• We are sorry, but NCBI web applications do not support your browser and may not function properly. More information
Logo of annrheumdAnnals of the Rheumatic DiseasesCurrent TOCInstructions for authors
Ann Rheum Dis. Oct 1987; 46(10): 734–740.
PMCID: PMC1003379

Fibronectin and immune complexes in rheumatic diseases.

Abstract

The relation between fibronectin and immune complexes in rheumatic disease was examined in a series of linked studies. Fibronectin was present in immune complexes formed in vitro in the absence of C1q. Gel filtration chromatography showed complexed fibronectin was present in the serum of a patient with rheumatoid vasculitis, but not in normal serum; the complexed fibronectin coeluted with IgA and C3. Two dimensional immunoelectrophoresis showed a single fibronectin component was present in normal serum, but a number of components were present in serum from a rheumatoid patient. Polyacrylamide gel electrophoresis followed by immunoblotting for fibronectin showed that polyethylene glycol precipitates of synovial fluid contained immunoreactive components of a variety of sizes, indicating the presence of fragments of the molecule. An analysis of fibronectin in polyethylene glycol precipitates of paired serum and synovial fluid samples from 17 patients with rheumatoid arthritis and 16 with osteoarthritis showed more fibronectin was present in rheumatoid samples, especially in synovial fluid. More fibronectin was also present in synovial fluid than in serum polyethylene glycol precipitates; there was no direct relationship with C1q levels. All these results suggest that fibronectin is an integral component of immune complexes. This has potential pathogenic significance because it shows that a product of connective tissue cells may influence the functions of the immune system.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (1.3M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.

