About this Journal Submit a Manuscript Table of Contents
BioMed Research International
Volume 2013 (2013), Article ID 292953, 21 pages
http://dx.doi.org/10.1155/2013/292953
Review Article

Nephrolithiasis: Molecular Mechanism of Renal Stone Formation and the Critical Role Played by Modulators

1Department of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Waknaghat, Solan, Himachal Pradesh 173234, India
2Department of Biochemistry, Himalyan Institute Hospital Trust, Swami Ram Nagar, Dehradun, Uttrakhand 248140, India

Received 29 April 2013; Accepted 26 July 2013

Academic Editor: Beatrice Charreau

Copyright © 2013 Kanu Priya Aggarwal et al. 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. G. Eknoyan, “History of urolithiasis,” Clinical Reviews in Bone and Mineral Metabolism, vol. 2, no. 3, pp. 177–185, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. M. López and B. Hoppe, “History, epidemiology and regional diversities of urolithiasis,” Pediatric Nephrology, vol. 25, no. 1, pp. 49–59, 2010. View at Publisher · View at Google Scholar · View at Scopus
  3. H. Wilkinson, “Clinical investigation and management of patients with renal stones,” Annals of Clinical Biochemistry, vol. 38, no. 3, pp. 180–187, 2001. View at Publisher · View at Google Scholar · View at Scopus
  4. G. Bihl and A. Meyers, “Recurrent renal stone disease—advances in pathogenesis and clinical management,” The Lancet, vol. 358, no. 9282, pp. 651–656, 2001. View at Publisher · View at Google Scholar · View at Scopus
  5. T. M. Reynolds, “Chemical pathology clinical investigation and management of nephrolithiasis,” Journal of Clinical Pathology, vol. 58, no. 2, pp. 134–140, 2005. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Aggarwal, C. D. Tandon, M. Forouzandeh, S. K. Singla, R. Kiran, and R. K. Jethi, “Role of biomolecules from human renal stone matrix on COM crystal growth,” Molecular and Cellular Biochemistry, vol. 210, no. 1-2, pp. 109–119, 2000. View at Scopus
  7. W. B. Gill, K. W. Jones, and K. J. Ruggiero, “Protective effects of heparin and other sulfated glycosaminoglycans on crystal adhesion to injured urothelium,” The Journal of Urology, vol. 127, no. 1, pp. 152–154, 1982. View at Scopus
  8. M. W. Bigelow, J. H. Wiessner, J. G. Kleinman, and N. S. Mandel, “Calcium oxalate-crystal membrane interactions: dependence on membrane lipid composition,” The Journal of Urology, vol. 155, no. 3, pp. 1094–1098, 1996. View at Publisher · View at Google Scholar · View at Scopus
  9. S. R. Khan and D. J. Kok, “Modulators of urinary stone formation,” Frontiers in Bioscience, vol. 9, pp. 1450–1482, 2004. View at Scopus
  10. I. R. Doyle, R. L. Ryall, and V. R. Marshall, “Inclusion of proteins into calcium oxalate crystals precipitated from human urine: a highly selective phenomenon,” Clinical Chemistry, vol. 37, no. 9, pp. 1589–1594, 1991. View at Scopus
  11. R. M. Morse and M. I. Resnick, “A new approach to the study of urinary macromolecules as a participant in calcium oxalate crystallization,” The Journal of Urology, vol. 139, no. 4, pp. 869–873, 1988. View at Scopus
  12. J. S. King Jr. and W. H. Boyce, “Immunological studies on serum and urinary proteins in urolith matrix in man,” Annals of the New York Academy of Sciences, vol. 104, p. 5791, 1963. View at Scopus
  13. W. G. Robertson, M. Peacock, and B. E. C. Nordin, “Activity products in stone-forming and non-stone-forming urine,” Clinical Science, vol. 34, no. 3, pp. 579–594, 1968. View at Scopus
  14. W. H. Boyce, “Organic matrix of human urinary concretions,” The American Journal of Medicine, vol. 45, no. 5, pp. 673–683, 1968. View at Scopus
  15. S. R. Khan, P. N. Shevock, and R. L. Hackett, “Presence of lipids in urinary stones: results of preliminary studies,” Calcified Tissue International, vol. 42, no. 2, pp. 91–96, 1988. View at Scopus
  16. T. Sugimoto, Y. Funae, H. Rubben, S. Nishio, R. Hautmann, and W. Lutzeyer, “Resolution of proteins in the kidney stone matrix using high-performance liquid chromatography,” European Urology, vol. 11, no. 5, pp. 334–340, 1985. View at Scopus
  17. C. W. Vermeulen and E. S. Lyon, “Mechanisms of genesis and growth of calculi,” The American Journal of Medicine, vol. 45, no. 5, pp. 684–691, 1956. View at Scopus
  18. B. Finlayson, C. W. Vermeulen, and E. J. Stewart, “Stone matrix and mucoprotein from urine,” The Journal of Urology, vol. 86, pp. 355–363, 1961. View at Scopus
  19. S. R. Khan and R. L. Hackett, “Role of organic matrix in urinary stone formation: an ultrastructural study of crystal matrix interface of calcium oxalate monohydrate stones,” The Journal of Urology, vol. 15, no. 1, pp. 239–245, 1993. View at Scopus
  20. I. R. Doyle, V. R. Marshall, C. J. Dawson, and R. L. Ryall, “Calcium oxalate crystal matrix extract: the most potent macromolecular inhibitor of crystal growth and aggregation yet tested in undiluted human urine in vitro,” Urological Research, vol. 23, no. 1, pp. 53–62, 1995. View at Publisher · View at Google Scholar · View at Scopus
  21. G. W. Drach, S. Thorson, and A. Randolph, “Effects of urinary organic macromelecules on crystallization of calcium oxalate: enhancement of nucleation,” The Journal of Urology, vol. 123, no. 4, pp. 519–523, 1980. View at Scopus
  22. R. L. Ryall, R. M. Harnett, C. M. Hibberd, K. A. Edyvane, and V. R. Marshall, “Effects of chondroitin sulphate, human serum albumin and Tamm-Horsfall mucoprotein on calcium oxalate crystallization in undiluted human urine,” Urological Research, vol. 19, no. 3, pp. 181–188, 1991. View at Scopus
  23. M. I. Resnick, M. E. Sorrell, J. A. Bailey, and W. H. Boyce, “Inhibitory effects of urinary calcium-binding substances on calcium oxalate crystallization,” The Journal of Urology, vol. 127, no. 3, pp. 568–571, 1982. View at Scopus
  24. P. K. Grover, R. L. Ryall, and V. R. Marshall, “Does Tamm-Horsfall mucoprotein inhibit or promote calcium oxalate crystallization in human urine?” Clinica Chimica Acta, vol. 190, no. 3, pp. 223–238, 1990. View at Publisher · View at Google Scholar · View at Scopus
  25. A. A. Campbell, A. Ebrahimpour, L. Perez, S. A. Smesko, and G. H. Nancollas, “The dual role of polyelectrolytes and proteins as mineralization promoters and inhibitors of calcium oxalate monohydrate,” Calcified Tissue International, vol. 45, no. 2, pp. 122–128, 1989. View at Scopus
  26. M. Utsunomiya, T. Koide, T. Yoshioka, S. Yamaguchi, and A. Okyama, “Influence of ionic strength on crystal adsorption and inhibitory activity of macromolecules,” British Journal of Urology, vol. 71, no. 5, pp. 516–522, 1993. View at Scopus
  27. M. Carvahlo and Y. Nakagawa, “Urinary supersaturation and recurrence in nephrolithiasis,” International Brazilian Journal of Urology, vol. 25, pp. 475–479, 1999.
