Venkatachalam, M. A. et al. Acute kidney injury: a springboard for progression in chronic kidney disease. Am. J. Physiol.-Ren. Physiol. 298, F1078–F1094 (2010).
Venkatachalam, M. A. et al. Failed tubule recovery, AKI-CKD transition, and kidney disease progression. J. Am. Soc. Nephrol. 26, 1765–1776 (2015).
Meng, X., Nikolic-Paterson, D. J. & Lan, H. Y. TGF-β: the master regulator of fibrosis. Nat. Rev. Nephrol. 12, 325–338 (2016).
Sureshbabu, A., Muhsin, S. A. & Choi, M. E. TGF-β signaling in the kidney: profibrotic and protective effects. Am. J. Physiol.-Ren. Physiol. 310, F596–F606 (2016).
Chen, J. et al. Pirfenidone inhibits macrophage infiltration in 5/6 nephrectomized rats. Am. J. Physiol.-Ren. Physiol. 304, F676–F685 (2013).
Chen, S. et al. Reversibility of established diabetic glomerulopathy by anti-TGF-beta antibodies in db/db mice. Biochem. Biophys. Res. Commun. 300, 16–22 (2003).
RamachandraRao, S. P. et al. Pirfenidone Is renoprotective in diabetic kidney disease. J. Am. Soc. Nephrol. 20, 1765–1775 (2009).
Sharma, K. et al. Neutralization of TGF-beta by anti-TGF-beta antibody attenuates kidney hypertrophy and the enhanced extracellular matrix gene expression in STZ-induced diabetic mice. Diabetes. 45, 522–530 (1996).
Ziyadeh, F. N. et al. Long-term prevention of renal insufficiency, excess matrix gene expression, and glomerular mesangial matrix expansion by treatment with monoclonal antitransforming growth factor-beta antibody in db/db diabetic mice. Proc. Natl Acad. Sci. USA 97, 8015–8020 (2000).
Huang, X. R. et al. Mice overexpressing latent TGF-β1 are protected against renal fibrosis in obstructive kidney disease. Am. J. Physiol.-Ren. Physiol. 295, F118–F127. (2008).
Huang, X. R. et al. Latent TGF-β1 protects against crescentic glomerulonephritis. J. Am. Soc. Nephrol. 19, 233–242 (2008).
Neelisetty, S. et al. Renal fibrosis is not reduced by blocking transforming growth factor-β signaling in matrix-producing interstitial cells. Kidney Int. 88, 503–514 (2015).
Li, R. X., Yiu, W. H. & Tang, S. C. Role of bone morphogenetic protein-7 in renal fibrosis. Front Physiol. 6, 114 (2015).
Mencke, R., Olauson, H. & Hillebrands, J. L. Effects of Klotho on fibrosis and cancer: a renal focus on mechanisms and therapeutic strategies. Adv. Drug Deliv. Rev. 121, 85–100 (2017).
Nastase, M. V., Iozzo, R. V. & Schaefer, L. Key roles for the small leucine-rich proteoglycans in renal and pulmonary pathophysiology. Biochim. Biophys. Acta 1840, 2460–70 (2014).
Chiba, T. et al. Retinoic acid signaling coordinates macrophage-dependent injury and repair after AKI. J. Am. Soc. Nephrol. 27, 495–508 (2016).
Nastase, M.V. et al. Targeting renal fibrosis: mechanisms and drug delivery systems. Adv Drug Deliv. Rev. 129, 295–307 (2017).
Zeke, A. et al. Scaffolds: interaction platforms for cellular signalling circuits. Trends Cell Biol. 19, 364–374 (2009).
Wang, H. et al. A novel role of the scaffolding protein JLP in tuning CD40-induced activation of dendritic cells. Immunobiology 218, 835–843 (2013).
Wang, H. et al. Scaffold protein JLP Is critical for CD40 signaling in B lymphocytes. J. Biol. Chem. 290, 5256–5266 (2015).
Ikonomov, O. C. et al. Kinesin adapter JLP links PIKfyve to microtubule-based endosome-to-trans-golgi network traffic of Furin. J. Biol. Chem. 284, 3750–3761 (2009).
Verhey, K. J. & Hammond, J. W. Traffic control: regulation of kinesin motors. Nat. Rev. Mol. Cell Biol. 10, 765–777 (2009).
Roberts, A. J. et al. Functions and mechanics of dynein motor proteins. Nat. Rev. Mol. Cell Biol. 14, 713–726 (2013).
Fu, M. & Holzbaur, E. L. F. Integrated regulation of motor-driven organelle transport by scaffolding proteins. Trends Cell Biol. 24, 564–574 (2014).
Mackeh, R. et al. Autophagy and microtubules-new story, old players. J. Cell Sci. 126, 1071–80 (2013).
Lee, C. M. et al. JLP: a scaffolding protein that tethers JNK/p38MAPK signaling modules and transcription factors. Proc. Natl Acad. Sci. USA 99, 14189–14194 (2002).
Kashef, K. et al. Endodermal differentiation of murine embryonic carcinoma cells by retinoic acid requires JLP, a JNK-scaffolding protein. J. Cell. Biochem. 98, 715–722 (2006).
