Advertisement

Cell Adhesions and Signaling: A Tool for Biocompatibility Assessment

  • Roumen PankovEmail author
  • Albena Momchilova
Conference paper
  • 936 Downloads
Part of the NATO Science for Peace and Security Series A: Chemistry and Biology book series (NAPSA)

Abstract

Interactions between cells and extracellular environment are mediated through specific cell adhesion sites. These structures are responsible for transmitting environmental signals, which affect essentially all aspects of a cell’s life, including proliferation, differentiation and death. The morphology, organization and type of signaling transmitted through these adhesions depend on the chemical identity, geometry and the physical properties of the substrate. Here we outline the cell adhesions organized by fibroblasts on natural two- and within three-dimensional substrates, the signaling associated with these structures and discuss the possible use of this knowledge in assessment of surface biocompatibility of new materials, prepared for regenerative medicine.

Keywords

Cell adhesions Focal contacts Fibrillar adhesions Three-dimensional matrix adhesions Integrins Extracellular matrix Cell signaling Biocompatibility Nanomaterials 

Notes

Acknowledgements

This work was supported in part through grants BУ-Б-1/05 and 1404/04 by the Bulgarian National Fund for Scientific Research.

References

  1. Abercrombie M, Heaysman JE, Pegrum SM (1971) The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. Exp Cell Res 67:359–367CrossRefGoogle Scholar
  2. Alon R, Feigelson SW, Manevich E, Rose DM, Schmitz J, Overby DR, Winter E, Grabovsky V, Shinder V, Matthews BD, Sokolovsky-Eisenberg M, Ingber DE, Benoit M, Ginsberg MH (2005) Alpha4beta1-dependent adhesion strengthening under mechanical strain is regulated by paxillin association with the alpha4-cytoplasmic domain. J Cell Biol 171:1073–1084CrossRefGoogle Scholar
  3. Arnaout MA, Goodman SL, Xiong JP (2007) Structure and mechanics of integrin-based cell adhesion. Curr Opin Cell Biol 19:1–13CrossRefGoogle Scholar
  4. Badylak SF (2005) Regenerative medicine and developmental biology: the role of the extracellular matrix. Anat Rec B New Anat 287:36–41Google Scholar
  5. Bershadsky AD, Balaban NQ, Geiger B (2003) Adhesion-dependent cell mechanosensitivity. Annu Rev Cell Dev Biol 19:677–695CrossRefGoogle Scholar
  6. Bockholt SM, Burridge K (1993) Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin. J Biol Chem 268:14565–14567Google Scholar
  7. Bois PR, O’Hara BP, Nietlispach D, Kirkpatrick J, Izard T (2006) The vinculin binding sites of talin and alpha-actinin are sufficient to activate vinculin. J Biol Chem 281:7228–7236CrossRefGoogle Scholar
  8. Brakebusch C, Fassler R (2003) The integrin-actin connection, an eternal love affair. EMBO J 22:2324–2333CrossRefGoogle Scholar
  9. Brown RA, Phillips JB (2007) Cell responses to biomimetic protein scaffolds used in tissue repair and engineering. Int Rev Cytol 262:75–150CrossRefGoogle Scholar
  10. Calderwood DA (2004) Integrin activation. J Cell Sci 117:657–666CrossRefGoogle Scholar
  11. Chen WT, Singer SJ (1982) Immunoelectron microscopic studies of the sites of cell-substratum and cell-cell contacts in cultured fibroblasts. J Cell Biol 95:205–222CrossRefGoogle Scholar
  12. Clark K, Pankov R, Travis MA, Askari JA, Mould AP, Craig SE, Newham P, Yamada KM, Humphries MJ (2005) A specific α5β1-integrin conformation promotes directional integrin translocation and fibronectin matrix formation. J Cell Sci 118:291–300CrossRefGoogle Scholar
  13. Critchley DR (2000) Focal adhesions – the cytoskeletal connection. Curr Opin Cell Biol 12:133–139CrossRefGoogle Scholar