  28. D. J. Kok and S. E. Papapoulos, “Physicochemical considerations in the development and prevention of calcium oxalate urolithiasis,” Bone and Mineral, vol. 20, no. 1, pp. 1–15, 1993. View at Scopus
  29. B. Finlayson and S. Reid, “The expectation of free and fixed particles in urinary stone disease,” Investigative Urology, vol. 15, no. 6, pp. 442–448, 1978. View at Scopus
  30. A. L. Boskey, “Current concepts of the physiology and biochemistry of calcification,” Clinical Orthopaedics and Related Research, vol. 157, pp. 225–257, 1981. View at Scopus
  31. L. H. Smith, “Solutions and solute,” Endocrinology and Metabolism Clinics of North America, vol. 19, no. 4, pp. 767–772, 1990. View at Scopus
  32. J. M. Fasano and S. R. Khan, “Intratubular crystallization of calcium oxalate in the presence of membrane vesicles,” Kidney International, vol. 59, no. 1, pp. 169–178, 2001. View at Publisher · View at Google Scholar · View at Scopus
  33. S. R. Khan, P. N. Shevock, and R. L. Hackett, “Membrane-associated crystallization of calcium oxalate,” Calcified Tissue International, vol. 46, no. 2, pp. 116–120, 1990. View at Scopus
  34. B. Finlayson, S. R. Khan, and R. L. Hackett, “Mechanisms of stone formation—an overview,” Scanning Electron Microscopy, vol. 3, pp. 1419–1425, 1984. View at Scopus
  35. M. Honda, T. Yoshioka, S. Yamaguchi et al., “Characterization of protein components of human urinary crystal surface binding substance,” Urological Research, vol. 25, no. 5, pp. 355–360, 1997. View at Publisher · View at Google Scholar · View at Scopus
  36. D. J. Kok and S. R. Khan, “Calcium oxalate nephrolithiasis, a free or fixed particle disease,” Kidney International, vol. 46, no. 3, pp. 847–854, 1994. View at Scopus
  37. B. Hess, L. Zipperle, and P. Jaeger, “Citrate and calcium effects on Tamm-Horsfall glycoprotein as a modifier of calcium oxalate crystal aggregation,” American Journal of Physiology, vol. 265, no. 6, part 2, pp. F784–F791, 1993. View at Scopus
  38. S. R. Khan, K. J. Byer, S. Thamilselvan et al., “Crystal-cell interaction and apoptosis in oxalate-associated injury of renal epithelial cells,” Journal of the American Society of Nephrology, vol. 10, no. 14, pp. S457–S463, 1999. View at Scopus
  39. Y. Kohjimoto, M. Ebisuno, M. Tamura, and T. Ohkawa, “Interactions between calcium oxalate monohydrate crystals and Madin-Darby canine kidney cells: endocytosis and cell proliferation,” Urological Research, vol. 24, no. 4, pp. 193–199, 1996. View at Scopus
  40. S. R. Khan, “Calcium oxalate crystal interaction with renal tubular epithelium, mechanism of crystal adhesion and its impact on stone development,” Urological Research, vol. 23, no. 2, pp. 71–79, 1995. View at Publisher · View at Google Scholar · View at Scopus
  41. J. C. Lieske, S. Deganello, and F. G. Toback, “Cell-crystal interactions and kidney stone formation,” Nephron, vol. 81, no. 1, pp. 8–17, 1999. View at Publisher · View at Google Scholar · View at Scopus
  42. J. C. Lieske, R. Leonard, and F. G. Toback, “Adhesion of calcium oxalate monohydrate crystals to renal epithelial cells is inhibited by specific anions,” American Journal of Physiology, vol. 268, no. 4, part 2, pp. F604–F612, 1995. View at Scopus
  43. J. C. Lieske, B. H. Spargo, and F. G. Toback, “Endocytosis of calcium oxalate crystals and proliferation of renal tubular epithelial cells in a patient with type 1 primary hyperoxaluria,” The Journal of Urology, vol. 148, no. 5, pp. 1517–1519, 1992. View at Scopus
  44. J. C. Lieske, H. Swift, T. Martin, B. Patterson, and F. G. Toback, “Renal epithelial cells rapidly bind and internalize calcium oxalate monohydrate crystals,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 15, pp. 6987–6991, 1994. View at Publisher · View at Google Scholar · View at Scopus
  45. B. Hess, “Tamm-Horsfall glycoprotein-inhibitor or promoter of calcium oxalate monohydrate crystallization processes?” Urological Research, vol. 20, no. 1, pp. 83–86, 1992. View at Publisher · View at Google Scholar · View at Scopus
  46. S. Kumar and A. Muchmore, “Tamm-Horsfall protein-uromodulin (1950–1990),” Kidney International, vol. 37, no. 6, pp. 1395–1401, 1990. View at Scopus
  47. M. Tsujihata, O. Miyake, K. Yoshimura, K.-I. Kakimoto, S. Takahara, and A. Okuyama, “Fibronectin as a potent inhibitor of calcium oxalate urolithiasis,” The Journal of Urology, vol. 164, no. 5, pp. 1718–1723, 2000. View at Scopus
  48. M. Tsujihata, K. Yoshimura, K. Tsujikawa, N. Tei, and A. Okuyama, “Fibronectin inhibits endocytosis of calcium oxalate crystals by renal tubular cells,” International Journal of Urology, vol. 13, no. 6, pp. 743–746, 2006. View at Publisher · View at Google Scholar · View at Scopus
  49. J. C. Lieske and F. G. Toback, “Regulation of renal epithelial cell endocytosis of calcium oxalate monohydrate crystals,” American Journal of Physiology, vol. 264, no. 5, pp. F800–F807, 1993. View at Scopus
  50. J. H. Wiessner, A. T. Hasegawa, L. Y. Hung, and N. S. Mandel, “Oxalate-induced exposure of phosphatidylserine on the surface of renal epithelial cells in culture,” Journal of the American Society of Nephrology, vol. 10, supplement 14, pp. S441–S445, 1999. View at Scopus
  51. S. R. Khan and R. L. Hackett, “Hyperoxaluria, enzymuria and nephrolithiasis,” Contributions to Nephrology, vol. 101, pp. 190–193, 1993. View at Scopus
  52. S. R. Khan, B. Finlayson, and R. L. Hackett, “Histologic study of the early events in oxalate induced intranephronic calculosis,” Investigative Urology, vol. 17, no. 3, pp. 199–203, 1979. View at Scopus
  53. S. R. Khan, B. Finlayson, and R. L. Hackett, “Experimental calcium oxalate nephrolithiasis in the rat,” The American Journal of Pathology, vol. 107, no. 1, pp. 59–69, 1982. View at Scopus
  54. J. H. Wiessner, A. T. Hasegawa, L. Y. Hung, G. S. Mandel, and N. S. Mandel, “Mechanisms of calcium oxalate crystal attachment to injured renal collecting duct cells,” Kidney International, vol. 59, no. 2, pp. 637–644, 2001. View at Publisher · View at Google Scholar · View at Scopus
  55. R. L. Hackett, P. N. Shevock, and S. R. Khan, “Madin-Darby canine kidney cells are injured by exposure to oxalate and to calcium oxalate crystals,” Urological Research, vol. 22, no. 4, pp. 197–204, 1994. View at Publisher · View at Google Scholar · View at Scopus
  56. S. R. Khan, J. M. Johnson, A. B. Peck, J. G. Cornelius, and P. A. Glenton, “Expression of osteopontin in rat kidneys: induction during ethylene glycol induced calcium oxalate nephrolithiasis,” The Journal of Urology, vol. 168, no. 3, pp. 1173–1181, 2002. View at Scopus
  57. M. Tsujihata, O. Miyake, K. Yoshimura, K. I. Kakimoto, S. Takahara, and A. Okuyama, “Comparison of fibronectin content in urinary macromolecules between normal subjects and recurrent stone formers,” European Urology, vol. 40, no. 4, pp. 458–462, 2001. View at Publisher · View at Google Scholar · View at Scopus
  58. S. R. Khan, “Role of renal epithelial cells in the initiation of calcium oxalate stones,” Nephron Experimental Nephrology, vol. 98, no. 2, pp. e55–e60, 2004. View at Publisher · View at Google Scholar · View at Scopus
  59. S. R. Khan, F. Atmani, P. Glenton, Z. C. Hou, D. R. Talham, and M. Khurshid, “Lipids and membranes in the organic matrix of urinary calcific crystals and stones,” Calcified Tissue International, vol. 59, no. 5, pp. 357–365, 1996. View at Publisher · View at Google Scholar · View at Scopus
  60. S. R. Khan, P. A. Glenton, R. Backov, and D. R. Talham, “Presence of lipids in urine, crystals and stones: implications for the formation of kidney stones,” Kidney International, vol. 62, no. 6, pp. 2062–2072, 2002. View at Publisher · View at Google Scholar · View at Scopus
