Journal of Biomechanics
Volume 38, Issue 3 , Pages 433-443 , March 2005

Estimation of the binding force of the collagen molecule-decorin core protein complex in collagen fibril

,Accepted 27 April 2004.

References 

  1. Bella J, Eaton M, Brodsky B, Berman HM. Crystal and molecular structure of a collagen-like peptide at 1.9Å resolution. Science. 1994;266:75–81
  2. Brodsky B, Ramshaw JAM. The collagen triple-helix structure. Matrix Biology. 1997;15:545–554
  3. Brodsky B, Shah NK. The triple helix motif in proteins. FASEB Journal. 1995;9:1537–1546
  4. Butler DL, Grood ES, Noyes FR, Zernicke RF, Brackett K. Effects of structure and strain measurement technique on the material properties of young human tendons and fascia. Journal of Biomechanics. 1984;17:579–596
  5. Butler DL, Kay MD, Stouffer DC. Comparison of material properties in fascicle-bone units from human patellar tendon and knee ligaments. Journal of Biomechanics. 1986;19:425–432
  6. Chopra RK, Pearson CH, Pringle GA, Fackre DS, Scott PG. Dermatan sulphate is located on serine-4 of bovine skin proteodermatan sulphate. Demonstration that most molecules possess only one glycosaminoglycan chain and comparison of amino acid sequences around glycosylation sites in different proteoglycans. Biochemical Journal. 1985;15:277–279
  7. Craig AS, Birtles MJ, Conway JF, Parry DAD. An estimate of the mean length of collagen fibrils in rat tail-tendon as a function of age. Connective Tissue Research. 1989;19:51–62
  8. Danielson KG, Baribault H, Holmes DF, Graham H, Kadler KE, Iozzo RV. Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility. Journal of Cell Biology. 1997;136:729–743
  9. Elliott DM, Robinson PS, Gimbel JA, Sarver JJ, Abboud JA, Iozzo RV, et al. Effect of altered matrix proteins on quasilinear viscoelastic properties in transgenic mouse tail tendons. Annals of Biomedical Engineering. 2003;31:599–605
  10. Folkhard W, Mosler E, Geercken E, Knorzer H, Nemetschek-Gansler H, Nemetschek T. Quantitative analysis of the molecular sliding mechanism in native tendon collagen—time-resolved dynamic studies using synchrotron radiation. International Journal of Biological Macromolecules. 1987;9:169–175
  11. Fraser RDB, MacRae TP, Suzuki E. Chain confirmation in the collagen molecule. Journal of Molecular Biology. 1979;129:463–481
  12. Fratzl P, Misof K, Zizak I. Fibrillar structure and mechanical properties of collagen. Journal of Structural Biology. 1997;122:119–122
  13. Graham HK, Holmes DF, Watson RB, Kadler KE. Identification of collagen fibril fusion during vertebrate tendon morphogenesis; the process relies on unipolar fibrils and is regulated by collagen–proteoglycans interaction. Journal of Molecular Biology. 2000;295:891–902
  14. Hocking AM, Shinomura T, McQuillan DJ. Leucine-rich repeat glycoproteins of the extracellular matrix. Matrix Biology. 1998;17:1–19
  15. Jarvelainen HT, Kinsella MG, Wight TN, Sandell LJ. Differential expression of small chondroitin/dermatan sulfate proteoglycans, PG-I/biglycan and PG-II/decorin, by vascular smooth muscle and endothelial cells in culture. Journal of Biological Chemistry. 1991;266:23274–23281
  16. Jenkins CL, Raines RT. Insights on the conformational stability of collagen. Natural Product Reports. 2002;19:49–59
  17. Kadler KE, Holmes DF, Trotter JA, Chapman JA. Collagen fibril formation. Biochemical Journal. 1996;316:1–11
  18. Keene DR, San Antonio JD, Mayne R, McQuillan DJ, Sarris G, Santoro SA, et al. Decorin binds near the c terminus of type I collagen. Journal of Biological Chemistry. 2000;276:21801–21804
  19. Kobe B, Deisenhofer J. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature. 1993;366:751–756
  20. Kobe B, Deisenhofer J. A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature. 1995;374:183–186
  21. Kramer RZ, Vitagliano L, Bella J, Berisio R, Mazzarella L, Brodsky B, et al. X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly). Journal of Molecular Biology. 1998;280:623–638
  22. Kramer RZ, Bella J, Brodsky B, Berman HM. The crystal and molecular structure of a collagen-like peptide with a biologically relevant sequence. Journal of Molecular Biology. 2001;311:131–147
  23. Krusius T, Ruoslahti E. Primary structure of an extracellular matrix proteoglycan core protein deduced from cloned cDNA. Proceedings of the National Academy of Sciences of the USA. 1986;83:7683–7687
  24. Lan Y, Cummings C, Sheehan JK, Kadler KE, Holmes DF, Chapman JA. Visualization of individual proteoglycan–collagen interactions. In:  Scott JE editors. Dermatan Sulphate Proteoglycans: Chemistry, Biology, Chemical Pathology. London: Portland Press; 1993;p. 183–188
  25. McBride DJ, Trelstad RL, Silver FH. Structural and mechanical assessment of developing chick tendon. International Journal of Biological Macromolecules. 1988;10:194–200