  14. Cukierman E, Pankov R, Stevens DR, Yamada KM (2001) Taking cell matrix adhesions to the third dimension. Science 294:1708–1712CrossRefGoogle Scholar
  15. Cukierman E, Pankov R, Yamada KM (2002) Cell interactions with three-dimensional matrices. Curr Opin Cell Biol 14:633–639CrossRefGoogle Scholar
  16. Damianova R, Stefanova N, Cukierman E, Momchilova A, Pankov R (2008) Three-dimensional matrix induces sustained activation of ERK1/2 via Src/Ras/Raf signaling pathway. Cell Biol Int 32:229–234CrossRefGoogle Scholar
  17. Edelman D, Keefer E (2005) A cultural renaissance: in vitro cell biology embraces three-dimensional context. Exp Neurol 192:1–6CrossRefGoogle Scholar
  18. Evans EA, Calderwood DA (2007) Forces and bond dynamics in cell adhesion. Science 316:1148–1153CrossRefGoogle Scholar
  19. Faucheux N, Tzoneva R, Nagel MD, Groth T (2006) The dependence of fibrillar adhesions in human fibroblasts on substratum chemistry. Biomaterials 27:234–245CrossRefGoogle Scholar
  20. Frisch SM, Francis H (1994) Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol 124:619–626CrossRefGoogle Scholar
  21. Geiger B, Bershadsky A (2001) Assembly and mechanosensory function of focal contacts. Curr Opin Cell Biol 13:584–592CrossRefGoogle Scholar
  22. Geiger B, Bershadsky A, Pankov R, Yamada KM (2001) Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat Rev Mol Cell Biol 2:793–805CrossRefGoogle Scholar
  23. Giancotti FG (2003) A structural view of integrin activation and signaling. Dev Cell 4:149–151CrossRefGoogle Scholar
  24. Giancotti FG, Tarone G (2003) Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annu Rev Cell Dev Biol 19:173–206CrossRefGoogle Scholar
  25. Gilmore AP, Burridge K (1996) Regulation of vinculin binding to talin and actin by phosphatidyl-inositol-4-5-bisphosphate. Nature 381:531–535CrossRefGoogle Scholar
  26. Glenney JR Jr, Zokas L (1989) Novel tyrosine kinase substrates from Rous sarcoma virus-transformed cells are present in the membrane skeleton. J Cell Biol 108:2401–2408CrossRefGoogle Scholar
  27. Halliday NL, Tomasek JJ (1995) Mechanical properties of the extracellular matrix influence fibronectin fibril assembly in vitro. Exp Cell Res 217:109–117CrossRefGoogle Scholar
  28. Hanks SK, Ryzhova L, Shin NY, Brabek J (2003) Focal adhesion kinase signaling activities and their implications in the control of cell survival and motility. Front Biosci 8:d982–d996CrossRefGoogle Scholar
  29. Hemmings L, Rees DJ, Ohanian V, Bolton SJ, Gilmore AP, Patel B, Priddle H, Trevithick JE, Hynes RO, Critchley DR (1996) Talin contains three actin-binding sites each of which is adjacent to a vinculin-binding site. J Cell Sci 109:2715–2726Google Scholar
  30. Hemmrich K, von Heimburg D (2006) Biomaterials for adipose tissue engineering. Expert Rev Med Devices 3:635–6345CrossRefGoogle Scholar
  31. Humphries MJ (2004) Monoclonal antibodies as probes of integrin priming and activation. Biochem Soc Trans 32:407–411CrossRefGoogle Scholar
  32. Humphries JD, Byron A, Humphries MJ (2006) Integrin ligands at a glance. J Cell Sci 119:3901–3903CrossRefGoogle Scholar
  33. Hynes RO (1987) Integrins: a family of cell surface receptors. Cell 48:549–554CrossRefGoogle Scholar
  34. Katti KS (2004) Biomaterials in total joint replacement. Colloids Surf B Biointerfaces 39:133–142CrossRefGoogle Scholar
  35. Katz BZ, Zamir E, Bershadsky A, Kam Z, Yamada KM, Geiger B (2000) Physical state of the extracellular matrix regulates the structure and molecular composition of cell-matrix adhesions. Mol Biol Cell 11:1047–1060Google Scholar