  61. S. R. Khan, P. O. Whalen, and P. A. Glenton, “Heterogeneous nucleation of calcium oxalate crystals in the presence of membrane vesicles,” Journal of Crystal Growth, vol. 134, no. 3-4, pp. 211–218, 1993. View at Scopus
  62. W. H. Boyce and F. K. Garvey, “The amount and nature of the organic matrix in urinary calculi: a review,” The Journal of Urology, vol. 76, no. 3, pp. 213–227, 1956. View at Scopus
  63. S. Nishio, Y. Abe, A. Wakatsuki, et al., “Matrix glycosaminoglycan in urinary stones,” The Journal of Urology, vol. 134, no. 3, pp. 503–505, 1985. View at Scopus
  64. E. Wessler, “The nature of the non-ultrafilterable glycosaminoglycans of normal human urine,” The Biochemical Journal, vol. 122, no. 3, pp. 373–384, 1971. View at Scopus
  65. S. Yamaguchi, T. Yoshioka, M. Utsunomiya et al., “Heparan sulfate in the stone matrix and its inhibitory effect on calcium oxalate crystallization,” Urological Research, vol. 21, no. 3, pp. 187–192, 1993. View at Scopus
  66. K. Suzuki, K. Mayne, I. R. Doyle, and R. L. Ryall, “Urinary glycosaminoglycans are selectively included into calcium oxalate crystals,” Scanning Microscopy, vol. 8, no. 3, pp. 523–530, 1994. View at Scopus
  67. H. Iwata, O. Kamei, Y. Abe et al., “The organic matrix of urinary uric acid crystals,” The Journal of Urology, vol. 139, no. 3, pp. 607–610, 1988. View at Scopus
  68. D. K. Y. Shum and M. D. I. Gohel, “Separate effects of urinary chondroitin sulphate and heparan sulphate on the crystallization of urinary calcium oxalate: differences between stone formers and normal control subjects,” Clinical Science, vol. 85, no. 1, pp. 33–39, 1993. View at Scopus
  69. C. T. Samuell, “A study of glycosaminoglycan excretion in normal and stone-forming subjects using a modified cetylpyridinium chloride technique,” Clinica Chimica Acta, vol. 117, no. 1, pp. 63–73, 1981. View at Publisher · View at Google Scholar · View at Scopus
  70. R. L. Ryall, “Glycosaminoglycans, proteins, and stone formation: adult themes and child's play,” Pediatric Nephrology, vol. 10, no. 5, pp. 656–666, 1996. View at Publisher · View at Google Scholar · View at Scopus
  71. E. Erturk, M. Kiernan, and S. R. Schoen, “Clinical association with urinary glycosaminoglycans and urolithiasis,” Urology, vol. 59, no. 4, pp. 495–499, 2002. View at Publisher · View at Google Scholar · View at Scopus
  72. M. C. Dalsing, G. L. Grosfeld, and M. A. Shiffler, “Superoxide dismutase: a cellular protective enzyme in bowel ischemia,” The Journal of Surgical Research, vol. 34, no. 6, pp. 589–596, 1983. View at Scopus
  73. J. A. Gokhale, P. A. Glenton, and S. R. Khan, “Characterization of Tamm-Horsfall protein in a rat nephrolithiasis model,” The Journal of Urology, vol. 166, no. 4, pp. 1492–1497, 2001. View at Scopus
  74. K. L. Sikri, C. L. Foster, N. MacHugh, and R. D. Marshall, “Localization of Tamm-Horsfall glycoprotein in the human kidney using immune-fluorescence and immuno-electron microscopical techniques,” Journal of Anatomy, vol. 132, no. 4, pp. 597–605, 1981. View at Scopus
  75. J. S. Hunt, A. R. McGiven, A. Groufsky, K. L. Lynn, and M. C. Taylor, “Affinity-purified antibodies of defined specificity for use in a solid-phase microplate radioimmunoassay of human Tamm-Horsfall glycoprotein in urine,” The The Biochemical Journal, vol. 227, no. 3, pp. 957–963, 1994. View at Scopus
  76. J. A. Gokhale, P. A. Glenton, and S. R. Khan, “Biochemical and quantitative analysis of Tamm Horsfall protein in rats,” Urological Research, vol. 25, no. 5, pp. 347–354, 1997. View at Publisher · View at Google Scholar · View at Scopus
  77. F. K. Stevenson, A. J. Cleave, and P. W. Kent, “The effect of ions on the viscometric and ultracentrifugal behaviour of Tamm-Horsfall glycoprotein,” Biochimica et Biophysica Acta, vol. 236, no. 1, pp. 59–66, 1971. View at Scopus
  78. F. Serafini-Cessi, N. Malagolini, and D. Cavallone, “Tamm-Horsfall glycoprotein: biology and clinical relevance,” American Journal of Kidney Diseases, vol. 42, no. 4, pp. 658–676, 2003. View at Publisher · View at Google Scholar · View at Scopus
  79. L. Mo, H.-Y. Huang, X.-H. Zhu, E. Shapiro, D. L. Hasty, and X.-R. Wu, “Tamm-Horsfall protein is a critical renal defense factor protecting against calcium oxalate crystal formation,” Kidney International, vol. 66, no. 3, pp. 1159–1166, 2004. View at Publisher · View at Google Scholar · View at Scopus
  80. K. Kaneko, R. Kobayashi, M. Yasuda, Y. Izumi, T. Yamanobe, and T. Shimizu, “Comparison of matrix proteins in different types of urinary stone by proteomic analysis using liquid chromatography-tandem mass spectrometry,” International Journal of Urology, vol. 19, no. 8, pp. 765–772, 2012. View at Publisher · View at Google Scholar · View at Scopus
  81. W. G. Robertson, D. S. Scurr, and C. M. Bridge, “Factors influencing the crystallisation of calcium oxalate in urine—critique,” Journal of Crystal Growth, vol. 53, no. 1, pp. 182–194, 1981. View at Scopus
  82. B. Fellstrom, B. G. Danielson, S. Ljunghall, and B. Wikstrom, “Crystal inhibition: the effects of polyanions on calcium oxalate crystal growth,” Clinica Chimica Acta, vol. 158, no. 3, pp. 229–235, 1986. View at Scopus
  83. P. K. Grover, V. R. Marshall, and R. L. Ryall, “Tamm-Horsfall mucoprotein reduces promotion of calcium oxalate crystal aggregation induced by urate in human urine in vitro,” Clinical Science, vol. 87, no. 2, pp. 137–142, 1994. View at Scopus
  84. G. A. Rose and S. Sulaiman, “Tamm-Horsfall mucoproteins promote calcium oxalate crystal formation in urine: quantitative studies,” The Journal of Urology, vol. 127, no. 1, pp. 177–179, 1982. View at Scopus
  85. T. Yoshioka, T. Koide, M. Utsunomiya, H. Itatani, T. Oka, and T. Sonoda, “Possible role of Tamm-Horsefall glycoprotein in calcium oxalate crystallisation,” British Journal of Urology, vol. 64, no. 5, pp. 463–467, 1989. View at Scopus
  86. K. A. Edyvane, C. M. Hibberd, R. M. Harnett, V. R. Marshall, and R. L. Ryall, “Macromolecules inhibit calcium oxalate crystal growth and aggregation in whole human urine,” Clinica Chimica Acta, vol. 167, no. 3, pp. 329–338, 1987. View at Scopus
  87. C. Thornley, A. Dawnay, and W. R. Cattell, “Human Tamm-Horsfall glycoprotein: urinary and plasma levels in normal subjects and patients with renal disease determined by a fully validated radioimmunoassay,” Clinical Science, vol. 68, no. 5, pp. 529–535, 1985. View at Scopus
  88. S. R. Marengo, D. H. C. Chen, H. L. C. Kaung, M. I. Resnick, and L. Yang, “Decreased renal expression of the putative calcium oxalate inhibitor Tamm-Horsfall protein in the ethylene glycol rat model of calcium oxalate urolithiasis,” The Journal of Urology, vol. 167, no. 5, pp. 2192–2197, 2002. View at Scopus
  89. S. Katsuma, S. Shiojima, A. Hirasawa et al., “Global analysis of differentially expressed genes during progression of calcium oxalate nephrolithiasis,” Biochemical and Biophysical Research Communications, vol. 296, no. 3, pp. 544–552, 2002. View at Publisher · View at Google Scholar · View at Scopus
  90. B. Hess, “The role of Tamm-Horsfall glycoprotein and nephrocalcin in calcium oxalate monohydrate crystallization processes,” Scanning Microscopy, vol. 5, no. 3, pp. 689–696, 1991. View at Scopus
  91. B. Hess, M. Jaggi, L. Zipperle, and P. Jaeger, “Reduced carbohydrate content of Tamm-Horsfall glycoprotein (THP) from severely recurrent Renal Calcium Stone Formers (RCSF),” Journal of American Society of Nephrology, vol. 6, pp. 949–952, 1995.
