988; 360: 486–489
   Google Scholar
• Van den Berg T. K., van der Ende M., Dopp E. A., Kraal G., Dijkstra C. D. Localization of β1 integrins and their extracellular ligands in human lymphoid tissues. Am. J. Pathol 1993; 143: 1098–1110
   PubMed Web of Science ®Google Scholar
• Verrando P., Hsi B. L., Yeh C. J.G., Pisani A., Serieys N., Ortonne J. P. Monoclonal antibody GB3: a new probe for the study of human basement membranes and hemidesmosomes. Exp. Cell Res 1987; 170: 116–128
   PubMed Web of Science ®Google Scholar
• Verrando P., Pisani A., Ortonne J. P. The new basement membrane antigen recognized by the monoclonal antibody GB3 is a large size weight protein: modulation of its expression by retinoic acid. Biochim. Biofys. Acta 1988; 942: 45–56
   PubMed Web of Science ®Google Scholar
• Wayner E. A., Gil S. G., Murphy G. F., Wilke M. S., Carter W. G. Epiligrin. a component of epithelial basement membranes. is an adhesive ligand for α3β1 positive T lymphocytes. J. Cell Biol 1993; 121: 1141–1152
   PubMed Web of Science ®Google Scholar