Summary
Binding of fibronectins (FN) to collagen types I–IV were studied using polyclonal antibodies against human and chicken FNs, proteoglycan monomers, collagen type II and monoclonal antibodies reacting with both soluble and insoluble forms of human FN. Plasma fibronectin and type II collagen were shown to interact specifically in a homologous system. Type II collagen, however, proved to be less effective in inhibition assays compared to other types of collagen.
In high density cultures of chicken limb bud cells, fibronectin was first localized within the fibroblast-like cells of 4 hr cultures and an extensive extracellular filamentous net-work developed by the end of day 1. Fibronectin was present in the newly formed cartilage nodules although it seemed to disappear by day 6, when the proteoglycan accumulation became more intensive. Enzyme treatments (testicular hyaluronidase, chondroitinase ABC) helped to localize FN at this stage of development of chicken cartilage, in microdroplet high density cultures of human fetal chondrocytes and in articular cartilage. Fibronectin was localized only in the pericellular ring of intact human articular cartilage using monoclonal antibodies with the biotin-avidin system.
Similar content being viewed by others
References
Atherton BT, Hynes RO (1981) A difference between plasma and cellular fibronectins located with monoclonal antibodies. Cell 25:133–141
Carnemolla B, Cutolo M, Castellani P, Balza E, Raffanti S, Zardi L (1984) Characterization of synovial fluid fibronectin from patients with rheumatic inflammatory diseases and healthy subjects. Arthritis Rheum 27:913–921
Chandrasekhar S, Sorrentino JA, Millis AJT (1983) Interaction of fibronectin with collagen: Age-specific defect in the biological activity of human fibroblast fibronectin. Proc Natl Acad Sci USA 80:4747–4751
Clemmensen I, Holund B, Johansen N, Andersen RB (1982) Demonstration of fibronectin in human articular cartilage by an indirect immunoperoxidase technique. Histochemistry 76: 51–56
Dessau W, Sasse F, Timpl R, Filek F, Vonder Mark K (1978) Synthesis and extracellular deposition of fibronectin in chondrocyte cultures. Response to the removal of extracellular cartilage matrix. J Cell Biol 79:342–355
Engvall E Ruoslahti E (1977) Binding of soluble form of fibroblast surface protein, fibronectin, to collagen. Int J Cancer 20:1–5
Epstein EH Jr (1974) [α1(III)]3 human skin collagen. Release by pepsin digestion and preponderance in fetal life. J Biol Chem 249:3225–3231
Evans HB, Ayad S, Abedin MZ, Hopkins S, Morgan K, Walton KW, Weiss JB, Holt PJL (1983) Localisation of collagen types and fibronectin in cartilage by immunofluorescence. Ann Rheum Dis 42:575–581
Fazekas de St. Groth S, Scheidegger D (1980) Production of monoclonal antibodies: strategy and tactics. J Immunol Methods 35:1–21
Fisher WD, Golds EE, van der Rest M, Cooke TD, Lyons HE, Poole AR (1982) Stimulation of collagenase secretion from rheumatoid synovial tissue by human collagen peptides. J Bone Joint Surg B 48:546–557
Glant T (1982a) Induction of cartilage degradation in experimental arthritis produced by allogeneic and xenogeneic proteoglycan antigens. Connect Tissue Res 9:137–144
Glant T (1982b) The concanavalin A-binding link protein in the proteoglycan aggregate of hyaline cartilage. Biochem Biophys Res Commun 106:158–163
Glant T, Lèvai G (1983) Localization of antigenic components in proteoglycan aggregate of bovine nasal cartilage. Histochemistry 77:217–232
Glant T, Mikecz K (1985) Antigenic profile of human, bovine and canine articular chondrocytes. J Bone Joint Surg A (Submitted for publication)
Glant T, Lèvai G, Hadhàzy CS (1977) The localization of proteoglycans and glycoproteins in the hyaline cartilage. Histochemistry 53:291–299
Glant T, Hadas E, Nagy M (1979), Cell-mediated and humoral immune responses to cartilage antigenic components. Scand J Immunol 9:39–44
Glant T, Csongor J, Szücs T (1980) Immunopathologic role of proteoglycan antigens in rheumatoid joint diseases. Scand J Immunol 11:247–252
Gold LI, Pearlstein E (1980) Fibronectin-collagen binding and requirement during cellular adhesion. Biochem J 186:551–559
Hadhàzy CS, Làszlò MB, Kostenszky, KS (1982) Cartilage differentiation in micro-mass cultures of chicken limb bud. Acta Morphol Acad Sci Hung 30:65–78
Hamburger V, Hamilton HL (1951) A series of normal stages in the development of the chicken embryo. J Morphol 88:49–92
Hayashi M, Yamada KM (1981) Differences in domain structures between plasma and cellular fibronectins. J Biol Chem 256:11292–11300
Hedman K, Johansson S, Vartio T, Kjellen L, Vaheri A, Hook M (1982) Structure of the pericellular matrix: association of heparan and chondroitin sulfates with fibronectin-procollagen fibers. Cell 28:663–671
Hewitt AT, Kleinman HK, Pennypacker JP, Martin GR (1980) Identification of an adhesive factor for chondrocytes. Proc Natl Acad Sci USA 77:385–388