  92. P. Schnierle, “A simple diagnostic method for the differentiation of Tamm-Horsfall glycoproteins from healthy probands and those from recurrent calcium oxalate renal stone formers,” Experientia, vol. 51, no. 11, pp. 1068–1072, 1995. View at Publisher · View at Google Scholar · View at Scopus
  93. Y. Nakagawa, E. T. Kaiser, and F. L. Coe, “Isolation and characterization of calcium oxalate crystal growth inhibitors from human urine,” Biochemical and Biophysical Research Communications, vol. 84, no. 4, pp. 1038–1044, 1978. View at Scopus
  94. Y. Nakagawa, H. C. Margolis, S. Yokoyama, F. J. Kézdy, E. T. Kaiser, and F. L. Coe, “Purification and characterization of a calcium oxalate monohydrate crystal growth inhibitor from human kidney tissue culture medium,” The Journal of Biological Chemistry, vol. 256, no. 8, pp. 3936–3944, 1981. View at Scopus
  95. Y. Nakagawa, V. Abram, and F. J. Kezdy, “Purification and characterization of the principal inhibitor of calcium oxalate monohydrate crystal growth in human urine,” The Journal of Biological Chemistry, vol. 258, no. 20, pp. 12594–12600, 1983. View at Scopus
  96. Y. Nakagawa, J. H. Parks, F. J. Kézdy, and F. L. Coe, “Molecular abnormality of urinary glycoprotein crystal growth inhibitor in calcium nephrolithiasis,” Transactions of the Association of American Physicians, vol. 98, pp. 281–289, 1985. View at Scopus
  97. F. L. Coe, H. C. Margolis, L. H. Deutsch, and A. L. Strauss, “Urinary macromolecular crystal growth inhibitors in calcium nephrolithiasis,” Mineral and Electrolyte Metabolism, vol. 3, no. 5, pp. 268–275, 1980. View at Scopus
  98. Y. Nakagawa, M. Ahmed, and S. L. Hall, “Isolation from human calcium oxalate renal stones of nephrocalcin, a glycoprotein inhibitor of calcium oxalate crystal growth. Evidence that nephrocalcin from patients with calcium oxalate nephrolithiasis is deficient in γ-carboxyglutamic acid,” The Journal of Clinical Investigation, vol. 79, no. 6, pp. 1782–1787, 1987. View at Scopus
  99. D. Mustafi and Y. Nakagawa, “Characterization of Ca2+-binding sites in the kidney stone inhibitor glycoprotein nephrocalcin using vanadyl ions: different metal binding properties in strong and weak inhibitor proteins revealed by EPR and ENDOR,” Biochemistry, vol. 35, no. 47, pp. 14703–14709, 1996. View at Scopus
  100. Y. Nakagawa, “Properties and function of nephrocalcin: mechanism of kidney stone inhibition or promotion,” The Keio Journal of Medicine, vol. 46, no. 1, pp. 1–9, 1997. View at Scopus
  101. Y. Nakagawa, M. Netzer, and F. L. Coe, “Immunohistochemical localization of nephrocalcin (NC) to proximal tubule and thick ascending limb of Henle's loop (TALH) of human and mouse kidney: resolution of a conflict,” Kidney International, vol. 37, p. 474, 1990.
  102. Y. Nakagawa, D. Sirivongs, M. B. Novy et al., “Nephrocalcin: biosynthesis by human renal carcinoma cells in vitro and in vivo,” Cancer Research, vol. 52, no. 6, pp. 1573–1579, 1992. View at Scopus
  103. B. Hess, Y. Nakagawa, and F. L. Coe, “Nephrocalcin isolated from human kidney stones is a defective calcium-oxalate-monohydrate crystal-aggregation inhibitor,” in Urolithiasis, V. R. Walker, R. A. L. Sutton, E. C. Cameron, C. Y. C. Pak, and W. G. Robertson, Eds., p. 137, Plenum, New York, NY, USA, 1989.
  104. K. Hochstrasser, P. Reisinger, G. Albrecht, E. Wachter, and O. L. Schonberger, “Isolation of acid-resistant urinary trypsin inhibitors by high performance liquid chromatography and their characterization by N-terminal amino-acid sequence determination,” Hoppe-Seyler's Zeitschrift fur Physiologische Chemie, vol. 365, no. 9, pp. 1123–1130, 1984. View at Scopus
  105. E. M. Worcester, J. L. Sebastian, J. G. Hiatt, A. M. Beshensky, and J. A. Sadowski, “The effect of warfarin on urine calcium oxalate crystal growth inhibition and urinary excretion of calcium and nephrocalcin,” Calcified Tissue International, vol. 53, no. 4, pp. 242–248, 1993. View at Scopus
  106. Y. Tang, P. K. Grover, R. L. Moritz, J. Simpson, and R. L. Ryall, “Is nephrocalcin related to the urinary derivative (bikunin) of inter-α-trypsin inhibitor?” British Journal of Urology, vol. 76, no. 4, pp. 425–430, 1995. View at Scopus
  107. F. Atmani, B. Lacour, T. Drueke, and M. Daudon, “Isolation and purification of a new glycoprotein from human urine inhibiting calcium oxalate crystallization,” Urological Research, vol. 21, no. 1, pp. 61–66, 1993. View at Publisher · View at Google Scholar · View at Scopus
  108. F. P. Reinholt, K. Hultenby, A. Oldberg, and D. Heinegard, “Osteopontin—a possible anchor of osteoclasts to bone,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 12, pp. 4473–4475, 1990. View at Publisher · View at Google Scholar · View at Scopus
  109. C. W. Prince, T. Oosawa, W. T. Butler et al., “Isolation, characterization, and biosynthesis of a phosphorylated glycoprotein from rat bone,” The Journal of Biological Chemistry, vol. 262, no. 6, pp. 2900–2907, 1987. View at Scopus
  110. A. Oldberg, A. Franzen, and D. Heinegard, “Cloning and sequence analysis of rat bone sialoprotein (osteopontin) cDNA reveals an Arg-Gly-Asp cell-binding sequence,” Proceedings of the National Academy of Sciences of the United States of America, vol. 83, no. 23, pp. 8819–8823, 1986. View at Scopus
  111. L. Addadi and S. Weiner, “Interactions between acidic proteins and crystals: stereochemical requirements in biomineralization,” Proceedings of the National Academy of Sciences of the United States of America, vol. 82, no. 12, pp. 4110–4114, 1985. View at Scopus
  112. E. R. O'Brien, M. R. Garvin, D. K. Stewart et al., “Osteopontin is synthesized by macrophage, smooth muscle, and endothelial cells in primary and restenotic human coronary atherosclerotic plaques,” Arteriosclerosis and Thrombosis, vol. 14, no. 10, pp. 1648–1656, 1994. View at Scopus
  113. H. Shiraga, W. Min, W. J. VanDusen et al., “Inhibition of calcium oxalate crystal growth in vitro by uropontin: another member of the aspartic acid-rich protein superfamily,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 1, pp. 426–430, 1992. View at Scopus
  114. M. C. Kiefr, D. M. Bauer, and P. J. Barr, “The cDNA and derived amino acid sequence for human osteopontin,” Nucleic Acids Research, vol. 17, no. 8, p. 3306, 1989. View at Scopus
  115. A. Franzen and D. Heinegard, “Isolation and characterization of two sialoproteins present only in bone calcified matrix,” The Biochemical Journal, vol. 232, no. 3, pp. 715–724, 1985. View at Scopus
  116. E. M. Worcester, “Urinary calcium oxalate crystal growth inhibitors,” Journal of the American Society of Nephrology, vol. 5, no. 1, pp. S46–S53, 1994. View at Scopus
  117. D. R. Basavaraj, C. S. Biyani, A. J. Browning, and J. J. Cartledge, “The role of urinary kidney stone inhibitors and promoters in the pathogenesis of calcium containing renal stones,” EAU-EBU Update Series, vol. 5, no. 3, pp. 126–136, 2007. View at Publisher · View at Google Scholar · View at Scopus
  118. B. M. Fraij, “Separation and identification of urinary proteins and stone-matrix proteins by mini-slab sodium dodecyl sulfate-polyacrylamide gel electrophoresis,” Clinical Chemistry, vol. 35, no. 4, pp. 658–662, 1989. View at Scopus
  119. S. Iida, A. B. Peck, K. J. Byer, and S. R. Khan, “Expression of bikunin mRNA in renal epithelial cells after oxalate exposure,” The Journal of Urology, vol. 162, no. 4, pp. 1480–1486, 1999. View at Publisher · View at Google Scholar · View at Scopus
  120. M. L. Merchant, T. D. Cummins, D. W. Wilkey et al., “Proteomic analysis of renal calculi indicates an important role for inflammatory processes in calcium stone formation,” American Journal of Physiology, vol. 295, no. 4, pp. F1254–F1258, 2008. View at Publisher · View at Google Scholar · View at Scopus
