All Title Author
Keywords Abstract


Role of Mindin in Diabetic Nephropathy

DOI: 10.1155/2011/486305

Full-Text   Cite this paper   Add to My Lib

Abstract:

A number of studies have shown that proinflammatory cytokines have important roles in determining the development of microvascular diabetic complications, including nephropathy. Inflammatory biomarkers should be useful for diagnosis or monitoring of diabetic nephropathy. Mindin (spondin 2) is a member of the mindin-/F-spondin family of secreted extracellular matrix (ECM) proteins. Recent studies showed that mindin is essential for initiation of innate immune response and represents a unique pattern-recognition molecule in the ECM. Previously, we demonstrated that the levels of urinary mindin in patients with type 2 diabetes were higher than those in healthy individuals. We propose that urinary mindin is a potent biomarker for the development of diabetic nephropathy. 1. Introduction Diabetic nephropathy is a major cause of end-stage kidney disease (ESKD) in the United States, Japan, and most of Europe [1]. Although the etiology of this insidious disorder is not well understood, hyperglycemia and hypertension may play pivotal roles in the pathogenesis of diabetic nephropathy. Actually, almost 30% of diabetic patients develop diabetic nephropathy despite strict blood glucose and/or blood pressure control [2]. Chronic low-grade inflammation (so-called microinflammation) has been found to play roles in the pathogenesis of diabetes [3, 4] and has been identified as a risk factor for the development of diabetes [5, 6]. Moreover, diabetes has been proposed as a disease of the innate immune system [7]. In addition, the studies in recent years have shown that inflammation and inflammatory cytokines are determinants in the development of microvascular diabetic complications such as neuropathy, retinopathy, and nephropathy [8–11]. In 1991, Hasegawa et al. reported that glomerular basement membranes from diabetic rats induced significantly greater amounts of tumor necrosis factor-α (TNF-α) and interleukin-1 (IL-1) in cultured peritoneal macrophages than when these cells were incubated with basement membranes from nondiabetic rats [12]. Based on these findings, the authors suggested for the first time that inflammatory cytokines may participate in the pathogenesis of diabetic nephropathy [12]. At present, a number of clinical studies have suggested relationships between inflammatory cytokines and diabetic nephropathy [13, 14]. Inflammatory cytokines, that is, IL-1, interleukin-6 (IL-6), and interleukin-18 (IL-18) [15, 16], vascular endothelial growth factor (VEGF) [17, 18], monocyte chemoattractant protein-1 (MCP-1) [19, 20], and transforming growth factor-β (TGF-β)

