Detection of urinary biomarkers for early diagnosis of acute renal allograft rejection by proteomic analysis

Proteomics - Clinical Applications

Volumn 3, Issue 6, 2009, Pages 694-704

  Jia, Xiongfei ^a   Gan, Chengjun ^a   Xiao, Ke ^b   He, Weifeng ^a   Zhang, Tao ^c   Huang, Cibing ^a   Wu, Xiongfei ^a   Luo, Gaoxing ^a   Wang, Xiaojuan ^a   Hu, Jie ^a   Tan, Jiangling ^a   Zhang, Xiaorong ^a   Larsen, Peter Mose ^b   Wu, Jun ^a  

^a THIRD MILITARY MEDICAL UNIVERSITY   (China)

^b Drugmode ApS ^*  (Denmark)

^c SICHUAN UNIVERSITY   (China)

Author keywords

Acute renal rejection; Alpha 1 antichymotrypsin precursor; Biomarker; Tumor rejection antigen gp96; Zn alpha 2 glycoprotein

Indexed keywords

ALPHA 1 ANTICHYMOTRYPSIN; ALPHA2 GLYCOPROTEIN; GLYCOPROTEIN GP 96; UNCLASSIFIED DRUG; ZINC ALPHA2 GLYCOPROTEIN;

ADULT; ARTICLE; CLINICAL ARTICLE; CONTROLLED STUDY; DIAGNOSTIC ACCURACY; DIAGNOSTIC VALUE; DISEASE MARKER; DOWN REGULATION; EARLY DIAGNOSIS; FEMALE; HUMAN; KIDNEY ALLOGRAFT REJECTION; KIDNEY TRANSPLANTATION; MALE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEIN URINE LEVEL; PROTEOMICS; SENSITIVITY AND SPECIFICITY; WESTERN BLOTTING;

EID: 70350104736     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200800209     Document Type: Article

References (25)

1. Rush, D., Protocol transplant biopsies: an underutilized tool in kidney transplantation. Clin. J. Am. Soc. Nephrol. 2006, 1, 138-143.
2. Moreso, F., Ibernon, M., Goma, M., Carrera, M. et al., Subclinical rejection associated with chronic allograft nephropathy in protocol biopsies as a risk factor for late graft loss. Am. J. Transplant. 2006, 6, 747-752.
3. Sorof, J. M., Vartanian, R. K., Olson, J. L., Tomlanovich, S. J. et al., Histopathological concordance of paired renal allograft biopsy cores. Effect on the diagnosis and management of acute rejection. Transplantation 1995, 60, 1215-1219.
4. Nicholson, M. L., Wheatley, T. J., Doughman, T. M., White, S. A. et al., A prospective randomized trial of three different sizes of core-cutting needle for renal transplant biopsy. Kidney Int. 2000, 58, 390-395.
5. Wittke, S., Haubitz, M., Walden, M., Rohde, F. et al., Detection of acute tubulointerstitial rejection by proteomic analysis of urinary samples in renal transplant recipients. Am. J. Transplant. 2005, 5, 2479-2488.
6. Schaub, S., Wilkins, J. A., Nickerson, P., Proteomics and renal transplantation: searching for novel biomarkers and therapeutic targets. Contrib. Nephrol. 2008, 160, 65-75.
7. Schaub, S., Wilkins, J. A., Antonovici, M., Krokhin, O. et al., Proteomic-based identification of cleaved urinary beta2-microglobulin as a potential marker for acute tubular injury in renal allografts. Am. J. Transplant. 2005, 5, 729-738.
8. Schaub, S., Rush, D., Wilkins, J., Gibson, I. W. et al., Proteomic-based detection of urine proteins associated with acute renal allograft rejection. J. Am. Soc. Nephrol. 2004, 15, 219-227.
9. Schaub, S., Mayr, M., Honger, G., Bestland, J. et al., Detection of subclinical tubular injury after renal transplantation: comparison of urine protein analysis with allograft histopathology. Transplantation 2007, 84, 104-112.
10. O'Riordan, E., Orlova, T. N., Podust, V. N., Chander, P. N. et al., Characterization of urinary peptide biomarkers of acute rejection in renal allografts. Am. J. Transplant. 2007, 7, 930-940.
11. O'Riordan, E., Orlova, T. N., Mei, J. J., Butt, K. et al., Bioinformatic analysis of the urine proteome of acute allograft rejection. J. Am. Soc. Nephrol. 2004, 15, 3240-3248.
12. Jahnukainen, T., Malehorn, D., Sun, M., Lyons-Weiler, J. et al., Proteomic analysis of urine in kidney transplant patients with BK virus nephropathy. J. Am. Soc. Nephrol. 2006, 17, 3248-3256.
13. Clarke, W., Silverman, B. C., Zhang, Z., Chan, D. W. et al., Characterization of renal allograft rejection by urinary proteomic analysis. Ann. Surg. 2003, 237, 660-664; discussion 664-665.
14. Shevchenko, A., Jensen, O. N., Podtelejnikov, A. V., Sagliocco, F. et al., Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels. Proc. Natl. Acad. Sci. USA 1996, 93, 14440-14445.
15. Gobom, J., Nordhoff, E., Mirgorodskaya, E., Ekman, R., Roepstorff, P., Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 1999, 34, 105-116.
16. Potempa, J., Korzus, E., Travis, J., The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J. Biol. Chem. 1994, 269, 15957-15960.
17. Zhang, S., Janciauskiene, S., Multi-functional capability of proteins: alpha1-antichymotrypsin and the correlation with Alzheimer's disease. J. Alzheimers Dis. 2002, 4, 115-122.
18. Binder, R. J., Han, D. K., Srivastava, P. K., CD91: a receptor for heat shock protein gp96. Nat. Immunol. 2000, 1, 151-155.
19. Berwin, B., Hart, J. P., Pizzo, S. V., Nicchitta, C. V., Cutting edge: CD91-independent cross-presentation of GRP94(gp96)-associated peptides. J. Immunol. 2002, 168, 4282-4286.
20. Basu, S., Binder, R. J., Ramalingam, T., Srivastava, P. K., CD91 is a common receptor for heat shock proteins gp96, hsp90, hsp70, and calreticulin. Immunity 2001, 14, 303-313.
21. Singh-Jasuja, H., Hilf, N., Scherer, H. U., Arnold-Schild, D. et al., The heat shock protein gp96: a receptor-targeted cross-priming carrier and activator of dendritic cells. Cell Stress Chaperones 2000, 5, 462-470.
22. Yang, Y., Liu, B., Dai, J., Srivastava, P. K. et al., Heat shock protein gp96 is a master chaperone for toll-like receptors and is important in the innate function of macrophages. Immunity 2007, 26, 215-226.
23. Todorov, P. T., McDevitt, T. M., Meyer, D. J., Ueyama, H. et al., Purification and characterization of a tumor lipid-mobilizing factor. Cancer Res. 1998, 58, 2353-2358.
24. Tisdale, M. J., Cachexia in cancer patients. Nat. Rev. Cancer 2002, 2, 862-871.
25. Rolli, V., Radosavljevic, M., Astier, V., Macquin, C. et al., Lipolysis is altered in MHC class I zinc-alpha(2)-glycoprotein deficient mice. FEBS Lett. 2007, 581, 394-400.