Hirano H, Yamada Y, Sullivan M, DeCrombrugghe B, Pastan I, Yamada KM (1983) Isolation of genomic DNA clones spanning the entire fibronectin gene. Proc Natl Acad Sci USA 80:46–50
Hynes RO (1981) Fibronectin and its relation to cellular structure and behaviour. In: Hay ED (ed) Cell biology of extracellular matrix. Academic Press. New York London, pp 295–334
Kornblihtt AR, Vibre-Pedersen K, Baralle FE (1983) Isolation and characterization of cDNA clones for human and bovine fibronectins. Proc Natl Acad Sci USA 80:3218–3222
Köhler G, Milstein C (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256: 495–497
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685
Lattera J, Culp LA (1982) Differences in hyaluronate binding to plasma and cell surface fibronectin. J Biol Chem 257:719–726
Mackel AM, DeLustro F, LeRoy EC (1981) Cell-mediated immunity to homologous basement membrane (type IV) collagen in C57 BL/6 mice. Clin Immunol Immunopathol 21:204–216
Mauger A, Demarchez M, Herbage D, Grimaud J-A, Druguei M, Hartmann DJ, Foidart J-M, Sengel P (1983) Immunofluorescent localization of collagen types I, III, IV, fibronectin and laminin during morphogenesis of scales and scaleless skin in the chick embryo. Roux's Arch Dev Biol 192:205–215
Miller EJ (1972) Structural studies on cartilage collagen employing limited cleavage and solubilization with pepsin. Biochemistry 11:4903–4909
Oi VT, Herzenberg LZ (1980) In: Mishell BB, Shiigi SM (eds) Selected methods in cellular immunology Freeman, San Francisco, CA, pp 351–372
Oldberg A, Ruoslahti E (1982) Interactions between chondroitin sulfate proteoglycan, fibronectin and collagen. J Biol Chem 217:4859–4863
Petersen TE, Thgersen HC, Skorstengaard K, Vibe-Pedersen K, Sahl P, Sottrup-Jensen L, Magnusson S (1983) Partial primary structure of bovine plasma fibronectin: three types of internal homology. Proc Natl Acad Sci USA 80:137–141
Poole AR (1983) Complexity of proteoglycan organization in articular cartilage: recent observations. J Rheumatol (Suppl 11) 10:70–74
Rich AM, Pearlstein E, Weissmann G Hoffstein ST (1981) Cartilage proteoglycans inhibit fibronectin mediated adhesion. Nature 293:224–226
Ruoslahti E, Vaheri A (1975) Interaction of soluble fibroblast surface antigen with fibronectin and fibrin. Identify with coldinsoluble globulin of human plasma. J Exp Med 141:497–501
Sckiguchi K, Hakomori-S-i, Funahashi M, Matsumoto I, Seno N (1983) Binding of fibronectin and its proteolytic fragments to glycosaminoglycans. Exposure of cryptic glycosaminoglycan-binding domains upon limited proteolysis. J Biol Chem 258:14359–14365
Sipos A, Glant T, Hadházy CS (1983) Interaction between collagen type II and plasma fibronectin. Fibronectin in the cartilage (abstract). The XIIth Symposium of the European Society of Osteoartherology, Debrecen, pp 94
Thesleff I, Barrach HJ, Foidart JM, Vaheri A, Pratt RM, Martin GR (1981) Changes in the distribution of type IV collagen, laminin, proteoglycan and fibronectin during mouse tooth development. Dev Biol 81:182–192
Towbin H, Staehelin T, Gordon J (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350–4354
Vartio T, Vaheri A (1983) Fibronectin: chains of domain with diversified functions. TIBS 8:442–444
Weiss RE, Reddi AH (1981a) Appearance of fibronectin during the differentiation of cartilage, bone and bone marrow. J Cell Biol 88:630–636
Weiss RE, Reddi AH (1981b) Isolation and charaterization of rat plasma fibronectin. Biochem J 197: 529–534
Wurster NB, Lust G (1982) Fibronectin in osteoarthritic canine articular cartilage. Biochem Biophys Res Commun 109: 1094–1101
Yamada KM (1981) Fibronectin and other structural proteins. In: Hay ED (ed) Cell biology of extracellular matrix. Academic Press, New York London, pp 95–119
Yamada KM (1982) Biochemistry of fibronectin. In: The glycoconjugates, Vol III Academic Press, New York London, pp 331–362
Yamada SS, Yamada KM, Willingham MC (1980) Intracellular localization of fibronectin by immunoelectron microscopy. J Histochem Cytochem 28:953–960
Zola H, Brooks D (1982) Techniques for the production and characterization of monoclonal hybridoma antibodies. In: Hurrell JGR (ed) Monoclonal hybridoma antibodies: techniques and applications. CRC Press, Boca Raton, Florida, pp 1–57
Author information
Authors and Affiliations
Additional information
Please send offprint request to: Dr. Tibor T. Glant (until April Joint Diseases Laboratory, Shriners Hospital for Crippled Children, 1529 Cedar Avenue, Montreal, Quebec, Canada, H3G 1A6
Rights and permissions
About this article
Cite this article
Glant, T.T., Hadházy, C., Mikecz, K. et al. Appearance and persistence of fibronectin in cartilage. Histochemistry 82, 149–158 (1985). https://doi.org/10.1007/BF00708199
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00708199