  121. B. K. Canales, L. Anderson, L. Higgins et al., “Proteome of human calcium kidney stones,” Urology, vol. 76, no. 4, pp. 1017.e13–1017.e20, 2010. View at Publisher · View at Google Scholar · View at Scopus
  122. E. M. Worcester and A. M. Beshensky, “Osteopontin inhibits nucleation of calcium oxalate crystals,” Annals of the New York Academy of Sciences, vol. 760, pp. 375–377, 1995. View at Publisher · View at Google Scholar · View at Scopus
  123. S. Nishio, M. Hatanaka, H. Takeda et al., “Calcium phosphate crystal-associated proteins: α2-HS-glycoprotein, prothrombin F1, and osteopontin,” Molecular Urology, vol. 4, no. 4, pp. 383–390, 2000. View at Scopus
  124. B. Christensen, T. E. Petersen, and E. S. Sørensen, “Post-translational modification and proteolytic processing of urinary osteopontin,” The Biochemical Journal, vol. 411, no. 1, pp. 53–61, 2008. View at Publisher · View at Google Scholar · View at Scopus
  125. W. H. Boyce, J. King, and M. Fielden, “Total Non-Dialyzable Solids (TNDS) in human urine XIII. Immunological detection of a component peculiar to renal calculous matrix and to urine of calculous patients,” The Journal of Clinical Investigation, vol. 41, no. 5, pp. 1180–1189, 1962. View at Publisher · View at Google Scholar
  126. B. Dussol, S. Geider, A. Lilova et al., “Analysis of the soluble organic matrix of five morphologically different kidney stones. Evidence for a specific role of albumin in the constitution of the stone protein matrix,” Urological Research, vol. 23, no. 1, pp. 45–51, 1995. View at Publisher · View at Google Scholar · View at Scopus
  127. C. Cerini, S. Geider, B. Dussol et al., “Nucleation of calcium oxalate crystals by albumin: involvement in the prevention of stone formation,” Kidney International, vol. 55, no. 5, pp. 1776–1786, 1999. View at Publisher · View at Google Scholar · View at Scopus
  128. K. Suzuki, M. Moriyama, C. Nakajima et al., “Isolation and partial characterization of crystal matrix protein as a potent inhibitor of calcium oxalate crystal aggregation: evidence of activation peptide of human prothrombin,” Urological Research, vol. 22, no. 1, pp. 45–50, 1994. View at Scopus
  129. R. L. Ryall, P. K. Grover, A. M. F. Stapleton et al., “The urinary FI activation peptide of human prothrombin is a potent inhibitor of calcium oxalate crystallization in undiluted human urine in vitro,” Clinical Science, vol. 89, no. 5, pp. 533–541, 1995. View at Scopus
  130. P. K. Grover and R. L. Ryall, “Inhibition of calcium oxalate crystal growth and aggregation by prothrombin and its fragments in vitro: relationship between protein structure and inhibitory activity,” European Journal of Biochemistry, vol. 263, no. 1, pp. 50–56, 1999. View at Publisher · View at Google Scholar · View at Scopus
  131. P. K. Grover and R. L. Ryall, “Effect of prothrombin and its activation fragments on calcium oxalate crystal growth and aggregation in undiluted human urine in vitro: relationship between protein structure and inhibitory activity,” Clinical Science, vol. 102, no. 4, pp. 425–434, 2002. View at Publisher · View at Google Scholar · View at Scopus
  132. S. Tardivel, J. Médétognon, C. Randoux et al., “Alpha-1-microglobulin: inhibitory effect on calcium oxalate crystallization in vitro and decreased urinary concentration in calcium oxalate stone formers,” Urological Research, vol. 27, no. 4, pp. 243–249, 1999. View at Publisher · View at Google Scholar · View at Scopus
  133. S. N. Pillay, J. R. Asplin, and F. L. Coe, “Evidence that calgranulin is produced by kidney cells and is an inhibitor of calcium oxalate crystallization,” American Journal of Physiology, vol. 275, no. 2 part 2, pp. F255–F261, 1998. View at Scopus
  134. S. Mushtaq, A. A. Siddiqui, Z. A. Naqvi et al., “Identification of myeloperoxidase, α-defensin and calgranulin in calcium oxalate renal stones,” Clinica Chimica Acta, vol. 384, no. 1-2, pp. 41–47, 2007. View at Publisher · View at Google Scholar · View at Scopus
  135. J. Bennett, S. P. Dretler, J. Selengut, and W. H. Orme-Johnson, “Identification of the calcium-binding protein calgranulin in the matrix of struvite stones,” Journal of Endourology, vol. 8, no. 2, pp. 95–98, 1994. View at Scopus
  136. F. Atmani, J. Mizon, and S. R. Khan, “Identification of uronic-acid-rich protein as urinary bikunin, the light chain of inter-α-inhibitor,” European Journal of Biochemistry, vol. 236, no. 3, pp. 984–990, 1996. View at Scopus
  137. M. Steinbuch, “The inter-alpha-trypsin inhibitor,” Methods in Enzymology, vol. 45, pp. 760–772, 1976. View at Publisher · View at Google Scholar · View at Scopus
  138. F. Atmani, B. Lacour, P. Jungers, T. Drüeke, and M. Daudon, “Reduced inhibitory activity of uronic-acid-rich protein in urine of stone formers,” Urological Research, vol. 22, no. 4, pp. 257–260, 1994. View at Publisher · View at Google Scholar · View at Scopus
  139. J. Médétognon-Benissan, S. Tardivel, C. Hennequin, M. Daudon, T. Drüeke, and B. Lacour, “Inhibitory effect of bikunin on calcium oxalate crystallization in vitro and urinary bikunin decrease in renal stone formers,” Urological Research, vol. 27, no. 1, pp. 69–75, 1999. View at Publisher · View at Google Scholar · View at Scopus
  140. F. Atmani and S. R. Khan, “Role of urinary bikunin in the inhibition of calcium oxalate crystallization,” Journal of the American Society of Nephrology, vol. 10, no. 14, pp. S385–S388, 1999. View at Scopus
  141. S. Ebisuno, M. Nishihata, T. Inagaki, M. Umehara, and Y. Kohjimoto, “Bikunin prevents adhesion of calcium oxalate crystal to renal tubular cells in human urine,” Journal of the American Society of Nephrology, vol. 10, no. 14, pp. S436–S440, 1999. View at Scopus
  142. J. M. Verdier, B. Dussol, P. Casanova et al., “Renal lithostathine, a new inhibitor of urinary stones formation,” Nephrologie, vol. 14, no. 6, pp. 261–264, 1993. View at Scopus
  143. S. Geider, B. Dussol, S. Nitsche et al., “Calcium carbonate crystals promote calcium oxalate crystallization by heterogeneous or epitaxial nucleation: possible involvement in the control of urinary lithogenesis,” Calcified Tissue International, vol. 59, no. 1, pp. 33–37, 1996. View at Publisher · View at Google Scholar · View at Scopus
  144. P. K. Grover, D. S. Kim, and R. L. Ryall, “The effect of seed crystals of hydroxyapatite and brushite on the crystallization of calcium oxalate in undiluted human urine in vitro: implications for urinary stone pathogenesis,” Molecular Medicine, vol. 8, no. 4, pp. 200–209, 2002. View at Scopus
  145. P. Priyadarshini, S. K. Singh, and C. Tandon, “Mass spectrometric identification of human phosphate cytidylyltransferase 1 as a novel calcium oxalate crystal growth inhibitor purified from human renal stone matrix,” Clinica Chimica Acta, vol. 408, no. 1-2, pp. 34–38, 2009. View at Publisher · View at Google Scholar · View at Scopus
  146. P. Priyadarshini, P. K. Naik, D. Sengupta, S. K. Singh, and C. D. Tandon, “Mode of interaction of calcium oxalate crystal with human phosphate cytidylyltransferase 1: a novel inhibitor purified from human renal stone matrix,” Journal of Biomedical Science and Engineering, vol. 4, no. 9, pp. 591–598, 2011. View at Publisher · View at Google Scholar · View at Scopus
  147. E. A. Sorokina, J. A. Wesson, and J. G. Kleinman, “An acidic peptide sequence of nucleolin-related protein can mediate the attachment of calcium oxalate to renal tubule cells,” Journal of the American Society of Nephrology, vol. 15, no. 8, pp. 2057–2065, 2004. View at Publisher · View at Google Scholar · View at Scopus
  148. K. P. Aggarwal, S. Tandon, P. K. Naik, S. K. Singh, and C. D. Tandon, “Novel antilithiatic cationic proteins from human calcium oxalate renal stone matrix identified by MALDI-TOF-MS endowed with cytoprotective potential: an insight into molecular mechanism of urolithiasis,” Clinica Chimica Acta, vol. 415, pp. 181–190, 2012.
