Human plasma and cerebrospinal fibronectins differ in the accessibility of the epitopes on the N-terminal domains

• Authors: Małgorzata Pupek , Anna Lemańska-Perek , Jolanta Jasonek , Iwona Kątnik-Prastowska
• Languages of publication: EN

Abstracts

EN

Three monoclonal antibodies specific to the central cell-binding and the C- and N-terminal domains of fibronectin (FN) were used to test antigenic epitope accessibility on human plasma and cerebrospinal fibronectins. In the plasma group, the mean N-terminal FN domain immunoreactivity was about one fourth that of the cell-binding and C-terminal domains, whereas in cerebrospinal fluid they were nearly equal. In the presence of 0.5-6 M urea N-terminal domain immunoreactivity in the plasma increased 3-6-fold, but it decreased 0.7-3-fold in the cerebrospinal fluid. Analysis of fibronectin domain immunoreactivities of the cell-binding and N-terminal domains by a panel of specific monoclonal antibodies may reveal N-terminal fibronectin domain accessibility for reaction with biological partner ligand(s) and/or processes in which FN could be implicated. Such determinations may have important clinical implications.

Keywords

EN

cerebrospinal fluid; cell-binding fibronectin domain; N-terminal fibronectin domain; C-terminal fibronectin domain; fibronectin

• Journal: Acta Biochimica Polonica
• Year: 2010
• Volume: 57
• Issue: 3
• Pages: 333-337

Dates

published

2010

received

2010-02-01

revised

2010-05-18

accepted

2010-06-08

(unknown)

2010-08-19

Contributors

author

Małgorzata Pupek

• Department of Chemistry and Immunochemistry, Medical University of Wrocław, Wrocław, Poland

author

Anna Lemańska-Perek

• Department of Chemistry and Immunochemistry, Medical University of Wrocław, Wrocław, Poland

author

Jolanta Jasonek

• Department and Clinic of Pediatrics and Infectious Diseases, Medical University of Wrocław, Wrocław, Poland

author

Iwona Kątnik-Prastowska

• Department of Chemistry and Immunochemistry, Medical University of Wrocław, Wrocław, Poland