  36. Ling K, Doughman RL, Iyer VV, Firestone AJ, Bairstow SF, Mosher DF, Schaller MD, Anderson RA (2003) Tyrosine phosphorylation of type Igamma phosphatidylinositol phosphate kinase by Src regulates an integrin–talin switch. J Cell Biol 163:1339–1349CrossRefGoogle Scholar
  37. Lo SH, Janmey PA, Hartwig JH, Chen LB (1994) Interactions of tensin with actin and identification of its three distinct actin-binding domains. J Cell Biol 125:1067–1075CrossRefGoogle Scholar
  38. McCleverty CJ, Lin DC, Liddington RC (2007) Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions. Protein Sci 16:1223–1229CrossRefGoogle Scholar
  39. Molony L, Burridge K (1985) Molecular shape and self-association of vinculin and metavinculin. J Cell Biochem 29:31–36CrossRefGoogle Scholar
  40. Nair LS, Laurencin CT (2006) Polymers as biomaterials for tissue engineering and controlled drug delivery. Adv Biochem Eng Biotechnol 102:47–90Google Scholar
  41. Ohashi T, Kiehart DP, Erickson HP (2002) Dual labeling of the fibronectin matrix and actin cytoskeleton with green fluorescent protein variants. J Cell Sci 115:1221–1229Google Scholar
  42. Pankov R, Cukierman E, Katz B-Z, Matsumoto K, Lin DC, Lin S, Hahn C, Yamada KM (2000) Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis. J Cell Biol 148:1075–1090CrossRefGoogle Scholar
  43. Pankov R, Cukierman E, Clark K, Matsumoto K, Hahn C, LaFlamme SE, Poulin B, Yamada KM (2003) Specific β1 integrin site selectively regulates Akt/PKB signaling via local activation of PP2A. J Biol Chem 278:18671–18681CrossRefGoogle Scholar
  44. Rosales C, O’Brien V, Kornberg L, Juliano RL (1995) Signal transduction by cell adhesion receptors. Biochim Biophys Acta 1242:77–98Google Scholar
  45. Rottner K, Hall A, Small JV (1999) Interplay between Rac and Rho in the control of substrate contact dynamics. Curr Biol 9:640–648CrossRefGoogle Scholar
  46. Schaller MD (2001) Paxillin: a focal adhesion-associated adaptor protein. Oncogene 20:6459–6472CrossRefGoogle Scholar
  47. Shimaoka M, Takagi J, Springer TA (2002) Conformational regulation of integrin structure and function. Annu Rev Biophys Biomol Struct 31:485–516CrossRefGoogle Scholar
  48. Thiery JP (2003) Cell adhesion in development: a complex signaling network. Curr Opin Gen Dev 13:365–371CrossRefGoogle Scholar
  49. Turner CE (2000) Paxillin interactions. J Cell Sci 113:4139–4140Google Scholar
  50. Tzoneva R, Faucheux N, Groth T (2007) Wettability of substrata controls cell-substrate and cell-cell adhesions. Biochim Biophys Acta 1770:1538–1547CrossRefGoogle Scholar
  51. Webb DJ, Donais K, Whitmore LA, Thomas SM, Turner CE, Parsons TF, Horwitz AF (2004) FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat Cell Biol 6:154–161CrossRefGoogle Scholar
  52. Zaidel-Bar R, Itzkovitz S, Ma’ayan A, Iyengar R, Geiger B (2007a) Functional atlas of the integrin adhesome. Nat Cell Biol 9:858–867CrossRefGoogle Scholar
  53. Zaidel-Bar R, Milo R, Kam Z, Geiger B (2007b) A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J Cell Sci 120:137–148CrossRefGoogle Scholar
  54. Zamir E, Katz BZ, Aota S, Yamada KM, Geiger B, Kam Z (1999) Molecular diversity of cell-matrix adhesions. J Cell Sci 112:1655–1669Google Scholar

Copyright information

© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.Sofia University “St. Kliment Ohridski”SofiaBulgaria
  2. 2.Laboratory of Cell and Developmental Biology, National Institute of Dental and Craniofacial ResearchNational Institutes of HealthBethesdaUSA
  3. 3.Department of Cytology, Histology and Embryology, Faculty of BiologySofia UniversitySofiaBulgaria
  4. 4.Institute of Biophysics, Bulgarian Academy of SciencesSofiaBulgaria

Personalised recommendations