  149. V. Kumar, S. Yu, G. Farell, F. G. Toback, and J. C. Lieske, “Renal epithelial cells constitutively produce a protein that blocks adhesion of crystals to their surface,” American Journal of Physiology, vol. 287, no. 3, pp. F373–F383, 2004. View at Publisher · View at Google Scholar · View at Scopus
  150. C. F. Verkoelen, “Crystal retention in renal stone disease: a crucial role for the glycosaminoglycan hyaluronan?” Journal of the American Society of Nephrology, vol. 17, no. 6, pp. 1673–1687, 2006. View at Publisher · View at Google Scholar · View at Scopus
  151. A. Verhulst, M. Asselman, V. P. Persy et al., “Crystal retention capacity of cells in the human nephron: involvement of CD44 and its ligands hyaluronic acid and osteopontin in the transition of a crystal binding—into a nonadherent epithelium,” Journal of the American Society of Nephrology, vol. 14, no. 1, pp. 107–115, 2003. View at Publisher · View at Google Scholar · View at Scopus
  152. M. Asselman, A. Verhulst, M. E. De Broe, and C. F. Verkoelen, “Calcium oxalate crystal adherence to Hyaluronan-, osteopontin-, and CD44-expressing injured/regenerating tubular epithelial cells in rat kidneys,” Journal of the American Society of Nephrology, vol. 14, no. 12, pp. 3155–3166, 2003. View at Publisher · View at Google Scholar · View at Scopus
  153. S. Chutipongtanate, Y. Nakagawa, S. Sritippayawan et al., “Identification of human urinary trefoil factor 1 as a novel calcium oxalate crystal growth inhibitor,” Journal of Clinical Investigation, vol. 115, no. 12, pp. 3613–3622, 2005. View at Publisher · View at Google Scholar · View at Scopus
  154. V. Thongboonkerd, S. Chutipongtanate, T. Semangoen, and P. Malasit, “Urinary trefoil factor 1 is a novel potent inhibitor of calcium oxalate crystal growth and aggregation,” The Journal of Urology, vol. 179, no. 4, pp. 1615–1619, 2008. View at Publisher · View at Google Scholar · View at Scopus
  155. M. J. Kim and F. W. K. Tam, “Urinary monocyte chemoattractant protein-1 in renal disease,” Clinica Chimica Acta, vol. 412, no. 23-24, pp. 2022–2030, 2011. View at Publisher · View at Google Scholar · View at Scopus
  156. T. Umekawa, N. Chegini, and S. R. Khan, “Oxalate ions and calcium oxalate crystals stimulate MCP-1 expression by renal epithelial cells,” Kidney International, vol. 61, no. 1, pp. 105–112, 2002. View at Publisher · View at Google Scholar · View at Scopus
  157. V. Kumar, G. Farell, S. Deganello, and J. C. Lieske, “Annexin II is present on renal epithelial cells and binds calcium oxalate monohydrate crystals,” Journal of the American Society of Nephrology, vol. 14, no. 2, pp. 289–297, 2003. View at Publisher · View at Google Scholar · View at Scopus
  158. D. Proudfoot and C. M. Shanahan, “Molecular mechanisms mediating vascular calcification: role of matrix Gla protein,” Nephrology, vol. 11, no. 5, pp. 455–461, 2006. View at Publisher · View at Google Scholar · View at Scopus
  159. B. Gao, T. Yasui, Y. Itoh, K. Tozawa, Y. Hayashi, and K. Kohri, “A polymorphism of matrix Gla protein gene is associated with kidney stones,” The Journal of Urology, vol. 177, no. 6, pp. 2361–2365, 2007. View at Publisher · View at Google Scholar · View at Scopus
  160. M. L. Cancela, B. Hu, and P. A. Price, “Effect of cell density and growth factors on matrix GLA protein expression by normal rat kidney cells,” Journal of Cellular Physiology, vol. 171, no. 2, pp. 125–134, 1997. View at Publisher · View at Google Scholar
  161. X. Lu, B. Gao, T. Yasui et al., “Matrix Gla protein is involved in crystal formation in kidney of hyperoxaluric rats,” Kidney and Blood Pressure Research, vol. 37, no. 1, pp. 15–23, 2013. View at Publisher · View at Google Scholar
  162. B. Gao, T. Yasui, X. Lu et al., “Matrix Gla protein expression in NRK-52E cells exposed to oxalate and calcium oxalate monohydrate crystals,” Urologia Internationalis, vol. 85, no. 2, pp. 237–241, 2010. View at Publisher · View at Google Scholar · View at Scopus
  163. P. Latha, P. Kalaiselvi, P. Varalakshmi, and G. Rameshkumar, “Characterization of histone (H1B) oxalate binding protein in experimental urolithiasis and bioinformatics approach to study its oxalate interaction,” Biochemical and Biophysical Research Communications, vol. 345, no. 1, pp. 345–354, 2006. View at Publisher · View at Google Scholar · View at Scopus
  164. L. P. Brown, B. Berse, L. Van De Water et al., “Expression and distribution of osteopontin in human tissues: widespread association with luminal epithelial surfaces,” Molecular Biology of the Cell, vol. 3, no. 10, pp. 1169–1180, 1992. View at Scopus
  165. J. R. Hoyer, “Uropontin in urinary calcium stone formation,” Mineral and Electrolyte Metabolism, vol. 760, no. 6, pp. 375–377, 1995. View at Scopus
  166. J. A. Wesson, E. M. Worcester, J. H. Wiessner, N. S. Mandel, and J. G. Kleinman, “Control of calcium oxalate crystal structure and cell adherence by urinary macromolecules,” Kidney International, vol. 53, no. 4, pp. 952–957, 1998. View at Publisher · View at Google Scholar · View at Scopus
  167. R. C. Hedgepeth, L. Yang, M. I. Resnick, and S. R. Marengo, “Expression of proteins that inhibit calcium oxalate crystallization in vitro in the urine of normal and stone-forming individuals,” American Journal of Kidney Diseases, vol. 37, no. 1, pp. 104–112, 2001. View at Scopus
  168. T. Yamate, H. Tsuji, N. Amasaki, M. Iguchi, T. Kurita, and K. Kohri, “Analysis of osteopontin DNA in patients with urolithiasis,” Urological Research, vol. 28, no. 3, pp. 159–166, 2000. View at Scopus
  169. A. M. F. Stapleton, R. J. Simpson, and R. L. Ryall, “Crystal matrix protein is related to human prothrombin,” Biochemical and Biophysical Research Communications, vol. 195, no. 3, pp. 1199–1203, 1993. View at Publisher · View at Google Scholar · View at Scopus
  170. A. M. F. Stapleton and R. L. Ryall, “Blood coagulation proteins and urolithiasis are linked: crystal matrix protein is the F1 activation peptide of human prothrombin,” British Journal of Urology, vol. 75, no. 6, pp. 712–719, 1995. View at Scopus
  171. K. Suzuki, T. Tanaka, K. Miyazawa et al., “Gene expression of prothrombin in human and rat kidneys: basic and clinical approach,” Journal of the American Society of Nephrology, vol. 10, no. 14, pp. S408–S411, 1999. View at Scopus
  172. A. M. F. Stapleton and R. L. Ryall, “Crystal matrix protein—getting blood out of a stone,” Mineral and Electrolyte Metabolism, vol. 20, no. 6, pp. 399–409, 1995. View at Scopus
  173. A. M. F. Stapleton, A. E. Seymour, J. S. Brennan, I. R. Doyle, V. R. Marshall, and R. L. Ryall, “Immunohistochemical distribution and quantification of crystal matrix protein,” Kidney International, vol. 44, no. 4, pp. 817–824, 1993. View at Scopus
  174. A. M. F. Stapleton, T. L. Timme, and R. L. Ryall, “Gene expression of prothrombin in the human kidney and its potential relevance to kidney stone disease,” British Journal of Urology, vol. 81, no. 5, pp. 666–672, 1998. View at Publisher · View at Google Scholar · View at Scopus
  175. J.-P. Salier, “Inter-α-trypsin inhibitor: emergence of a family within the Kunitz-type protease inhibitor superfamily,” Trends in Biochemical Sciences, vol. 15, no. 11, pp. 435–439, 1990. View at Scopus
  176. C. Franck and J. Z. Pedersen, “Trypsin-inhibitory activities of acid-stable fragments of the inter-alpha-trypsin inhibitor in inflammatory and uraemic conditions,” Scandinavian Journal of Clinical and Laboratory Investigation, vol. 43, no. 2, pp. 151–155, 1983. View at Scopus
  177. R. K. Chawla, D. J. Rausch, F. W. Miller, W. R. Vogler, and D. H. Lawson, “Abnormal profile of serum proteinase inhibitors in cancer patients,” Cancer Research, vol. 44, no. 6, pp. 2718–2723, 1984. View at Scopus
  178. N. Toki and H. Sumi, “Urinary trypsin inhibitor and urokinase activities in renal diseases,” Acta Haematologica, vol. 67, no. 2, pp. 109–113, 1982. View at Scopus
  179. J. Bauer and Z. Reich, “Uber die antitryptische. Wirkung des Harns,” in Medizinische Klinik, vol. 46, pp. 1744–1747, 1909.
