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Arthritis
Volume 2013 (2013), Article ID 154812, 30 pages
http://dx.doi.org/10.1155/2013/154812
Review Article

Defects in Tendon, Ligament, and Enthesis in Response to Genetic Alterations in Key Proteoglycans and Glycoproteins: A Review

Arthritis Program, Division of Orthopaedic Surgery, Toronto Western Hospital, Toronto, ON, Canada M5T 2S8

Received 22 May 2013; Accepted 7 August 2013

Academic Editor: Ruben Burgos-Vargas

Copyright © 2013 Subhash C. Juneja and Christian Veillette. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. H. Yoon and J. Halper, “Tendon proteoglycans: biochemistry and function,” Journal of Musculoskeletal Neuronal Interactions, vol. 5, no. 1, pp. 22–34, 2005. View at Scopus
  2. A. Malmström, B. Bartolini, M. A. Thelin, B. Pacheco, and M. Maccarana, “Iduronic acid in chondroitin/dermatan sulfate: biosynthesis and biological function,” Journal of Histochemistry & Cytochemistry, vol. 60, pp. 916–925, 2012.
  3. L. W. Ruddock and M. Molinari, “N-glycan processing in ER quality control,” Journal of Cell Science, vol. 119, no. 21, pp. 4373–4380, 2006. View at Publisher · View at Google Scholar · View at Scopus
  4. P. Kannus, “Structure of the tendon connective tissue,” Scandinavian Journal of Medicine and Science in Sports, vol. 10, no. 6, pp. 312–320, 2000. View at Scopus
  5. L. Jozsa and P. Kannus, Eds., Human Tendons: Anatomy, Physiology, and Pathology, Human Kinetics, Champaign, III, USA, 1997.
  6. S. Fukuta, M. Oyama, K. Kavalkovich, F. H. Fu, and C. Niyibizi, “Identification of types II, IX and X collagens at the insertion site of the bovine Achilles tendon,” Matrix Biology, vol. 17, no. 1, pp. 65–73, 1998. View at Publisher · View at Google Scholar · View at Scopus
  7. C. M. McNeilly, A. J. Banes, M. Benjamin, and J. R. Ralphs, “Tendon cells in vivo form a three dimensional network of cell processes linked by gap junctions,” Journal of Anatomy, vol. 189, no. 3, pp. 593–600, 1996. View at Scopus
  8. M. Benjamin and D. McGonagle, “Entheses: tendon and ligament attachment sites,” Scandinavian Journal of Medicine and Science in Sports, vol. 19, no. 4, pp. 520–527, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. M. P. G. Bostrom, A. Boskey, J. K. Kauffman, and T. A. Einhorn, “Form and function of bone,” in Orthopaedic Basic Science, J. A. Buckwalter, T. A. Einhorn, and S. R. Simon, Eds., pp. 319–370, AAOS, Rosement, Ill, USA, 2000.
  10. S. L. Woo, K. An, C. B. Frank et al., “Anatomy, biology, and biomechanics of tendon and ligament,” in Orthopaedic Basic Science, J. A. Buckwalter, T. A. Einhorn, and S. R. Simon, Eds., pp. 581–616, AAOS, Rosement, Ill, USA, 2000.
  11. R. M. Jones, Mechanics of Composite Materials, Taylor & Francis, Philadelphia, Pa, USA, 1999.
  12. S. Thomopoulos, G. M. Genin, and L. M. Galatz, “The development and morphogenesis of the tendon-to-bone insertion—what development can teach us about healing,” Journal of Musculoskeletal Neuronal Interactions, vol. 10, no. 1, pp. 35–45, 2010. View at Scopus
  13. M. Benjamin and J. R. Ralphs, “Fibrocartilage in tendons and ligaments—an adaptation to compressive load,” Journal of Anatomy, vol. 193, no. 4, pp. 481–494, 1998. View at Publisher · View at Google Scholar · View at Scopus
  14. M. R. Capecchi, “Targeted gene replacement,” Scientific American, vol. 270, no. 3, pp. 52–59, 1994. View at Scopus
  15. F. Recillas-Targa, “Multiple strategies for gene transfer, expression, knockdown, and chromatin influence in mammalian cell lines and transgenic animals,” Molecular Biotechnology, vol. 34, no. 3, pp. 337–354, 2006. View at Publisher · View at Google Scholar · View at Scopus
  16. C. R. Scriver, A. L. Beaudet, W. S. Sly, and D. Valle, Eds., The Metabolic & Molecular Bases of Inherited Disease, vol. 1–4, McGraw-Hill, New York, NY, USA, 8th edition, 2001.
  17. H. Lango and M. N. Weedon, “What will whole genome searches for susceptibility genes for common complex disease offer to clinical practice?” Journal of Internal Medicine, vol. 263, no. 1, pp. 16–27, 2008. View at Publisher · View at Google Scholar · View at Scopus
  18. L. Schaefer and R. V. Iozzo, “Biological functions of the small leucine-rich proteoglycans: from genetics to signal transduction,” Journal of Biological Chemistry, vol. 283, no. 31, pp. 21305–21309, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Chakravarti, R. L. Stallings, N. SundarRaj, P. K. Cornuet, and J. R. Hassell, “Primary structure of human lumican (keratan sulfate proteoglycan) and localization of the gene (LUM) to chromosome 12q21.3-q22,” Genomics, vol. 27, no. 3, pp. 481–488, 1995. View at Publisher · View at Google Scholar · View at Scopus
  20. S. Chakravarti, T. Magnuson, J. H. Lass, K. J. Jepsen, C. LaMantia, and H. Carroll, “Lumican regulates collagen fibril assembly: skin fragility and corneal opacity in the absence of lumican,” Journal of Cell Biology, vol. 141, no. 5, pp. 1277–1286, 1998. View at Publisher · View at Google Scholar · View at Scopus
  21. R. V. Iozzo, “The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins,” Journal of Biological Chemistry, vol. 274, no. 27, pp. 18843–18846, 1999. View at Publisher · View at Google Scholar · View at Scopus
  22. A.-M. K. Säämänen, H. J. Salminen, A. J. Rantakokko, D. Heinegård, and E. I. Vuorio, “Murine fibromodulin: cDNA and genomic structure, and age-related expression and distribution in the knee joint,” Biochemical Journal, vol. 355, no. 3, pp. 577–585, 2001. View at Scopus
  23. M. V. Nurminskaya and D. E. Birk, “Differential expression of fibromodulin mRNA associated with tendon fibril growth: isolation and characterization of a chicken fibromodulin cDNA,” Biochemical Journal, vol. 317, no. 3, pp. 785–789, 1996. View at Scopus
  24. S. Kalamajski and Å. Oldberg, “Fibromodulin binds collagen type I via Glu-353 and Lys-355 in leucine-rich repeat 11,” Journal of Biological Chemistry, vol. 282, no. 37, pp. 26740–26745, 2007. View at Publisher · View at Google Scholar · View at Scopus
  25. S. Kalamajski and Å. Oldberg, “Homologous sequence in Lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding,” Journal of Biological Chemistry, vol. 284, no. 1, pp. 534–539, 2009. View at Publisher · View at Google Scholar · View at Scopus
  26. Y. Ezura, S. Chakravarti, A. Oldberg, I. Chervoneva, and D. E. Birk, “Differential expression of lumican and fibromodulin regulate collagen fibrillogenesis in developing mouse tendons,” Journal of Cell Biology, vol. 151, no. 4, pp. 779–788, 2000. View at Publisher · View at Google Scholar · View at Scopus