References

[1]  N. Ismail, B. Becker, P. Strzelczyk, and E. Ritz, “Renal disease and hypertension in non-insulin-dependent diabetes mellitus,” Kidney International, vol. 55, no. 1, pp. 1–28, 1999.
[2]  A. S. Krolewski, J. H. Warram, L. I. Rand, and C. R. Kahn, “Epidemiologic approach to the etiology of type I diabetes mellitus and its complications,” New England Journal of Medicine, vol. 317, no. 22, pp. 1390–1398, 1987.
[3]  J. C. Pickup, “Inflammation and activated innate immunity in the pathogenesis of type 2 diabletes,” Diabetes Care, vol. 27, no. 3, pp. 813–823, 2004.
[4]  M. Crook, “Type 2 diabetes mellitus: a disease of the innate immune system? An update,” Diabetic Medicine, vol. 21, no. 3, pp. 203–207, 2004.
[5]  A. Festa, R. D'Agostino, R. P. Tracy, and S. M. Haffner, “Elevated levels of acute-phase proteins and plasminogen activator inhibitor-1 predict the development of type 2 diabetes: the insulin resistance atherosclerosis study,” Diabetes, vol. 51, no. 4, pp. 1131–1137, 2002.
[6]  A. Rivero, C. Mora, M. Muros, J. García, H. Herrera, and J. F. Navarro-González, “Pathogenic perspectives for the role of inflammation in diabetic nephropathy,” Clinical Science, vol. 116, no. 6, pp. 479–492, 2009.
[7]  J. C. Pickup and M. A. Crook, “Is type II diabetes mellitus a disease of the innate immune system?” Diabetologia, vol. 41, no. 10, pp. 1241–1248, 1998.
[8]  J. F. Navarro and C. Mora, “Role of inflammation in diabetic complications,” Nephrology Dialysis Transplantation, vol. 20, no. 12, pp. 2601–2604, 2005.
[9]  C. Mora and J. F. Navarro, “Inflammation and diabetic nephropathy,” Current Diabetes Reports, vol. 6, no. 6, pp. 463–468, 2006.
[10]  W. J. Jeffcoate, F. Game, and P. R. Cavanagh, “The role of proinflammatory cytokines in the cause of neuropathic osteoarthropathy (acute Charcot foot) in diabetes,” Lancet, vol. 366, no. 9502, pp. 2058–2061, 2005.
[11]  N. Demircan, B. G. Safran, M. Soylu, A. A. Ozcan, and S. Sizmaz, “Determination of vitreous interleukin-1 (IL-1) and tumour necrosis factor (TNF) levels in proliferative diabetic retinopathy,” Eye, vol. 20, no. 12, pp. 1366–1369, 2006.
[12]  G. Hasegawa, K. Nakano, M. Sawada et al., “Possible role of tumor necrosis factor and interleukin-1 in the development of diabetic nephropathy,” Kidney International, vol. 40, no. 6, pp. 1007–1012, 1991.
[13]  J. F. Navarro, C. Mora, M. Maca, and J. García, “Inflammatory parameters are independently associated with urinary albumin in type 2 diabetes mellitus,” American Journal of Kidney Diseases, vol. 42, no. 1, pp. 53–61, 2003.
[14]  J. F. Navarro, C. Mora, A. Rivero et al., “Urinary protein excretion and serum tumor necrosis factor in diabetic patients with advanced renal failure: effects of pentoxifylline administration,” American Journal of Kidney Diseases, vol. 33, no. 3, pp. 458–463, 1999.
[15]  J. A. Royall, R. L. Berkow, J. S. Beckman, M. K. Cunningham, S. Matalon, and B. A. Freeman, “Tumor necrosis factor and interleukin 1 α increase vascular endothelial permeability,” American Journal of Physiology, vol. 257, pp. L399–L410, 1989.
[16]  C. Melcion, L. Lachman, and P. D. Killen, “Mesangial cells, effect of monocyte products on proliferation and matrix synthesis,” Transplantation Proceedings, vol. 14, no. 3, pp. 559–564, 1982.
[17]  T. Lenz, T. Haak, J. Malek, H. J. Gr?ne, H. Geiger, and J. Gossmann, “Vascular endothelial growth factor in diabetic nephropathy,” Kidney and Blood Pressure Research, vol. 26, no. 5-6, pp. 338–343, 2003.
[18]  H. S. Lim, G. Y. Lip, and A. D. Blann, “Angiopoietin-1 and angiopoietin-2 in diabetes mellitus: relationship to VEGF, glycaemic control, endothelial damage/dysfunction and atherosclerosis,” Atherosclerosis, vol. 180, no. 1, pp. 113–118, 2005.
[19]  N. Banba, T. Nakamura, M. Matsumura, H. Kuroda, Y. Hattori, and K. Kasai, “Possible relationship of monocyte chemoattractant protein-1 with diabetic nephropathy,” Kidney International, vol. 58, no. 2, pp. 684–690, 2000.
[20]  G. H. Tesch, “MCP-1/CCL2: a new diagnostic marker and therapeutic target for progressive renal injury in diabetic nephropathy,” American Journal of Physiology—Renal Physiology, vol. 294, no. 4, pp. F697–F701, 2008.
[21]  S. Chen, B. Jim, and F. N. Ziyadeh, “Diabetic nephropathy and transforming growth factor-β: transforming our view of glomerulosclerosis and fibrosis build-up,” Seminars in Nephrology, vol. 23, no. 6, pp. 532–543, 2003.
[22]  J. F. Navarro, F. J. Milena, C. Mora et al., “Tumor necrosis factor-α gene expression in diabetic nephropathy: relationship with urinary albumin excretion and effect of angiotensin-converting enzyme inhibition,” Kidney International, vol. 68, no. 99, pp. S-98–S-102, 2005.
[23]  E. T. Mccarthy, R. Sharma, M. Sharma et al., “TNF-α increases albumin permeability of isolated rat glomeruli through the generation of superoxide,” Journal of the American Society of Nephrology, vol. 9, no. 3, pp. 433–438, 1998.