  180. F. Atmani, B. Lacour, G. Strecker, P. Parvy, T. Drueke, and M. Daudon, “Molecular characteristics of uronic-acid-rich protein, a strong inhibitor of calcium oxalate crystallization in vitro,” Biochemical and Biophysical Research Communications, vol. 191, no. 3, pp. 1158–1165, 1993. View at Publisher · View at Google Scholar · View at Scopus
  181. K. Hochstrasser, G. Bretzel, H. Feuth, W. Hilla, and K. Lempart, “The inter α trypsin inhibitor as precursor of the acid stable proteinase inhibitors in human serum and urine,” Hoppe-Seyler's Zeitschrift fur Physiologische Chemie, vol. 357, no. 2, pp. 153–162, 1976. View at Scopus
  182. J. J. Enghild, I. B. Thogersen, S. V. Pizzo, and G. Salvesen, “Analysis of inter-α-trypsin inhibitor and a novel trypsin inhibitor, pre-α-trypsin inhibitor, from human plasma. Polypeptide chain stoichiometry and assembly by glycan,” The Journal of Biological Chemistry, vol. 264, no. 27, pp. 15975–15981, 1989. View at Scopus
  183. U. Janssen, G. Thomas, T. Glant, and A. Phillips, “Expression of inter-α-trypsin inhibitor and tumor necrosis factor-stimulated gene 6 in renal proximal tubular epithelial cells,” Kidney International, vol. 60, no. 1, pp. 126–136, 2001. View at Publisher · View at Google Scholar · View at Scopus
  184. S. Iida, A. B. Peck, J. Johnson-Tardieu et al., “Temporal changes in mRNA expression for bikunin in the kidneys of rats during calcium oxalate nephrolithiasis,” Journal of the American Society of Nephrology, vol. 10, no. 5, pp. 986–996, 1999. View at Scopus
  185. S. Suzuki, H. Kobayashi, S. Kageyama, K. Shibata, M. Fujie, and T. Terao, “Excretion of bikunin and its fragments in the urine of patients with renal stones,” The Journal of Urology, vol. 166, no. 1, pp. 268–274, 2001. View at Scopus
  186. C. Dean, J. Kanellos, H. Pham et al., “Effects of inter-α-inhibitor and several of its derivatives on calcium oxalate crystallization in vitro,” Clinical Science, vol. 98, no. 4, pp. 471–480, 2000. View at Scopus
  187. H. Kobayashi, K. Shibata, M. Fujie, D. Sugino, and T. Terao, “Identification of structural domains in inter-α-trypsin inhibitor involved in calcium oxalate crystallization,” Kidney International, vol. 53, no. 6, pp. 1727–1735, 1998. View at Publisher · View at Google Scholar · View at Scopus
  188. M. Okuyama, S. Yamaguchi, and S. Yachiku, “Identification of bikunin isolated from human urine inhibits calcium oxalate crystal growth and its localization in the kidneys,” International Journal of Urology, vol. 10, no. 10, pp. 530–535, 2003. View at Publisher · View at Google Scholar · View at Scopus
  189. F. Atmani, F. J. Opalko, and S. R. Khan, “Association of urinary macromolecules with calcium oxalate crystals induced in vitro in normal human and rat urine,” Urological Research, vol. 24, no. 1, pp. 45–50, 1996. View at Publisher · View at Google Scholar · View at Scopus
  190. D. Zimmer, E. Cornwall, A. Landar, and W. Song, “The S100 protein family: history, function, and expression,” Brain Research Bulletin, vol. 37, no. 4, pp. 417–429, 1995. View at Publisher · View at Google Scholar · View at Scopus
  191. Y. Naito, Y. Ohtawara, S. Kageyama et al., “Morphological analysis of renal cell culture models of calcium phosphate stone formation,” Urological Research, vol. 25, no. 1, pp. 59–65, 1997. View at Publisher · View at Google Scholar · View at Scopus
  192. J. M. Verdier, B. Dussol, P. Casanova et al., “Evidence that human kidney produces a protein similar to lithostathine, the pancreatic inhibitor of CaCO3 crystal growth,” European Journal of Clinical Investigation, vol. 22, no. 7, pp. 469–474, 1992. View at Scopus
  193. F. Atmani, P. A. Glenton, and S. R. Khan, “Identification of proteins extracted from calcium oxalate and calcium phosphate crystals induced in the urine of healthy and stone forming subjects,” Urological Research, vol. 26, no. 3, pp. 201–207, 1998. View at Publisher · View at Google Scholar · View at Scopus
  194. B. Hess, U. Meinhardt, L. Zipperle, R. Giovanoli, and P. Jaeger, “Simultaneous measurements of calcium oxalate crystal nucleation and aggregation: impact of various modifiers,” Urological Research, vol. 23, no. 4, pp. 231–238, 1995. View at Publisher · View at Google Scholar · View at Scopus
  195. A. Ebrahimpour, L. Perez, and G. H. Nancollas, “Induced crystal growth of calcium oxalate monohydrate at hydroxapatite surfaces. The influence of human serum albumin, citrate, and magnesium,” Langmuir, vol. 7, no. 3, pp. 577–583, 1991. View at Scopus
  196. S. Ribieras, C. Tomasetto, and M. C. Rio, “The pS2/TFF1 trefoil factor, from basic research to clinical applications,” Biochimica et Biophysica Acta, vol. 1378, no. 1, pp. F61–F77, 1998. View at Publisher · View at Google Scholar · View at Scopus
  197. J. Y. Lee and A. P. Spicer, “Hyaluronan: a multifunctional, megaDalton, stealth molecule,” Current Opinion in Cell Biology, vol. 12, no. 5, pp. 581–586, 2000. View at Publisher · View at Google Scholar · View at Scopus
  198. B. P. Toole, “Hyaluronan in morphogenesis,” Journal of Internal Medicine, vol. 242, no. 1, pp. 35–40, 1997. View at Scopus
  199. B. P. Toole, “Developmental role of hyaluronate,” Connective Tissue Research, vol. 10, no. 1, pp. 93–100, 1982. View at Scopus
  200. V. Sibalic, X. Fan, J. Loffing, and R. P. Wüthrich, “Upregulated renal tubular CD44, hyaluronan, and osteopontin in kdkd mice with interstitial nephritis,” Nephrology Dialysis Transplantation, vol. 12, no. 7, pp. 1344–1353, 1997. View at Publisher · View at Google Scholar · View at Scopus
  201. V. Göransson, C. Johnsson, A. Jacobson, P. Heldin, R. Hällgren, and P. Hansell, “Renal hyalurona accumulation and hyaluronan synthase expression after ischaemia-reperfusion injury in the rat,” Nephrology Dialysis Transplantation, vol. 19, no. 4, pp. 823–830, 2004. View at Publisher · View at Google Scholar · View at Scopus
  202. E. Feusi, L. Sun, A. Sibalic, B. Beck-Schimmer, B. Oertli, and R. P. Wüthrich, “Enhanced hyaluronan synthesis in the MRL-Fas(lpr) kidney: role of cytokines,” Nephron, vol. 83, no. 1, pp. 66–73, 1999. View at Publisher · View at Google Scholar · View at Scopus
  203. A. Wells, E. Larsson, E. Hanas, T. Laurent, R. Hallgren, and G. Tufveson, “Increased hyaluronan in acutely rejecting human kidney grafts,” Transplantation, vol. 55, no. 6, pp. 1346–1349, 1993. View at Scopus
  204. R. P. Wüthrich, “The proinflammatory role of hyaluronan-CD44 interactions in renal injury,” Nephrology Dialysis Transplantation, vol. 14, no. 11, pp. 2554–2556, 1999. View at Scopus