  27. L. Svensson, A. Aszódi, F. P. Reinholt, R. Fässler, D. Heinegård, and Å. Oldberg, “Fibromodulin-null mice have abnormal collagen fibrils, tissue organization, and altered lumican deposition in tendon,” Journal of Biological Chemistry, vol. 274, no. 14, pp. 9636–9647, 1999. View at Publisher · View at Google Scholar · View at Scopus
  28. K. J. Jepsen, F. Wu, J. H. Peragallo et al., “A syndrome of joint laxity and impaired tendon integrity in lumican- and fibromodulin-deficient mice,” Journal of Biological Chemistry, vol. 277, no. 38, pp. 35532–35540, 2002. View at Publisher · View at Google Scholar · View at Scopus
  29. S. Kalamajski and A. Oldberg, “The role of small leucine-rich proteoglycans in collagen fibrillogenesis,” Matrix Biology, vol. 29, no. 4, pp. 248–253, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. E. Schönherr, H. Hausser, L. Beavan, and H. Kresse, “Decorin-type I collagen interaction. Presence of separate core protein- binding domains,” Journal of Biological Chemistry, vol. 270, no. 15, pp. 8877–8883, 1995. View at Publisher · View at Google Scholar · View at Scopus
  31. C. Wiberg, E. Hedbom, A. Khairullina et al., “Biglycan and decorin bind close to the N-terminal region of the collagen VI triple helix,” Journal of Biological Chemistry, vol. 276, no. 22, pp. 18947–18952, 2001. View at Publisher · View at Google Scholar · View at Scopus
  32. C. Wiberg, A. R. Klatt, R. Wagener et al., “Complexes of matrilin-1 and biglycan or decorin connect collagen VI microfibrils to both collagen II and aggrecan,” Journal of Biological Chemistry, vol. 278, no. 39, pp. 37698–37704, 2003. View at Publisher · View at Google Scholar · View at Scopus
  33. G. Zhang, Y. Ezura, I. Chervoneva et al., “Decorin regulates assembly of collagen fibrils and acquisition of biomechanical properties during tendon development,” Journal of Cellular Biochemistry, vol. 98, no. 6, pp. 1436–1449, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. J. R. Robbins, S. P. Evanko, and K. G. Vogel, “Mechanical loading and TGF-β regulate proteoglycan synthesis in tendon,” Archives of Biochemistry and Biophysics, vol. 342, no. 2, pp. 203–211, 1997. View at Publisher · View at Google Scholar · View at Scopus
  35. K. G. Danielson, H. Baribault, D. F. Holmes, H. Graham, K. E. Kadler, and R. V. Iozzo, “Targeted disruption of decorin leads to abnormal collagen fibril morphology and skin fragility,” Journal of Cell Biology, vol. 136, no. 3, pp. 729–743, 1997. View at Publisher · View at Google Scholar · View at Scopus
  36. A. Corsi, T. Xu, X.-D. Chen et al., “Phenotypic effects of biglycan deficiency are linked to collagen fibril abnormalities, are synergized by decorin deficiency, and mimic Ehlers-Danlos-like changes in bone and other connective tissues,” Journal of Bone and Mineral Research, vol. 17, no. 7, pp. 1180–1189, 2002. View at Scopus
  37. L. Häkkinen, S. Strassburger, V.-M. Kähäri et al., “A role for decorin in the structural organization of periodontal ligament,” Laboratory Investigation, vol. 80, no. 12, pp. 1869–1880, 2000. View at Scopus
  38. L. M. Dourte, L. Pathmanathan, A. F. Jawad et al., “Influence of decorin on the mechanical, compositional, and structural properties of the mouse patellar tendon,” Journal of Biomechanical Engineering, vol. 134, no. 3, Article ID 031005, 2012. View at Publisher · View at Google Scholar · View at Scopus
  39. S. Ilkhani-Pour, P. B. Voleti, M. R. Buckley et al., “Achilles tendon repair response to injury is enhanced by the absence of decorin,” in Proceedings of the Orthopedic Research Society Annual Meeting, San Antonio, Tex, USA, January 2013.
  40. M. Maccarana, S. Kalamajski, M. Kongsgaard, S. Peter Magnusson, Å. Oldberg, and A. Malmström, “Dermatan sulfate epimerase 1-deficient mice have reduced content and changed distribution of iduronic acids in dermatan sulfate and an altered collagen structure in skin,” Molecular and Cellular Biology, vol. 29, no. 20, pp. 5517–5528, 2009. View at Publisher · View at Google Scholar · View at Scopus
  41. S. Matheson, H. Larjava, and L. Häkkinen, “Distinctive localization and function for lumican, fibromodulin and decorin to regulate collagen fibril organization in periodontal tissues,” Journal of Periodontal Research, vol. 40, no. 4, pp. 312–324, 2005. View at Publisher · View at Google Scholar · View at Scopus
  42. D. M. Elliott, P. S. Robinson, J. A. Gimbel et al., “Effect of altered matrix proteins on quasilinear viscoelastic properties in transgenic mouse tail tendons,” Annals of Biomedical Engineering, vol. 31, no. 5, pp. 599–605, 2003. View at Publisher · View at Google Scholar · View at Scopus
  43. A. Schnieke, K. Harbers, and R. Jaenisch, “Embryonic lethal mutation in mice induced by retrovirus insertion into the α1(I) collagen gene,” Nature, vol. 304, no. 5924, pp. 315–320, 1983. View at Scopus
  44. K. Harbers, M. Kuehn, H. Delius, and R. Jaenisch, “Insertion of retrovirus into the first intron of α1(I) collagen gene leads to embryonic lethal mutation in mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 20, no. 1, pp. 1504–1508, 1984. View at Scopus
  45. J. Bonadio, T. L. Saunders, E. Tsai et al., “Transgenic mouse model of the mild dominant form of osteogenesis imperfecta,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 18, pp. 7145–7149, 1990. View at Scopus
  46. P. S. Robinson, T. W. Lin, P. R. Reynolds, K. A. Derwin, R. V. Iozzo, and L. J. Soslowsky, “Strain-Rate Sensitive Mechanical Properties of Tendon Fascicles from Mice with Genetically Engineered Alterations in Collagen and Decorin,” Journal of Biomechanical Engineering, vol. 126, no. 2, pp. 252–257, 2004. View at Publisher · View at Google Scholar · View at Scopus
  47. X. Liu, H. Wu, M. Byrne, J. Jeffrey, S. Krane, and R. Jaenisch, “A targeted mutation at the known collagenase cleavage site in mouse type I collagen impairs tissue remodeling,” Journal of Cell Biology, vol. 130, no. 1, pp. 227–237, 1995. View at Publisher · View at Google Scholar · View at Scopus
  48. P. S. Robinson, T. W. Lin, A. F. Jawad, R. V. Iozzo, and L. J. Soslowsky, “Investigating tendon fascicle structure-function relationships in a transgenic-age mouse model using multiple regression models,” Annals of Biomedical Engineering, vol. 32, no. 7, pp. 924–931, 2004. View at Publisher · View at Google Scholar · View at Scopus
  49. T. Xu, P. Bianco, L. W. Fisher et al., “Targeted disruption of the biglycan gene leads to an osteoporosis-like phenotype in mice,” Nature Genetics, vol. 20, no. 1, pp. 78–82, 1998. View at Publisher · View at Google Scholar · View at Scopus
  50. Y. Hiroyuki, F. Hiromichi, A. Wataru, and N. Norimasa, “Patellar tendon strength of a specific protein-knockout mouse. Effects of biglycan on the mechanical property of biological fibrous tissues,” Nihon Kikai Gakkai Kanto Shibu Sokai Koen Ronbunshu, vol. 11, pp. 475–476, 2005.