References

• Baneyx G, Baugh L, Vogel V (2002) Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc Natl Acad Sci 99: 5139-5143.
• Brown PD, Davies SL, Speake T, Millar ID (2004) Molecular mechanisms of cerebrospinal fluid production. Neuroscience 129: 957-970.
• Cukierman E, Pankov R, Yamada KM (2002) Cell interactions with three-dimensional matrices. Curr Opin Cell Biol 14: 633-639.
• Ffrench-Constant C (1995) Alternative splicing of fibronectin - many different proteins but few different functions. Exp Cell Res 221: 261-271.
• Hirnle L, Kątnik-Prastowska I (2007) Amniotic fibronectin fragmentation and domain and sialyl- and fucosyl-glycotope expression associated with pregnancy complicated by intrauterine infection. Clin Chem Lab Med 45: 208-214.
• Hynes RO (1999) The dynamic dialogue between cells and matrices: implications of fibronectin's elasticity. Proc Natl Acad Sci USA 96: 2588-2590.
• Ito H, Rucker E, Steplewski A, McAdams E, Brittingham RJ, Alabyeva T, Fertala A (2005) Guilty by association: some collagen II mutants alter the formation of ECM as a result of atypical interaction with fibronectin. J Mol Biol 352: 382-395.
• Johnson KJ, Sage H, Briscoe G, Erickson HP (1999) The compact conformation of fibronectin is determined by intramolecular ionic interactions. J Biol Chem 274: 15473-15479.
• Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
• Lairez D, Pauthe E, Pelta J (2003) Refolding of a high molecular weight protein: salt effect on collapse. Biophys J 84: 3904-3916.
• Liesi P, Kirkwood T, Vaheri A (1986) Fibronectin is expressed by astrocytes cultured from embryonic and early postnatal rat brain. Exp Cell Res 163: 175-185.
• Magnusson MK, Mosher DF (1998) Fibronectin: structure, assembly, and cardiovascular implications. Arterioscler Thromb Vasc Biol 18: 1363-1370.
• Makogonenko E, Ingham KC, Medved L (2007) Interaction of the fibronectin COOH-Terminal Fib-2 regions with fibrin: further characterization and localization of the Fib-2 binding sites. Biochemistry 46: 5418-5426.
• Mao Y, Schwarzbauer JE (2005) Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol 24: 389-399.
• Moretti FA, Chauhan AK, Iaconcig A, Porro F, Baralle FE, Muro AF (2007) A major fraction of fibronectin present in the extracellular matrix of tissues is plasma-derived. J Biol Chem 282: 28057-28062.
• Nelea V, Nakano Y, Kaartinen MT (2008) Size distribution and molecular associations of plasma fibronectin and fibronectin crosslinked by transglutaminase 2. Protein J 27: 223-233.
• Olszowski S, Olszowska E, Kusior D, Piwowarczyk M, Stelmaszyńska T (2003) Hypochlorite action on plasma fibronectin promotes its extended conformation in complex with antibodies. J Protein Chem 22: 449-456.
• Pankov R, Yamada KM (2002) Fibronectin at a glance. J Cell Sci 115: 3861-3863.
• Patel S, Chaffotte AF, Amana B, Goubard F, Pauthe E (2006) In vitro denaturation-renaturation of fibronectin. Formation of multimers disulfide-linked and shuffling of intramolecular disulfide bonds. Int J Biochem Cell Biol 38: 1547-1560.
• Plata K, Rosato AE, Węgrzyn G (2009) Staphylococcus aureus as an infectious agent: overview of biochemistry and molecular genetics of its pathogenicity. Acta Biochim Pol 56: 597-612.
• Pupek M, Krzyżanowska-Gołąb D, Dyła T, Lemańska-Perek A, Jankowska R, Kątnik-Prastowska I (2009) Presence of high-molecular-weight forms and domain alterations of fibronectin in pleural effusion of patients with lung cancer. Clin Biochem 42: 654-661.
• Sakai K, Fujii T, Hayashi T (1996) Conformational change precedes the formation of multimeric fibronectin. J Biochem 119: 58-62.
• Sedor FA (2000) Body fluid analysis. In Clinical chemistry: principles, procedures, correlations. Bishop ML, Duben-Engelkirk JL, Fody EP, eds, pp 477-89. Lippincott Williams & Willkins, Philadelphia.
• Spitzfaden C, Grant RP, Mardon HJ, Campbell ID (1997) Module-module interactions in the cell binding region of fibronectin: stability, flexibility and specificity. J Mol Biol 265: 565-579.
• Torre D, Zeroli C, Ferrario G, Bonetta G, Fiori GP, Martegani R (1993) Cerebrospinal fluid concentration of fibronectin in patients with HIV-1 infection and central nervous system disorders. J Clin Pathol 46: 1039-1041.
• 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: 56350-4354.
• Vakonakis I, Campbell ID (2007) Extracellular matrix: from atomic resolution to ultrastructure. Curr Opin Cell Biol 19: 578-583.
• Vakonakis I, Staunton D, Ellis IR, Sarkies P, Flanagan A, Schor AM, Schor SL, Campbell ID (2009) Motogenic sites in human fibronectin are masked by long range interactions. J Biol Chem 284: 15668-15675.
• Vakonakis I, Staunton D, Rooney LM, Campbell ID (2007) Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis. EMBO J 26: 2575-2583.
• Vogel V, Thomas WE, Craig DW, Krammer A, Baneyx G (2001) Structural insights into the mechanical regulation of molecular recognition sites. Trends Biotechnol 19: 416-423.
• Yi M, Sakai T, Fassler R, Ruoslahti E (2003) Antiangiogenic proteins require plasma fibronectin or vitronectin for in vivo activity. Proc Natl Acad Sci USA 100: 11435-11438.