Dhanasekaran, D. N. et al. Scaffold proteins of MAP-kinase modules. Oncogene 26, 3185–3202 (2007).
Ramkumar, P. et al. JNK-associated leucine zipper protein functions as a docking platform for polo-like kinase 1 and regulation of the associating transcription factor forkhead box protein K1. J. Biol. Chem. 290, 29617–29628 (2015).
Sato, T. et al. JSAP1/JIP3 and JLP regulate kinesin-1-dependent axonal transport to prevent neuronal degeneration. Cell Death Differ. 22, 1260–74 (2015).
Yan, Q. et al. Scaffold protein JLP mediates TCR-initiated CD4 + T cell activation and CD154 expression. Mol. Immunol. 87, 258–266 (2017).
Ito, M. et al. Isoforms of JSAP1 scaffold protein generated through alternative splicing. Gene 255, 229–34 (2000).
Iwanaga, A. et al. Ablation of the scaffold protein JLP causes reduced fertility in male mice. Transgenic Res. 17, 1045–1058 (2008).
Kashef, K. et al. JNK-Interacting leucine zipper protein is a novel scaffolding protein in the Gα13 signaling pathway†. Biochemistry 44, 14090–14096 (2005).
Gantulga, D. et al. The scaffold protein c-Jun NH2-terminal kinase-associated leucine zipper protein regulates cell migration through interaction with the G protein G 13. J. Biochem. 144, 693–700 (2008).
Garg, M. et al. Small interfering RNA-mediated down-regulation ofSPAG9 inhibits cervical tumor growth. Cancer 115, 5688–5699 (2009).
Yi, F. et al. SPAG9 is overexpressed in human astrocytoma and promotes cell proliferation and invasion. Tumor Biol. 34, 2849–2855 (2013).
Sinha, A. et al. Down regulation of SPAG9 reduces growth and invasive potential of triple-negative breast cancer cells: possible implications in targeted therapy. J. Exp. Clin. Cancer Res. 32, 69 (2013).
Li, H. et al. SPAG9 is overexpressed in human prostate cancer and promotes cancer cell proliferation. Tumor Biol. 35, 6949–6954 (2014).
JIANG, J. et al. Sperm-associated antigen 9 promotes astrocytoma cell invasion through the upregulation of podocalyxin. Mol. Med. Rep. 10, 417–422 (2014).
CHEN, F. et al. SPAG9 expression is increased in human prostate cancer and promotes cell motility, invasion and angiogenesis in vitro. Oncol. Rep. 32, 2533–2540 (2014).
Lou, G. et al. Direct targeting sperm-associated antigen 9 by miR-141 influences hepatocellular carcinoma cell growth and metastasis via JNK pathway. J. Exp. Clin. Cancer Res. 35, 14 (2016).
Wang, X. et al. MicroRNA-200a-3p suppresses tumor proliferation and induces apoptosis by targeting SPAG9 in renal cell carcinoma. Biochem. Biophys. Res. Commun. 470, 620–626 (2016).
Yan, Q. et al. SPAG9 is involved in hepatocarcinoma cell migration and invasion via modulation of ELK1 expression. OncoTargets Ther. 9, 1067 (2016).
Jagadish, N. et al. Sperm-associated antigen 9 (SPAG9) promotes the survival and tumor growth of triple-negative breast cancer cells. Tumor Biol. 37, 13101–13110 (2016).
Garg, M. et al. Sperm-associated antigen 9: a Novel diagnostic marker for thyroid cancer. J. Clin. Endocrinol. Metab. 94, 4613–4618 (2009).
Kanojia, D. et al. Sperm associated antigen 9 expression and humoral response in chronic myeloid leukemia. Leuk. Res. 34, 858–863 (2010).
Yu, P. et al. Expression and clinical significance of sperm-associated antigen 9 in patients with endometrial carcinoma. Int. J. Gynecologic Cancer 22, 87–93 (2012).
Wang, Y. et al. Clinical significance and biological roles of SPAG9 overexpression in non-small cell lung cancer. Lung Cancer 81, 266–272 (2013).
Kanojia, D. et al. Sperm associated antigen 9 plays an important role in bladder transitional cell carcinoma. PLoS ONE 8, e81348 (2013).
Xie, C. et al. Overexpression of SPAG9 correlates with poor prognosis and tumor progression in hepatocellular carcinoma. Tumor Biol. 35, 7685–7691 (2014).
Agarwal, S. et al. Sperm associated antigen 9 (SPAG9) expression and humoral response in benign and malignant salivary gland tumors. OncoImmunology 3, e974382 (2015).
Seleit, I. et al. Immunohistochemical expression of sperm-associated antigen 9 in nonmelanoma skin cancer. Am. J. Dermatopathol. 37, 38–45 (2015).
Ren, B. et al. Cancer testis antigen SPAG9 is a promising marker for the diagnosis and treatment of lung cancer. Oncol. Rep. 35, 2599–2605 (2016).