  51. R. Chiu, W. Li, R. P. Herber, S. J. Marshall, M. Young, and S. P. Ho, “Effects of biglycan on physico-chemical properties of ligament-mineralized tissue attachment sites,” Archives of Oral Biology, vol. 57, no. 2, pp. 177–187, 2012. View at Publisher · View at Google Scholar · View at Scopus
  52. L. Ameye, D. Aria, K. Jepsen, A. K. E. Oldberg, T. Xu, and M. F. Young, “Abnormal collagen fibrils in tendons of biglycan/fibromodulin-deficient mice lead to gait impairment, ectopic ossification, and osteoarthritis,” FASEB Journal, vol. 16, no. 7, pp. 673–680, 2002. View at Publisher · View at Google Scholar · View at Scopus
  53. Y. Bi, D. Ehirchiou, T. M. Kilts et al., “Identification of tendon stem/progenitor cells and the role of the extracellular matrix in their niche,” Nature Medicine, vol. 13, no. 10, pp. 1219–1227, 2007. View at Publisher · View at Google Scholar · View at Scopus
  54. T. Kilts, L. Ameye, F. Syed-Picard et al., “Potential roles for the small leucine-rich proteoglycans biglycan and fibromodulin in ectopic ossification of tendon induced by exercise and in modulating rotarod performance,” Scandinavian Journal of Medicine and Science in Sports, vol. 19, no. 4, pp. 536–546, 2009. View at Publisher · View at Google Scholar · View at Scopus
  55. P. S. Robinson, T.-F. Huang, E. Kazam, R. V. Iozzo, D. E. Birk, and L. J. Soslowsky, “Influence of decorin and biglycan on mechanical properties of multiple tendons in knockout mice,” Journal of Biomechanical Engineering, vol. 127, no. 1, pp. 181–185, 2005. View at Publisher · View at Google Scholar · View at Scopus
  56. A. A. Dunkman, M. R. Buckley, M. J. Mienaltowski et al., “Decorin expression is important for age-related changes in tendon structure and mechanical properties,” Matrix Biology, vol. 32, pp. 3–13, 2013.
  57. B. K. Connizzo, J. J. Sarver, D. E. Birk, and L. J. Soslowsky, “Effect of age and proteoglycan deficiency on collagen fiber re-alignment and mechanical properties in mouse supraspinatus tendon,” Journal of Biomechanical Engineering, vol. 135, no. 2, Article ID 021019, 2013. View at Publisher · View at Google Scholar
  58. G. Zhang, S. Chen, S. Goldoni et al., “Genetic evidence for the coordinated regulation of collagen fibrillogenesis in the cornea by decorin and biglycan,” Journal of Biological Chemistry, vol. 284, no. 13, pp. 8888–8897, 2009. View at Publisher · View at Google Scholar · View at Scopus
  59. M. Nakajima, H. Kizawa, M. Saitoh, I. Kou, K. Miyazono, and S. Ikegawa, “Mechanisms for asporin function and regulation in articular cartilage,” Journal of Biological Chemistry, vol. 282, no. 44, pp. 32185–32192, 2007. View at Publisher · View at Google Scholar · View at Scopus
  60. M. Tomoeda, S. Yamada, H. Shirai, Y. Ozawa, M. Yanagita, and S. Murakami, “PLAP-1/asporin inhibits activation of BMP receptor via its leucine-rich repeat motif,” Biochemical and Biophysical Research Communications, vol. 371, no. 2, pp. 191–196, 2008. View at Publisher · View at Google Scholar · View at Scopus
  61. S. Kalamajski, A. Aspberg, K. Lindblom, D. Heinegård, and Å. Oldberg, “Asporin competes with decorin for collagen binding, binds calcium and promotes osteoblast collagen mineralization,” Biochemical Journal, vol. 423, no. 1, pp. 53–59, 2009. View at Publisher · View at Google Scholar · View at Scopus
  62. S. Yamada, M. Tomoeda, Y. Ozawa et al., “PLAP-1/asporin, a novel negative regulator of periodontal ligament mineralization,” Journal of Biological Chemistry, vol. 282, no. 32, pp. 23070–23080, 2007. View at Publisher · View at Google Scholar · View at Scopus
  63. I. Kou, M. Nakajima, and S. Ikegawa, “Expression and regulation of the osteoarthritis-associated protein asporin,” Journal of Biological Chemistry, vol. 282, no. 44, pp. 32193–32199, 2007. View at Publisher · View at Google Scholar · View at Scopus
  64. S. P. Henry, M. Takanosu, T. C. Boyd et al., “Expression pattern and gene characterization of asporin. A newly discovered member of the leucine-rich repeat protein family,” Journal of Biological Chemistry, vol. 276, no. 15, pp. 12212–12221, 2001. View at Publisher · View at Google Scholar · View at Scopus
  65. C. Li, C. Li, J. Yue et al., “miR-21 and miR-101 regulate PLAP-1 expression in periodontal ligament cells,” Molecular Medicine Reports, vol. 5, no. 5, pp. 1340–1346, 2012. View at Publisher · View at Google Scholar · View at Scopus
  66. M. W. M. Schellings, Y. M. Pinto, and S. Heymans, “Matricellular proteins in the heart: possible role during stress and remodeling,” Cardiovascular Research, vol. 64, no. 1, pp. 24–31, 2004. View at Publisher · View at Google Scholar · View at Scopus
  67. J. C. Adams, “Thrombospondins: multifunctional regulators of cell interactions,” Annual Review of Cell and Developmental Biology, vol. 17, pp. 25–51, 2001.