Images in this article

Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Coppock JS, Scott DL, Carter SD, Moreland TM, Robinson MW. Fibronectin in polyethylene glycol precipitates: evidence for a role in immune complexes. Rheumatol Int. 1986;6(2):79–83. [PubMed]
  • Sorvillo J, Gigli I, Pearlstein E. Fibronectin binding to C1q associated with antigen-antibody complexes in EDTA-treated plasma. Scand J Immunol. 1986 Feb;23(2):153–160. [PubMed]
  • Yamada KM, Olden K. Fibronectins--adhesive glycoproteins of cell surface and blood. Nature. 1978 Sep 21;275(5677):179–184. [PubMed]
  • Mosesson MW, Amrani DL. The structure and biologic activities of plasma fibronectin. Blood. 1980 Aug;56(2):145–158. [PubMed]
  • Ruoslahti E, Engvall E, Hayman EG. Fibronectin: current concepts of its structure and functions. Coll Relat Res. 1981;1(1):95–128. [PubMed]
  • Mosher DF. Fibronectin. Prog Hemost Thromb. 1980;5:111–151. [PubMed]
  • Pierschbacher MD, Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature. 1984 May 3;309(5963):30–33. [PubMed]
  • Molnar J, Gelder FB, Lai MZ, Siefring GE, Jr, Credo RB, Lorand L. Purification of opsonically active human and rat cold-insoluble globulin (plasma fibronectin). Biochemistry. 1979 Sep 4;18(18):3909–3916. [PubMed]
  • Saba TM, Jaffe E. Plasma fibronectin (opsonic glycoprotein): its synthesis by vascular endothelial cells and role in cardiopulmonary integrity after trauma as related to reticuloendothelial function. Am J Med. 1980 Apr;68(4):577–594. [PubMed]
  • Simpson AW, Boughton BJ. Fibronectin as an opsonic regulator of monocyte phagocytosis. J Clin Pathol. 1984 Jul;37(7):787–789. [PMC free article] [PubMed]
  • Anderson B, Rucker M, Entwistle R, Schmid FR, Wood GW. Plasma fibronectin is a component of cryoglobulins from patients with connective tissue and other diseases. Ann Rheum Dis. 1981 Feb;40(1):50–54. [PMC free article] [PubMed]
  • Scott DL, Almond TJ, Naqvi SN, Lea DJ, Stone R, Walton KW. The significance of fibronectin in cryoprecipitation in rheumatoid arthritis and other diseases. J Rheumatol. 1982 Jul-Aug;9(4):514–518. [PubMed]
  • Scott DL, Bedford PA, Walton KW. The preparation of plasma fibronectin antigen and antiserum. J Immunol Methods. 1981;43(1):29–33. [PubMed]
  • Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC. Measurement of protein using bicinchoninic acid. Anal Biochem. 1985 Oct;150(1):76–85. [PubMed]
  • Selmer J, Eriksen H, Clemmensen I. Native and degraded fibronectin: new immunological methods for distinction. Scand J Clin Lab Invest. 1984 Feb;44(1):57–63. [PubMed]
  • Scott DL, Farr M, Crockson AP, Walton KW. Synovial fluid and plasma fibronectin levels in rheumatoid arthritis. Clin Sci (Lond) 1982 Jan;62(1):71–76. [PubMed]
  • Clarke HG, Freeman T. Quantitative immunoelectrophoresis of human serum proteins. Clin Sci. 1968 Oct;35(2):403–413. [PubMed]
  • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. [PubMed]
  • Schwarzbauer JE, Paul JI, Hynes RO. On the origin of species of fibronectin. Proc Natl Acad Sci U S A. 1985 Mar;82(5):1424–1428. [PMC free article] [PubMed]
  • Oldberg A, Ruoslahti E. Evolution of the fibronectin gene. Exon structure of cell attachment domain. J Biol Chem. 1986 Feb 15;261(5):2113–2116. [PubMed]
  • Carsons S, Mosesson MW, Diamond HS. Detection and quantitation of fibronectin in synovial fluid from patients with rheumatic disease. Arthritis Rheum. 1981 Oct;24(10):1261–1267. [PubMed]
  • Scott DL, Carter SD, Coppock JS, Robinson M, Walton KW. Differences between plasma and synovial fluid fibronectin. Rheumatol Int. 1985;5(2):49–54. [PubMed]
  • Carnemolla B, Cutolo M, Castellani P, Balza E, Raffanti S, Zardi L. Characterization of synovial fluid fibronectin from patients with rheumatic inflammatory diseases and healthy subjects. Arthritis Rheum. 1984 Aug;27(8):913–921. [PubMed]
  • Carsons S, Lavietes BB, Diamond HS, Kinney SG. The immunoreactivity, ligand, and cell binding characteristics of rheumatoid synovial fluid fibronectin. Arthritis Rheum. 1985 Jun;28(6):601–612. [PubMed]
  • Yamada KM, Schlesinger DH, Kennedy DW, Pastan I. Characterization of a major fibroblast cell surface glycoprotein. Biochemistry. 1977 Dec 13;16(25):5552–5559. [PubMed]
  • McDonald JA, Baum BJ, Rosenberg DM, Kelman JA, Brin SC, Crystal RG. Destruction of a major extracellular adhesive glycoprotein (fibronectin) of human fibroblasts by neutral proteases from polymorphonuclear leukocyte granules. Lab Invest. 1979 Mar;40(3):350–357. [PubMed]
  • Furie MB, Rifkin DB. Proteolytically derived fragments of human plasma fibronectin and their localization within the intact molecule. J Biol Chem. 1980 Apr 10;255(7):3134–3140. [PubMed]
  • Humphries MJ, Ayad SR. Stimulation of DNA synthesis by cathepsin D digests of fibronectin. Nature. 305(5937):811–813. [PubMed]
  • Savill CM, Ayad SR. The mitogenic activity of a heparin-binding fibronectin fragment (Mr 35,000) produced by cathepsin D digestion. Anticancer Res. 1986 Mar-Apr;6(2):321–326. [PubMed]
  • Bykowska K, Wegrzynowicz Z, Lopaciuk S, Kopeć M. Effect of proteolysis on quantitation of plasma fibronectin concentration by two immunoassays (electroimmunoassay and immunoturbidimetric technique). Thromb Haemost. 1985 Jun 24;53(3):377–380. [PubMed]
  • Bing DH, Almeda S, Isliker H, Lahav J, Hynes RO. Fibronectin binds to the C1q component of complement. Proc Natl Acad Sci U S A. 1982 Jul;79(13):4198–4201. [PMC free article] [PubMed]
  • Pearlstein E, Sorvillo J, Gigli I. The interaction of human plasma fibronectin with a subunit of the first component of complement, C1q. J Immunol. 1982 May;128(5):2036–2039. [PubMed]
  • Reid KB, Edmondson J. Location of the binding site in subcomponent C1q for plasma fibronectin. Acta Pathol Microbiol Immunol Scand Suppl. 1984;284:11–17. [PubMed]
  • Bevilacqua MP, Amrani D, Mosesson MW, Bianco C. Receptors for cold-insoluble globulin (plasma fibronectin) on human monocytes. J Exp Med. 1981 Jan 1;153(1):42–60. [PMC free article] [PubMed]
  • Walton KW, Almond TJ, Robinson M, Scott DL. An experimental model for the study of the opsonic activity of fibronectin in the clearance of intravascular complexes. Br J Exp Pathol. 1984 Apr;65(2):191–200. [PMC free article] [PubMed]
  • Hautanen A, Keski-Oja J. Affinity of myeloma IgG proteins for fibronectin. Clin Exp Immunol. 1983 Jul;53(1):233–238. [PMC free article] [PubMed]
  • Siri A, Balza E, Carnemolla B, Castellani P, Borsi L, Zardi L. DNA-binding domains of human plasma fibronectin. pH and calcium ion modulation of fibronectin binding to DNA and heparin. Eur J Biochem. 1986 Feb 3;154(3):533–538. [PubMed]
  • Hautanen A, Keski-Oja J. Interaction of fibronectin with complement component C3. Scand J Immunol. 1983 Mar;17(3):225–230. [PubMed]
  • Proctor RA, Prendergast E, Mosher DF. Fibronectin mediates attachment of Staphylococcus aureus to human neutrophils. Blood. 1982 Apr;59(4):681–687. [PubMed]
  • Eriksen HO, Espersen F, Clemmensen I. Opsonic activity of fibronectin in the phagocytosis of Staphylococcus aureus by polymorphonuclear leukocytes. Eur J Clin Microbiol. 1984 Apr;3(2):108–112. [PubMed]

Articles from Annals of the Rheumatic Diseases are provided here courtesy of BMJ Group

Formats:

Related citations in PubMed

See reviews...See all...

Cited by other articles in PMC

See all...

Links

  • MedGen
    MedGen
    Related information in MedGen
  • PubMed
    PubMed
    PubMed citations for these articles
  • Substance
    Substance
    PubChem Substance links

Recent Activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...