  205. S. G. Jones, T. Ito, and A. O. Phillips, “Regulation of proximal tubular epithelial cell CD44-mediated binding and internalisation of hyaluronan,” The International Journal of Biochemistry and Cell Biology, vol. 35, no. 9, pp. 1361–1377, 2003. View at Publisher · View at Google Scholar · View at Scopus
  206. V. Gerke and S. E. Moss, “Annexins: from structure to function,” Physiological Reviews, vol. 82, no. 2, pp. 331–371, 2002. View at Scopus
  207. A. S. P. Ma and L. J. Ozers, “Annexins I and II show differences in subcellular localization and differentiation related changes in human epidermal keratinocytes,” Archives of Dermatological Research, vol. 288, no. 10, pp. 596–603, 1996. View at Publisher · View at Google Scholar · View at Scopus
  208. K. A. Hajjar, C. A. Guevara, E. Lev, K. Dowling, and J. Chacko, “Interaction of the fibrinolytic receptor, annexin II, with the endothelial cell surface. Essential role of endonexin repeat 2,” The Journal of Biological Chemistry, vol. 271, no. 35, pp. 21652–21659, 1996. View at Publisher · View at Google Scholar · View at Scopus
  209. D. A. Eberhard and S. R. Vandenberg, “Annexins I and II bind to lipid A: a possible role in the inhibition of endotoxins,” The Biochemical Journal, vol. 330, no. 1 part 1, pp. 67–72, 1998. View at Scopus
  210. C. M. Raynor, J. F. Wright, D. M. Waisman, and E. L. Pryzdial, “Annexin II enhances cytomegalovirus binding and fusion to phospholipid membranes,” Biochemistry, vol. 38, no. 16, pp. 5089–5095, 1999. View at Publisher · View at Google Scholar · View at Scopus
  211. D. T. Baran, J. M. Quail, R. Ray, J. Leszyk, and T. Honeyman, “Annexin II is the membrane receptor that mediates the rapid actions of 1α,25-dihydroxyvitamin D3,” Journal of Cellular Biochemistry, vol. 78, no. 1, pp. 34–46, 2000. View at Scopus
  212. K. Ma, R. Simantov, J. C. Zhang, R. Silverstein, K. A. Hajjar, and K. R. McCrae, “High affinity binding of β2-glycoprotein I to human endothelial cells is mediated by annexin II,” The Journal of Biological Chemistry, vol. 275, no. 20, pp. 15541–15548, 2000. View at Publisher · View at Google Scholar · View at Scopus
  213. K. S. Hajjar, L. Mauri, A. T. Jacovina et al., “Tissue plasminogen activator binding to the annexin II tail domain: direct modulation by homocysteine,” The Journal of Biological Chemistry, vol. 273, no. 16, pp. 9987–9993, 1998. View at Publisher · View at Google Scholar · View at Scopus
  214. L. Yan, S. Zucker, and B. P. Toole, “Roles of the multifunctional glycoprotein, emmprin (basigin; CD147), in tumour progression,” Thrombosis and Haemostasis, vol. 93, no. 2, pp. 199–204, 2005. View at Publisher · View at Google Scholar · View at Scopus
  215. G. F. Weber, S. Ashkar, M. J. Glimcher, and H. Cantor, “Receptor-ligand interaction between CD44 and osteopontin (Eta-1),” Science, vol. 271, no. 5248, pp. 509–512, 1996. View at Scopus
  216. M. Yamazaki, F. Nakajima, A. Ogasawara, H. Moriya, R. J. Majeska, and T. A. Einhorn, “Spatial and temporal distribution of CD44 and osteopontin in fracture callus,” Journal of Bone and Joint Surgery B, vol. 81, no. 3, pp. 508–515, 1999. View at Publisher · View at Google Scholar · View at Scopus
  217. C. F. Verkoelen, B. G. Van der Boom, and J. C. Romijn, “Identification of hyaluronan as a crystal-binding molecule at the surface of migrating and proliferating MDCK cells,” Kidney International, vol. 58, no. 3, pp. 1045–1054, 2000. View at Publisher · View at Google Scholar · View at Scopus
  218. J. D. Fraser and P. A. Price, “Lung, heart, and kidney express high levels of mRNA for the vitamin K-dependent matrix Gla protein. Implications for the possible functions of matrix Gla protein and for the tissue distribution of the γ-carboxylase,” The Journal of Biological Chemistry, vol. 263, no. 23, pp. 11033–11036, 1988. View at Scopus
  219. G. Luo, P. Ducy, M. D. McKee et al., “Spontaneous calcification of arteries and cartilage in mice lacking matrix GLA protien,” Nature, vol. 386, no. 6620, pp. 78–81, 1997. View at Publisher · View at Google Scholar · View at Scopus
  220. M. Murshed, T. Schinke, M. D. McKee, and G. Karsenty, “Extracellular matrix mineralization is regulated locally; different roles of two gla-containing proteins,” Journal of Cell Biology, vol. 165, no. 5, pp. 625–630, 2004. View at Publisher · View at Google Scholar · View at Scopus
  221. L. Gu, S. C. Tseng, and B. J. Rollins, “Monocyte chemoattractant protein-1,” Chemical Immunology, vol. 72, pp. 7–29, 1999. View at Scopus
  222. W. Wagner, C. Roderburg, F. Wein et al., “Molecular and secretory profiles of human mesenchymal stromal cells and their abilities to maintain primitive hematopoietic progenitors,” Stem Cells, vol. 25, no. 10, pp. 2638–2647, 2007. View at Publisher · View at Google Scholar · View at Scopus
  223. S. J. Hyduk, J. R. Chan, S. T. Duffy et al., “Phospholipase C, calcium, and calmodulin are critical for α4β1 integrin affinity up-regulation and monocyte arrest triggered by chemoattractants,” Blood, vol. 109, no. 1, pp. 176–184, 2007. View at Publisher · View at Google Scholar · View at Scopus
  224. J. S. Duffield, “Macrophages and immunologic inflammation of the kidney,” Seminars in Nephrology, vol. 30, no. 3, pp. 234–254, 2010. View at Publisher · View at Google Scholar · View at Scopus
  225. A. Yadav, V. Saini, and S. Arora, “MCP-1: chemoattractant with a role beyond immunity: a review,” Clinica Chimica Acta, vol. 411, no. 21-22, pp. 1570–1579, 2010. View at Publisher · View at Google Scholar · View at Scopus
  226. P. Pathak, S. K. Singh, and C. Tandon, “Effect of biomolecules from human renal matrix of calcium oxalate monohydrate (CaOx) stones on in vitro calcium phosphate crystallization,” International Brazilian Journal of Urology, vol. 36, no. 5, pp. 621–628, 2010. View at Publisher · View at Google Scholar · View at Scopus
  227. M. F. Moghadam, C. Tandon, S. Aggarwal et al., “Concentration of a potent calcium oxalate monohydrate crystal growth inhibitor in the urine of normal persons and kidney stone patients by ELISA-based assay system employing monoclonal antibodies,” Journal of Cellular Biochemistry, vol. 90, no. 6, pp. 1261–1275, 2003. View at Publisher · View at Google Scholar · View at Scopus
  228. S. Aggarwal, C. Tandon, M. Forouzandeh, S. K. Singla, R. Kiran, and R. K. Jethi, “Role of a protein inhibitor isolated from human renal stone matrix in urolithiasis,” Indian Journal of Biochemistry and Biophysics, vol. 42, no. 2, pp. 113–117, 2005. View at Scopus
  229. K. P. Aggarwal, S. Tandon, S. K. Singh, and C. D. Tandon, “2D map of proteins from human renal stone matrix and evaluation of their effect on oxalate induced renal tubular epithelial cell injury,” International Brazilian Journal of Urology, vol. 39, no. 1, pp. 128–136, 2013.