  68. M. Koch, F. Hussein, A. Woeste et al., “CD36-mediated activation of endothelial cell apoptosis by an N-terminal recombinant fragment of thrombospondin-2 inhibits breast cancer growth and metastasis in vivo,” Breast Cancer Research and Treatment, vol. 128, no. 2, pp. 337–346, 2011. View at Publisher · View at Google Scholar · View at Scopus
  69. R. Simantov, M. Febbraio, and R. L. Silverstein, “The antiangiogenic effect of thrombospondin-2 is mediated by CD36 and modulated by histidine-rich glycoprotein,” Matrix Biology, vol. 24, no. 1, pp. 27–34, 2005. View at Publisher · View at Google Scholar · View at Scopus
  70. A. S. Asch, S. Silbiger, E. Heimer, and R. L. Nachman, “Thrombospondin sequence motif (CSVTCG) is responsible for CD36 binding,” Biochemical and Biophysical Research Communications, vol. 182, no. 3, pp. 1208–1217, 1992. View at Scopus
  71. T. M. Misenheimer, A. J. Hahr, A. C. Harms, D. S. Annis, and D. F. Mosher, “Disulfide connectivity of recombinant C-terminal region of human thrombospondin 2,” Journal of Biological Chemistry, vol. 276, no. 49, pp. 45882–45887, 2001. View at Publisher · View at Google Scholar · View at Scopus
  72. C. B. Carlson, D. A. Bernstein, D. S. Annis et al., “Structure of the calcium-rich signature domain of human thrombospondin-2,” Nature Structural and Molecular Biology, vol. 12, no. 10, pp. 910–914, 2005. View at Publisher · View at Google Scholar · View at Scopus
  73. H. Chen, J. Sottile, K. M. O'Rourke, V. M. Dixit, and D. F. Mosher, “Properties of recombinant mouse thrombospondin 2 expressed in Spodoptera cells,” Journal of Biological Chemistry, vol. 269, no. 51, pp. 32226–32232, 1994. View at Scopus
  74. H. Chen, D. K. Strickland, and D. F. Mosher, “Metabolism of thrombospondin 2: binding and degradation by 3T3 cells and glycosaminoglycan-variant Chinese hamster ovary cells,” Journal of Biological Chemistry, vol. 271, no. 27, pp. 15993–15999, 1996. View at Publisher · View at Google Scholar · View at Scopus
  75. M. L. Iruela-Arispe, D. J. Liska, E. H. Sage, and P. Bornstein, “Differential expression of thrombospondin 1, 2, and 3 during murine development,” Developmental Dynamics, vol. 197, no. 1, pp. 40–56, 1993. View at Scopus
  76. R. P. Tucker, J. C. Adams, and J. Lawler, “Thrombospondin-4 is expressed by early osteogenic tissues in the chick embryo,” Developmental Dynamics, vol. 203, no. 4, pp. 477–490, 1995. View at Scopus
  77. T. R. Kyriakides, Y.-H. Zhu, L. T. Smith et al., “Mice that lack thrombospondin 2 display connective tissue abnormalities that are associated with disordered collagen fibrillogenesis, an increased vascular density, and a bleeding diathesis,” Journal of Cell Biology, vol. 140, no. 2, pp. 419–430, 1998. View at Publisher · View at Google Scholar · View at Scopus
  78. P. Bornstein, T. R. Kyriakides, Z. Yang, L. C. Armstrong, and D. E. Birk, “Thrombospondin 2 modulates collagen fibrillogenesis and angiogenesis,” Journal of Investigative Dermatology Symposium Proceedings, vol. 5, no. 1, pp. 61–66, 2000. View at Publisher · View at Google Scholar · View at Scopus
  79. R. Zohar, W. Lee, P. Arora, S. Cheifetz, C. McCulloch, and J. Sodek, “Single cell analysis of intracellular osteopontin in osteogenic cultures of fetal rat calvarial cells,” Journal of Cellular Physiology, vol. 170, no. 1, pp. 88–100, 1997.
  80. B. Christensen, M. S. Nielsen, K. F. Haselmann, T. E. Petersen, and E. S. Sørensen, “Post-translationally modified residues of native human osteopontin are located in clusters: identification of 36 phosphorylation and five O-glycosylation sites and their biological implications,” Biochemical Journal, vol. 390, no. 1, pp. 285–292, 2005. View at Publisher · View at Google Scholar · View at Scopus
  81. V. S. Tagliabracci, J. L. Engel, J. Wen et al., “Secreted kinase phosphorylates extracellular proteins that regulate biomineralization,” Science, vol. 336, no. 6085, pp. 1150–1153, 2012. View at Publisher · View at Google Scholar
  82. E. S. Sorensen, P. Hojrup, and T. E. Petersen, “Posttranslational modifications of bovine osteopontin: identification of twenty-eight phosphorylation and three O-glycosylation sites,” Protein Science, vol. 4, no. 10, pp. 2040–2049, 1995. View at Scopus
  83. D. T. Denhardt, M. Noda, A. W. O'Regan, D. Pavlin, and J. S. Berman, “Osteopontin as a means to cope with environmental insults: regulation of inflammation, tissue remodeling, and cell survival,” Journal of Clinical Investigation, vol. 107, no. 9, pp. 1055–1061, 2001. View at Scopus
  84. S. Ashkar, G. F. Weber, V. Panoutsakopoulou et al., “Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity,” Science, vol. 287, no. 5454, pp. 860–864, 2000. View at Publisher · View at Google Scholar · View at Scopus
  85. N. Mori, T. Majima, N. Iwasaki et al., “The role of osteopontin in tendon tissue remodeling after denervation-induced mechanical stress deprivation,” Matrix Biology, vol. 26, no. 1, pp. 42–53, 2007. View at Publisher · View at Google Scholar · View at Scopus
  86. E. Takeuchi, K. Sugamoto, T. Nakase et al., “Localization and expression of osteopontin in the rotator cuff tendons in patients with calcifying tendinitis,” Virchows Archiv, vol. 438, no. 6, pp. 612–617, 2001. View at Publisher · View at Google Scholar · View at Scopus
  87. S. R. Rittling, H. N. Matsumoto, M. D. Mckee et al., “Mice lacking osteopontin show normal development and bone structure but display altered osteoclast formation in vitro,” Journal of Bone and Mineral Research, vol. 13, no. 7, pp. 1101–1111, 1998. View at Publisher · View at Google Scholar · View at Scopus
  88. J. Engel, W. Taylor, M. Paulsson, H. Sage, and B. Hogan, “Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues,” Biochemistry, vol. 26, no. 22, pp. 6958–6965, 1987. View at Scopus