  26. Mosler E, Folkhard W, Knorzer E, Nemetschek-Gansler H, Nemetschek T, Koch MHJ. Stress-induced molecular rearrangement in tendon collagen. Journal of Molecular Biology. 1985;182:589–596
  27. Ottani V, Raspanti M, Ruggeri A. Collagen structure and functional implications. Micron. 2001;32:251–260
  28. Ottani V, Martini D, Franchi M, Ruggeri A, Raspanti M. Hierarchical structures in fibrillar collagens. Micron. 2002;33:587–596
  29. Parry DAD, Craig AS. Growth and development of collagen fibrils in connective tissue. In:  Ruggeri A,  Motta PM editor. Ultrastructure of the Connective Tissue Matrix. Boston: Martinus Nijhoff; 1984;p. 34–64
  30. Petruska JA, Hodge AJ. A subunit model for the tropocollagen macromolecule. Proceedings of the National Academy of Sciences of the United States of America. 1964;51:871–876
  31. Pins GD, Christiansen DL, Patel R, Silver FH. Self-assembly of collagen fibers. Influence of fibrillar alignment and decorin on mechanical properties. Biophysical Journal. 1997;73:2164–2172
  32. Ramachandran GN, Kartha G. Structure of collagen. Nature. 1954;174:269–270
  33. Raspanti M, Alessandrini A, Ottani V, Ruggeri A. Direct visualization of collagen-bound proteoglycans by tapping-mode atomic force microscopy. Journal of Structural Biology. 1997;119:118–122
  34. Raspanti M, Congiu T, Alessandrini A, Gobbi P, Ruggeri A. Different patterns of collagen–proteoglycan interaction (a scanning electron microscopy and atomic force microscopy study). European Journal of Histochemistry. 2000;44:335–343
  35. Raspanti M, Congiu T, Guizzardi S. Structural aspects of the extracellular matrix of tendon (an atomic force and scanning electron microscopy study). Archives of Histology and Cytology. 2002;65:37–43
  36. Redaelli A, Vesentini S, Soncini M, Vena P, Mantero S, Montevecchi FM. The possible role of decorin glycosaminoglycans in fibril to fibril force transfer in relative mature tendons—a computational study from molecular to microstructural level. Journal of Biomechanics. 2003;36:1555–1569
  37. Rosenberg LC, Choi HU, Tang LH, Johnson TL, Pal S, Webber C, et al. Isolation of dermatan sulfate proteoglycans from mature bovine articular cartilages. Journal of Biological Chemistry. 1985;260:6304–6313
  38. Schönherr E, Hausser H, Beavans L, Kresse H. Decorin-type I collagen interaction. Presence of separate core protein-binding domains. Journal of Biological Chemistry. 1995;270:8877–8883
  39. Scott JE. Proteoglycan-fibrillar collagen interactions. Biochemical Journal. 1988;252:313–323
  40. Scott JE. Supramolecular organization of extracellular matrix glycosaminoglycans, in vitro and in the tissues. FASEB Journal. 1992;6:2639–2645
  41. Scott JE. Proteodermatan and proteokeratan sulfate (decorin, lumican/fibromodulin) proteins are horseshoe shaped. Implications for their interactions with collagen. Biochemistry. 1996;35:8795–8799
  42. Scott JE. Structure and function in extracellular matrices depend on interactions between anionic glycosaminoglycans. Pathologie Biologie. 2001;49:284–289
  43. Scott JE, Orford CR. Dermatan sulphate-rich proteoglycan associates with rat tail-tendon collagen at the d band in the gap region. Biochemical Journal. 1981;197:213–216
  44. Scott JE, Ritchie M, Glanville RW, Cronshaw AD. Peptide sequences in glutaraldehyde-linked proteodermatan sulphate (collagen fragments from rat tail tendon locate the proteoglycan binding sites). Biochemical Society Transactions. 1997;25:S663
  45. Svensson L, Heinegård D, Oldberg Å. Decorin-binding site for collagen type I are mainly located in leucine-rich repeats 4-5. Journal of Biological Chemistry. 1995;270:20712–20716
  46. Tenni R, Viola M, Wesler F, Sini P, Giudici C, Rossi A, et al. Interaction of decorin with cnbr peptides from collagens I and II. Evidence for multiple binding site and essential lysyl residues in collagen. European Journal of Biochemistry. 2002;269:1428–1437
  47. Trotter JA, Wofsy C. The length of collagen fibrils in tendons. Transactions of the Orthopaedic Research Society. 1989;14:180
  48. Weber IT, Harrison RW, Iozzo RV. Model structure of decorin and implications for collagen fibrillogenesis. Journal of Biological Chemistry. 1996;271:31767–31770
  49. Weiner SJ, Kollman PA, Nguyen DT, Case DA. An all atom force field for simulations of proteins and nucleic acids. Journal of Computational Chemistry. 1986;7:230–252
  50. Woo SL, Gomez MA, Amiel D, Ritter MA, Gelberman RH, Akeson WH. The effects of exercise on the biomechanical and biochemical properties of swine digital flexor tendons. Transaction of ASME. Journal of Biomechanical Engineering. 1981;103:51–56

PII: S0021-9290(04)00216-7

doi: 10.1016/j.jbiomech.2004.04.032

Journal of Biomechanics
Volume 38, Issue 3 , Pages 433-443 , March 2005

Article Tools

* Image Usage & Resolution