[24]  K. Kalantarinia, A. S. Awad, and H. M. Siragy, “Urinary and renal interstitial concentrations of TNF-α increase prior to the rise in albuminuria in diabetic rats,” Kidney International, vol. 64, no. 4, pp. 1208–1213, 2003.
[25]  M. Murakoshi, M. Tanimoto, T. Gohda et al., “Mindin: a novel marker for podocyte injury in diabetic nephropathy,” Nephrology Dialysis Transplantation, vol. 26, no. 7, pp. 2153–2160, 2011.
[26]  Y. W. He, H. Li, J. Zhang et al., “The extracellular matrix protein mindin is a pattern-recognition molecule for microbial pathogens,” Nature Immunology, vol. 5, no. 1, pp. 88–97, 2004.
[27]  W. Jia, H. Li, and Y. W. He, “The extracellular matrix protein mindin serves as an integrin ligand and is critical for inflammatory cell recruitment,” Blood, vol. 106, no. 12, pp. 3854–3859, 2005.
[28]  H. Li, T. Oliver, W. Jia, and Y. W. He, “Efficient dendritic cell priming of T lymphocytes depends on the extracellular matrix protein mindin,” EMBO Journal, vol. 25, no. 17, pp. 4097–4107, 2006.
[29]  W. Jia, H. Li, and Y. W. He, “Pattern recognition molecule mindin promotes intranasal clearance of influenza viruses,” Journal of Immunology, vol. 180, no. 9, pp. 6255–6261, 2008.
[30]  Z. Li, S. Garantziotis, W. Jia et al., “The extracellular matrix protein mindin regulates trafficking of murine eosinophils into the airspace,” Journal of Leukocyte Biology, vol. 85, no. 1, pp. 124–131, 2009.
[31]  B. Guleng, Y. M. Lian, and J. L. Ren, “Mindin is upregulated during colitis and may activate NF-κB in a TLR-9 mediated manner,” World Journal of Gastroenterology, vol. 16, no. 9, pp. 1070–1075, 2010.
[32]  A. Klar, M. Baldassare, and T. M. Jessell, “F-spondin: a gene expressed at high levels in the floor plate encodes a secreted protein that promotes neural cell adhesion and neurite extension,” Cell, vol. 69, no. 1, pp. 95–110, 1992.
[33]  S. Higashijima, A. Nose, G. Eguchi, Y. Hotta, and H. Okamoto, “Mindin/F-spondin family: novel ECM proteins expressed in the zebrafish embryonic axis,” Developmental Biology, vol. 192, no. 2, pp. 211–227, 1997.
[34]  T. Umemiya, M. Takeichi, and A. Nose, “M-spondin, a novel ECM protein highly homologous to vertebrate F- spondin, is localized at the muscle attachment sites in the Drosophila embryo,” Developmental Biology, vol. 186, no. 2, pp. 165–176, 1997.
[35]  Y. Feinstein, V. Borrell, C. Garcia et al., “F-spondin and mindin: two structurally and functionally related genes expressed in the hippocampus that promote outgrowth of embryonic hippocampal neurons,” Development, vol. 126, no. 16, pp. 3637–3648, 1999.
[36]  R. Manda, T. Kohno, Y. Matsuno, S. Takenoshita, H. Kuwano, and J. Yokota, “Identification of genes (SPON2 and C20orf2) differentially expressed between cancerous and noncancerous lung cells by mRNA differential display,” Genomics, vol. 61, no. 1, pp. 5–14, 1999.
[37]  S. Zisman, K. Marom, O. Avraham et al., “Proteolysis and membrane capture of F-spondin generates combinatorial guidance cues from a single molecule,” Journal of Cell Biology, vol. 178, no. 7, pp. 1237–1249, 2007.
[38]  J. C. Adams and R. P. Tucker, “The thrombospondin type 1 repeat (TSR) superfamily: diverse proteins with related roles in neuronal development,” Developmental Dynamics, vol. 218, no. 2, pp. 280–299, 2000.
[39]  Y. Li, C. Cao, W. Jia et al., “Structure of the F-spondin domain of mindin, an integrin ligand and pattern recognition molecule,” EMBO Journal, vol. 28, no. 3, pp. 286–297, 2009.
[40]  C. McDonald and G. Nu?ez, “Mindin the fort,” Nature Immunology, vol. 5, no. 1, pp. 16–18, 2004.
[41]  S. Decramer, A. G. de Peredo, B. Breuil et al., “Urine in clinical proteomics,” Molecular and Cellular Proteomics, vol. 7, no. 10, pp. 1850–1862, 2008.
[42]  M. Okazaki, Y. Saito, Y. Udaka et al., “Diabetic nephropathy in KK and KK-Ay mice,” Experimental Animals, vol. 51, no. 2, pp. 191–196, 2002.
[43]  K. Asanuma and P. Mundel, “The role of podocytes in glomerular pathobiology,” Clinical and Experimental Nephrology, vol. 7, no. 4, pp. 255–259, 2003.
[44]  S. Adler, “Characterization of glomerular epithelial cell matrix receptors,” American Journal of Pathology, vol. 141, no. 3, pp. 571–578, 1992.
[45]  C. J. Raats, J. van den Born, M. A. Bakker et al., “Expression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathies,” American Journal of Pathology, vol. 156, no. 5, pp. 1749–1765, 2000.
[46]  H. M. Regele, E. Fillipovic, B. Langer et al., “Glomerular expression of dystroglycans is reduced in minimal change nephrosis but not in focal segmental glomerulosclerosis,” Journal of the American Society of Nephrology, vol. 11, no. 3, pp. 403–412, 2000.

Full-Text

comments powered by Disqus

Contact Us

service@oalib.com

QQ:3279437679

微信:OALib Journal