  89. S. McCurdy, C. F. Baicu, S. Heymans, and A. D. Bradshaw, “Cardiac extracellular matrix remodeling: fibrillar collagens and secreted protein Acidic and Rich in Cysteine (SPARC),” Journal of Molecular and Cellular Cardiology, vol. 48, no. 3, pp. 544–549, 2010. View at Publisher · View at Google Scholar · View at Scopus
  90. C. Giudici, N. Raynal, H. Wiedemann et al., “Mapping of SPARC/BM-40/osteonectin-binding sites on fibrillar collagens,” Journal of Biological Chemistry, vol. 283, no. 28, pp. 19551–19560, 2008. View at Publisher · View at Google Scholar · View at Scopus
  91. T. J. Rentz, F. Poobalarahi, P. Bornstein, E. H. Sage, and A. D. Bradshaw, “SPARC regulates processing of procollagen I and collagen fibrillogenesis in dermal fibroblasts,” Journal of Biological Chemistry, vol. 282, no. 30, pp. 22062–22071, 2007. View at Publisher · View at Google Scholar · View at Scopus
  92. E. Van Der Zee, V. Everts, and W. Beertsen, “Cytokines modulate routes of collagen breakdown Review with special emphasis on mechanisms of collagen degradation in the periodontium and the burst hypothesis of periodontal disease progression,” Journal of Clinical Periodontology, vol. 24, no. 5, pp. 297–305, 1997. View at Scopus
  93. J. S. Kinney, C. A. Ramseier, and W. V. Giannobile, “Oral fluid-based biomarkers of alveolar bone loss in periodontitis,” Annals of the New York Academy of Sciences, vol. 1098, pp. 230–251, 2007. View at Publisher · View at Google Scholar · View at Scopus
  94. K. Norose, J. I. Clark, N. A. Syed et al., “SPARC deficiency leads to early-onset cataractogenesis,” Investigative Ophthalmology and Visual Science, vol. 39, no. 13, pp. 2674–2680, 1998. View at Scopus
  95. J. M. Trombetta and A. D. Bradshaw, “SPARC/osteonectin functions to maintain homeostasis of the collagenous extracellular matrix in the periodontal ligament,” Journal of Histochemistry and Cytochemistry, vol. 58, no. 10, pp. 871–879, 2010. View at Publisher · View at Google Scholar · View at Scopus
  96. J. Trombetta-Esilva, H. Yu, D. N. Arias, C. Rossa Jr., K. L. Kirkwood, and A. D. Bradshaw, “LPS induces greater bone and PDL loss in SPARC-null mice,” Journal of Dental Research, vol. 90, no. 4, pp. 477–482, 2011. View at Publisher · View at Google Scholar · View at Scopus
  97. J. Trombetta-Esilva and A. D. Bradshaw, “The function of SPARC as a mediator of fibrosis,” The Open Rheumatology Journal, vol. 6, pp. 146–155, 2012. View at Publisher · View at Google Scholar
  98. J. Wilde, M. Yokozeki, K. Terai, A. Kudo, and K. Moriyama, “The divergent expression of periostin mRNA in the periodontal ligament during experimental tooth movement,” Cell and Tissue Research, vol. 312, no. 3, pp. 345–351, 2003. View at Publisher · View at Google Scholar · View at Scopus
  99. D. W. Hamilton, “Functional role of periostin in development and wound repair: implications for connective tissue disease,” Journal of Cell Communication and Signaling, vol. 2, no. 1-2, pp. 9–17, 2008. View at Publisher · View at Google Scholar · View at Scopus
  100. A. Kudo, “Periostin in fibrillogenesis for tissue regeneration: periostin actions inside and outside the cell,” Cellular and Molecular Life Sciences, vol. 68, no. 19, pp. 3201–3207, 2011. View at Publisher · View at Google Scholar · View at Scopus
  101. H. Rios, S. V. Koushik, H. Wang et al., “periostin null mice exhibit dwarfism, incisor enamel defects, and an early-onset periodontal disease-like phenotype,” Molecular and Cellular Biology, vol. 25, no. 24, pp. 11131–11144, 2005. View at Publisher · View at Google Scholar · View at Scopus
  102. I. Kii, N. Amizuka, L. Minqi, S. Kitajima, Y. Saga, and A. Kudo, “Periostin is an extracellular matrix protein required for eruption of incisors in mice,” Biochemical and Biophysical Research Communications, vol. 342, no. 3, pp. 766–772, 2006. View at Publisher · View at Google Scholar · View at Scopus
  103. G. P. Riley, R. L. Harrall, T. E. Cawston, B. L. Hazleman, and E. J. Mackie, “Tenascin-C and human tendon degeneration,” American Journal of Pathology, vol. 149, no. 3, pp. 933–943, 1996. View at Scopus
  104. H. Suzuki, N. Amizuka, I. Kii et al., “Immunohistochemical localization of periostin in tooth and its surrounding tissues in mouse mandibles during development,” Anatomical Record A, vol. 281, no. 2, pp. 1264–1275, 2004. View at Publisher · View at Google Scholar · View at Scopus
  105. H. F. Rios, D. Ma, Y. Xie et al., “Periostin is essential for the integrity and function of the periodontal ligament during occlusal loading in mice,” Journal of Periodontology, vol. 79, no. 8, pp. 1480–1490, 2008. View at Publisher · View at Google Scholar · View at Scopus
  106. D. Hakuno, N. Kimura, M. Yoshioka et al., “Periostin advances atherosclerotic and rheumatic cardiac valve degeneration by inducing angiogenesis and MMP production in humans and rodents,” Journal of Clinical Investigation, vol. 120, no. 7, pp. 2292–2306, 2010. View at Publisher · View at Google Scholar · View at Scopus
  107. T. Oka, J. Xu, R. A. Kaiser et al., “Genetic manipulation of periostin expression reveals a role in cardiac hypertrophy and ventricular remodeling,” Circulation Research, vol. 101, no. 3, pp. 313–321, 2007. View at Publisher · View at Google Scholar · View at Scopus
  108. R. A. Morris, B. Damon, V. Mironov et al., “Periostin regulates collagen fibrillogenesis and the biomechanical properties of connective tissues,” Journal of Cellular Biochemistry, vol. 101, no. 3, pp. 695–711, 2007. View at Publisher · View at Google Scholar · View at Scopus
  109. C. S. Chamberlain, K. I. Rolnick, E. M. Leiferman, S. Liegel, G. S. Baer, and R. Vanderby, “Periostin deficient mouse tendons exhibit altered collagen patterns,” in Proceedings of the Orthopedic Research Society Annual Meeting, San Antonio, Tex, USA, January 2013.
  110. R. Chiquet-Ehrismann and R. P. Tucker, “Tenascins and the importance of adhesion modulation,” Cold Spring Harbor Perspectives in Biology, vol. 3, no. 5, 2011. View at Scopus
  111. F. Morellini and M. Schachner, “Enhanced novelty-induced activity, reduced anxiety, delayed resynchronization to daylight reversal and weaker muscle strength in tenascin-C-deficient mice,” European Journal of Neuroscience, vol. 23, no. 5, pp. 1255–1268, 2006. View at Publisher · View at Google Scholar · View at Scopus
  112. S. C. Juneja, R. J. O’Keefe, E. M. Schwarz, and H. A. Awad, “Cellular and molecular interactions in flexor tendon repairs: towards regenerative scarless healing,” in Proceedings of the Orthopedic Research Society Annual Meeting, pp. 4–7, Francisco, Calif, USA, February 2012.
  113. S. C. Juneja, “Cellular distribution and gene expression profile during flexor tendon graft repair: a novel tissue engineering approach,” Journal of Tissue Engineering, vol. 4, 2013. View at Publisher · View at Google Scholar
  114. I. Eshed, M. Bollow, D. G. McGonagle et al., “MRI of enthesitis of the appendicular skeleton in spondyloarthritis,” Annals of the Rheumatic Diseases, vol. 66, no. 12, pp. 1553–1559, 2007. View at Publisher · View at Google Scholar · View at Scopus
  115. L. Jozsa, M. Kvist, B. J. Balint et al., “The role of recreational sport activity in Achilles tendon rupture. A clinical, pathoanatomical, and sociological study of 292 cases,” American Journal of Sports Medicine, vol. 17, no. 3, pp. 338–343, 1989. View at Scopus
  116. E. J. Mackie, “Molecules in focus: tenascin-C,” The International Journal of Biochemistry & Cell Biology, vol. 29, pp. 1133–1137, 1997.
  117. M. Chiquet and D. M. Fambrough, “Chick myotendinous antigen. II. A novel extracellular glycoprotein complex consisting of large disulfide-linked subunits,” Journal of Cell Biology, vol. 98, no. 6, pp. 1937–1946, 1984. View at Scopus
  118. T. A. H. Järvinen, L. Jozsa, P. Kannus et al., “Mechanical loading regulates tenascin-C expression in the osteotendinous junction,” Journal of Cell Science, vol. 112, no. 18, pp. 3157–3166, 1999. View at Scopus
  119. T. A. H. Järvinen, L. Józsa, P. Kannus et al., “Mechanical loading regulates the expression of tenascin-C in the myotendinous junction and tendon but does not induce de novo synthesis in the skeletal muscle,” Journal of Cell Science, vol. 116, no. 5, pp. 857–866, 2003. View at Publisher · View at Google Scholar · View at Scopus
  120. P. L. Jones and F. S. Jones, “Tenascin-C in development and disease: gene regulation and cell function,” Matrix Biology, vol. 19, no. 7, pp. 581–596, 2000. View at Publisher · View at Google Scholar · View at Scopus
  121. F. T. Bosman and I. Stamenkovic, “Functional structure and composition of the extracellular matrix,” Journal of Pathology, vol. 200, no. 4, pp. 423–428, 2003. View at Publisher · View at Google Scholar · View at Scopus
  122. D. Ireland, R. Harrall, V. Curry et al., “Multiple changes in gene expression in chronic human Achilles tendinopathy,” Matrix Biology, vol. 20, no. 3, pp. 159–169, 2001. View at Publisher · View at Google Scholar · View at Scopus
  123. C. J. Saunders, L. van der Merwe, M. Posthumus et al., “Investigation of variants within the COL27A1 and TNC genes and Achilles tendinopathy in two populations,” Journal of Orthopaedic Research, vol. 31, pp. 632–637, 2013.
  124. G. G. Mokone, M. Gajjar, A. V. September et al., “The guanine-thymine dinucleotide repeat polymorphism within the tenascin-C gene is associated with Achilles tendon injuries,” American Journal of Sports Medicine, vol. 33, no. 7, pp. 1016–1021, 2005. View at Publisher · View at Google Scholar · View at Scopus
  125. K. Yagishita, I. Sekiya, Y. Sakaguchi, K. Shinomiya, and T. Muneta, “The effect of hyaluronan on tendon healing in rabbits,” Arthroscopy, vol. 21, no. 11, pp. 1330–1336, 2005. View at Publisher · View at Google Scholar · View at Scopus
  126. D. Egging, F. Van Den Berkmortel, G. Taylor, J. Bristow, and J. Schalkwijk, “Interactions of human tenascin-X domains with dermal extracellular matrix molecules,” Archives of Dermatological Research, vol. 298, no. 8, pp. 389–396, 2007. View at Publisher · View at Google Scholar · View at Scopus
  127. J. R. Mao, G. Taylor, W. B. Dean et al., “Tenascin-X deficiency mimics Ehlers-Danlos syndrome in mice through alteration of collagen deposition,” Nature Genetics, vol. 30, no. 4, pp. 421–425, 2002. View at Publisher · View at Google Scholar · View at Scopus
  128. P. A. Huijing, N. C. Voermans, G. C. Baan, T. E. Busé, B. G. M. Van Engelen, and A. De Haan, “Muscle characteristics and altered myofascial force transmission in tenascin-X-deficient mice, a mouse model of Ehlers-Danlos syndrome,” Journal of Applied Physiology, vol. 109, no. 4, pp. 986–995, 2010. View at Publisher · View at Google Scholar · View at Scopus
  129. O. Brandau, A. Meindl, R. Fässler, and A. Aszódi, “A novel gene, tendin, is strongly expressed in tendons and ligaments and shows high homology with chondromodulin-I,” Developmental Dynamics, vol. 221, pp. 72–80, 2001.
  130. K. Yamana, H. Wada, Y. Takahashi, H. Sato, Y. Kasahara, and M. Kiyoki, “Molecular cloning and characterization of ChM1L, a novel membrane molecule similar to chondromodulin-I,” Biochemical and Biophysical Research Communications, vol. 280, no. 4, pp. 1101–1106, 2001. View at Publisher · View at Google Scholar · View at Scopus
  131. P. J. Neame, J. T. Treep, and C. N. Young, “An 18-kDa glycoprotein from bovine nasal cartilage. Isolation and primary structure of small, cartilage-derived glycoprotein,” Journal of Biological Chemistry, vol. 265, no. 17, pp. 9628–9633, 1990. View at Scopus
  132. Y. Hiraki, H. Tanaka, H. Inoue, J. Kondo, A. Kamizono, and F. Suzuki, “Molecular cloning of a new class of cartilage-specific matrix, chondromodulin-I, which stimulates growth of cultured chondrocytes,” Biochemical and Biophysical Research Communications, vol. 175, no. 3, pp. 971–977, 1991. View at Publisher · View at Google Scholar · View at Scopus
  133. L. Sánchez-Pulido, D. Devos, and A. Valencia, “BRICHOS: a conserved domain in proteins associated with dementia, respiratory distress and cancer,” Trends in Biochemical Sciences, vol. 27, no. 7, pp. 329–332, 2002. View at Publisher · View at Google Scholar · View at Scopus
  134. Y. Oshima, C. Shukunami, J. Honda et al., “Expression and localization of tenomodulin, a transmembrane type chondromodulin-I-related angiogenesis inhibitor, in mouse eyes,” Investigative Ophthalmology and Visual Science, vol. 44, no. 5, pp. 1814–1823, 2003. View at Publisher · View at Google Scholar · View at Scopus
  135. Y. Oshima, K. Sato, F. Tashiro et al., “Anti-angiogenic action of the C-terminal domain of tenomodulin that shares homology with chondromodulin-I,” Journal of Cell Science, vol. 117, no. 13, pp. 2731–2744, 2004. View at Publisher · View at Google Scholar · View at Scopus
  136. D. Docheva, E. B. Hunziker, R. Fässler, and O. Brandau, “Tenomodulin is necessary for tenocyte proliferation and tendon maturation,” Molecular and Cellular Biology, vol. 25, no. 2, pp. 699–705, 2005. View at Publisher · View at Google Scholar · View at Scopus
  137. O. Brandau, A. Aszódi, E. B. Hunziker, P. J. Neame, D. Vestweber, and R. Fässler, “Chondromodulin I is dispensable during enchondral ossification and eye development,” Molecular and Cellular Biology, vol. 22, no. 18, pp. 6627–6635, 2002. View at Publisher · View at Google Scholar · View at Scopus
  138. J. Qi, J. M. Dmochowski, A. N. Banes et al., “Differential expression and cellular localization of novel isoforms of the tendon biomarker tenomodulin,” Journal of Applied Physiology, vol. 113, pp. 861–871, 2012.
  139. C. Shukunami, A. Takimoto, M. Oro, and Y. Hiraki, “Scleraxis positively regulates the expression of tenomodulin, a differentiation marker of tenocytes,” Developmental Biology, vol. 298, no. 1, pp. 234–247, 2006. View at Publisher · View at Google Scholar · View at Scopus
  140. R. Schmits, J. Filmus, N. Gerwin et al., “CD44 regulates hematopoietic progenitor distribution, granuloma formation, and tumorigenicity,” Blood, vol. 90, no. 6, pp. 2217–2233, 1997. View at Scopus
  141. H. L. Ansorge, P. K. Beredjiklian, and L. J. Soslowsky, “CD44 deficiency improves healing tendon mechanics and increases matrix and cytokine expression in a mouse patellar tendon injury model,” Journal of Orthopaedic Research, vol. 27, no. 10, pp. 1386–1391, 2009. View at Publisher · View at Google Scholar · View at Scopus
  142. A. M. Malfait, J. Ritchie, A. S. Gil et al., “ADAMTS-5 deficient mice do not develop mechanical allodynia associated with osteoarthritis following medial meniscal destabilization,” Osteoarthritis and Cartilage, vol. 18, no. 4, pp. 572–580, 2010. View at Publisher · View at Google Scholar · View at Scopus
  143. V. M. Wang, R. M. Bell, R. Thakore et al., “Murine tendon function is adversely affected by aggrecan accumulation due to the knockout of ADAMTS5,” Journal of Orthopaedic Research, vol. 30, no. 4, pp. 620–626, 2012. View at Publisher · View at Google Scholar · View at Scopus
  144. D. K. Rhee, J. Marcelino, M. Baker et al., “The secreted glycoprotein lubricin protects cartilage surfaces and inhibits synovial cell overgrowth,” Journal of Clinical Investigation, vol. 115, no. 3, pp. 622–631, 2005. View at Publisher · View at Google Scholar · View at Scopus
  145. R. T. Kohrs, C. Zhao, Y.-L. Sun et al., “Tendon fascicle gliding in wild type, heterozygous, and lubricin knockout mice,” Journal of Orthopaedic Research, vol. 29, no. 3, pp. 384–389, 2011. View at Publisher · View at Google Scholar · View at Scopus
  146. J. Reuvers, A. R. Thoreson, C. Zhao et al., “The mechanical properties of tail tendon fascicles from lubricin knockout, wild type and heterozygous mice,” Journal of Structural Biology, vol. 176, no. 1, pp. 41–45, 2011. View at Publisher · View at Google Scholar · View at Scopus
  147. T. Ochi, R. Iwase, and N. Okabe, “The pathology of the involved tendons in patients with familial arthropathy and congenital camptodactyly,” Arthritis and Rheumatism, vol. 26, no. 7, pp. 896–900, 1983. View at Scopus
  148. J. Marcelino, J. D. Carpten, W. M. Suwairi et al., “CACP, encoding a secreted proteoglycan, is mutated in camptodactyly- arthropathy-coxa vara-pericarditis syndrome,” Nature Genetics, vol. 23, no. 3, pp. 319–322, 1999. View at Publisher · View at Google Scholar · View at Scopus
  149. S. Basit, Z. Iqbal, M. Umicevic-Mirkov et al., “A novel deletion mutation in proteoglycan-4 underlies camptodactyly-arthropathy-coxa-vara-pericarditis syndrome in a consanguineous pakistani family,” Archives of Medical Research, vol. 42, no. 2, pp. 110–114, 2011. View at Publisher · View at Google Scholar · View at Scopus
  150. S. Goodison, V. Urquidi, and D. Tarin, “CD44 cell adhesion molecules,” Journal of Clinical Pathology, vol. 52, no. 4, pp. 189–196, 1999. View at Scopus
  151. A. Aruffo, I. Stamenkovic, M. Melnick, C. B. Underhill, and B. Seed, “CD44 is the principal cell surface receptor for hyaluronate,” Cell, vol. 61, no. 7, pp. 1303–1313, 1990. View at Publisher · View at Google Scholar · View at Scopus
  152. M. Berglund, D. A. Hart, and M. Wiig, “The inflammatory response and hyaluronan synthases in the rabbit flexor tendon and tendon sheath following injury,” Journal of Hand Surgery. European Volume, vol. 32, no. 5, pp. 581–587, 2007. View at Publisher · View at Google Scholar · View at Scopus
  153. M. Favata, P. K. Beredjiklian, M. H. Zgonis et al., “Regenerative properties of fetal sheep tendon are not adversely affected by transplantation into an adult environment,” Journal of Orthopaedic Research, vol. 24, no. 11, pp. 2124–2132, 2006. View at Publisher · View at Google Scholar · View at Scopus
  154. S. Porter, I. M. Clark, L. Kevorkian, and D. R. Edwards, “The ADMTS metalloproteinases,” Biochemical Journal, vol. 386, no. 1, pp. 15–27, 2005. View at Publisher · View at Google Scholar · View at Scopus
  155. A. D. Waggett, J. R. Ralphs, A. P. L. Kwan, D. Woodnutt, and M. Benjamin, “Characterization of collagens and proteoglycans at the insertion of the human Achilles tendon,” Matrix Biology, vol. 16, no. 8, pp. 457–470, 1998. View at Publisher · View at Google Scholar · View at Scopus
  156. K. G. Vogel, J. D. Sandy, G. Pogany, and J. R. Robbins, “Aggrecan in bovine tendon,” Matrix Biology, vol. 14, no. 2, pp. 171–179, 1994. View at Publisher · View at Google Scholar · View at Scopus
  157. A. Plaas, J. D. Sandy, H. Liu et al., “Biochemical identification and immunolocalizaton of aggrecan, ADAMTS5 and inter-alpha-trypsin-inhibitor in equine degenerative suspensory ligament desmitis,” Journal of Orthopaedic Research, vol. 29, no. 6, pp. 900–906, 2011. View at Publisher · View at Google Scholar · View at Scopus
  158. K. A. Waller, L. X. Zhang, K. A. Elsaid, B. C. Fleming, M. L. Warman, and G. D. Jay, “Role of lubricin and boundary lubrication in the prevention of chondrocyte apoptosis,” Proceedings of the National Academy of Sciences of the United States of America, vol. 110, pp. 5852–5857, 2013.
  159. D. K. Rhee, J. Marcelino, S. Al-Mayou et al., “Consequences of disease-causing mutations on lubricin protein synthesis, secretion, and post-translational processing,” Journal of Biological Chemistry, vol. 280, no. 35, pp. 31325–31332, 2005. View at Publisher · View at Google Scholar · View at Scopus
  160. S. Ikegawa, M. Sano, Y. Koshizuka, and Y. Nakamura, “Isolation, characterization and mapping of the mouse and human PRG4 (proteoglycan 4) genes,” Cytogenetics and Cell Genetics, vol. 90, no. 3-4, pp. 291–297, 2000. View at Scopus
  161. B. L. Schumacher, J. A. Block, T. M. Schmid, M. B. Aydelotte, and K. E. Kuettner, “A novel proteoglycan synthesized and secreted by chondrocytes of the superficial zone of articular cartilage,” Archives of Biochemistry and Biophysics, vol. 311, no. 1, pp. 144–152, 1994. View at Publisher · View at Google Scholar · View at Scopus
  162. G. D. Jay, D. E. Britt, and C.-J. Cha, “Lubricin is a product of megakaryocyte stimulating factor gene expression by human synovial fibroblasts,” Journal of Rheumatology, vol. 27, no. 3, pp. 594–600, 2000. View at Scopus
  163. M. Taguchi, Y.-L. Sun, C. Zhao et al., “Lubricin surface modification improves extrasynovial tendon gliding in a canine model in vitro,” Journal of Bone and Joint Surgery A, vol. 90, no. 1, pp. 129–135, 2008. View at Publisher · View at Google Scholar · View at Scopus
  164. Y. Sun, E. J. Berger, C. Zhao, G. D. Jay, K.-N. An, and P. C. Amadio, “Expression and mapping of lubricin in canine flexor tendon,” Journal of Orthopaedic Research, vol. 24, no. 9, pp. 1861–1868, 2006. View at Publisher · View at Google Scholar · View at Scopus
  165. T. Funakoshi, T. Schmid, H.-P. Hsu, and M. Spector, “Lubricin distribution in the goat infraspinatus tendon: a basis for interfascicular lubrication,” Journal of Bone and Joint Surgery A, vol. 90, no. 4, pp. 803–814, 2008. View at Publisher · View at Google Scholar · View at Scopus
  166. Y. L. Sun, C. Zhao, G. D. Jay, T. M. Schmid, K. N. An, and P. C. Amadio, “Effects of stress deprivation on lubricin synthesis and gliding of flexor tendons in a canine model in vivo,” The Journal of Bone & Joint Surgery, vol. 95, pp. 273–278, 2013.
  167. J. Braun, R. Van Den Berg, X. Baraliakos et al., “2010 update of the ASAS/EULAR recommendations for the management of ankylosing spondylitis,” Annals of the Rheumatic Diseases, vol. 70, no. 6, pp. 896–904, 2011. View at Publisher · View at Google Scholar · View at Scopus
  168. R. Burgos-Vargas and J. C. Casasola-Vargas, “From retrospective analysis of patients with undifferentiated spondyloarthritis (SpA) to analysis of prospective cohorts and detection of axial and peripheral SpA,” Journal of Rheumatology, vol. 37, no. 6, pp. 1091–1095, 2010. View at Publisher · View at Google Scholar · View at Scopus
  169. A. Malaviaya, “Classification of spondyloarthritis: a journey well worth,” Indian Journal of Rheumatology, vol. 8, no. 3, pp. 122–129, 2013. View at Publisher · View at Google Scholar
  170. D. D. O'Rielly DD and P. Rahman, “Advances in the genetics of spondyloarthritis and clinical implications,” Current Rheumatology Reports, vol. 15, article 347, 2013. View at Publisher · View at Google Scholar
  171. P. V. Balint, D. Kane, H. Wilson, I. B. McInnes, and R. D. Sturrock, “Ultrasonography of entheseal insertions in the lower limb in spondyloarthropathy,” Annals of the Rheumatic Diseases, vol. 61, no. 10, pp. 905–910, 2002. View at Publisher · View at Google Scholar · View at Scopus
  172. P. Falsetti, B. Frediani, G. Filippou et al., “Enthesitis of proximal insertion of the deltoid in the course of seronegative spondyloarthritis: an atypical enthesitis that can mime impingement syndrome,” Scandinavian Journal of Rheumatology, vol. 31, no. 3, pp. 158–162, 2002. View at Scopus
  173. D. McGonagle, H. Marzo-Ortega, P. O'Connor et al., “Histological assessment of the early enthesitis lesion in spondyloarthropathy,” Annals of the Rheumatic Diseases, vol. 61, no. 6, pp. 534–537, 2002. View at Publisher · View at Google Scholar · View at Scopus
  174. R. Burgos-Vargas, “The assessment of the spondyloarthritis international society concept and criteria for the classification of axial spondyloarthritis and peripheral spondyloarthritis: a critical appraisal for the pediatric rheumatologist,” Pediatric Rheumatology, vol. 10, article 14, 2012. View at Publisher · View at Google Scholar
  175. L. S. Tam, J. Gu, and D. Yu, “Pathogenesis of ankylosing spondylitis,” Nature Reviews Rheumatology, vol. 6, no. 7, pp. 399–405, 2010. View at Publisher · View at Google Scholar
  176. P. C. Robinson and M. A. Brown, “The genetics of ankylosing spondylitis and axial spondyloarthritis,” Rheumatic Disease Clinics of North America, vol. 38, pp. 539–553, 2012.