Kanojia, D. et al. Sperm-associated antigen 9 Is a novel biomarker for colorectal cancer and is involved in tumor growth and tumorigenicity. Am. J. Pathol. 178, 1009–1020 (2011).
Kang, H. M. et al. Defective fatty acid oxidation in renal tubular epithelial cells has a key role in kidney fibrosis development. Nat. Med. 21, 37–46 (2015).
Qiang, F. et al. Role of scaffolding protein JLP on the progression of renal interstitial fibrosis in mice model of unilateral ureteral obstruction and its underlying mechanism. Chinese J. Nephrol. 32, 30–36 (2016).
Eddy, A. A. Overview of the cellular and molecular basis of kidney fibrosis. Kidney Int. Suppl. 4, 2–8 (2014).
Strutz, F. et al. TGF-β1 induces proliferation in human renal fibroblasts via induction of basic fibroblast growth factor (FGF-2). Kidney Int. 59, 579–592 (2001).
Kim, W. et al. The role of autophagy in unilateral ureteral obstruction rat model. Nephrology 17, 148–159 (2012).
Livingston, M. J. et al. Persistent activation of autophagy in kidney tubular cells promotes renal interstitial fibrosis during unilateral ureteral obstruction. Autophagy 12, 976–998 (2016).
Bernard, M. et al. Autophagy fosters myofibroblast differentiation through MTORC2 activation and downstream upregulation of CTGF. Autophagy 10, 2193–2207 (2015).
Xu, Y. et al. Autophagy and apoptosis in tubular cells following unilateral ureteral obstruction are associated with mitochondrial oxidative stress. Int. J. Mol. Med. 31, 628–636 (2013).
Koesters, R. et al. Tubular overexpression of transforming growth factor-β1 induces autophagy and fibrosis but not mesenchymal transition of renal epithelial cells. Am. J. Pathol. 177, 632–643 (2010).
Ding, Y. et al. Autophagy regulates TGF-βExpression and suppresses kidney fibrosis induced by unilateral ureteral obstruction. J. Am. Soc. Nephrol. 25, 2835–2846 (2014).
Yan, Q. et al. Autophagy activation contributes to lipid accumulation in tubular epithelial cells during kidney fibrosis. Cell Death Discov. 4, 2 (2018).
Doi, S. et al. Klotho inhibits transforming growth factor-β1 (TGF-β1) signaling and suppresses renal fibrosis and cancer metastasis in mice. J. Biol. Chem. 286, 8655–8665 (2011).
Duffield, J. S. Cellular and molecular mechanisms in kidney fibrosis. J. Clin. Investig. 124, 2299–2306 (2014).
Yanagita, M. Inhibitors/antagonists of TGF-beta system in kidney fibrosis. Nephrol. Dialysis Transplant. 27, 3686–3691 (2012).
Ide, N. et al. In vivo evidence for a limited role of proximal tubular Klotho in renal phosphate handling. Kidney Int. 90, 348–362 (2016).
Tanaka, M. et al. Expression of BMP-7 and USAG-1 (a BMP antagonist) in kidney development and injury. Kidney Int 73, 181–91 (2008).
Luo, G. et al. BMP-7 is an inducer of nephrogenesis, and is also required for eye development and skeletal patterning. Genes Dev. 9, 2808–20 (1995).
Dudley, A. T., Lyons, K. M. & Robertson, E. J. A requirement for bone morphogenetic protein-7 during development of the mammalian kidney and eye. Genes Dev. 9, 2795–807 (1995).
Kuro-o, M. et al. Mutation of the mouse klotho gene leads to a syndrome resembling ageing. Nature 390, 45–51 (1997).
Eddy, A. A. & Neilson, E. G. Chronic kidney disease progression. J. Am. Soc. Nephrol. 17, 2964–2966 (2006).
Yang, Z. & Klionsky, D. J. Eaten alive: a history of macroautophagy. Nat. Cell Biol. 12, 814–822 (2010).
Mizushima, N. & Komatsu, M. Autophagy: renovation of cells and tissues. Cell 147, 728–741 (2011).
Takabatake, Y. et al. Autophagy and the kidney: health and disease. Nephrol. Dial. Transpl. 29, 1639–47 (2014).
Periyasamy-Thandavan, S. et al. Autophagy is cytoprotective during cisplatin injury of renal proximal tubular cells. Kidney Int. 74, 631–640 (2008).
Jiang, M. et al. Autophagy is a renoprotective mechanism during in vitro hypoxia and in vivo ischemia-reperfusion injury. Am. J. Pathol. 176, 1181–1192 (2010).
Jiang, M. et al. Autophagy in proximal tubules protects against acute kidney injury. Kidney Int. 82, 1271–1283 (2012).
Li, L. et al. Autophagy Is a component of epithelial cell fate in obstructive uropathy. Am. J. Pathol. 176, 1767–1778 (2010).
Forbes, M. S., Thornhill, B. A. & Chevalier, R. L. Proximal tubular injury and rapid formation of atubular glomeruli in mice with unilateral ureteral obstruction: a new look at an old model. Am. J. Physiol.-Ren. Physiol. 301, F110–F117 (2011).
Kim, S. I. et al. Autophagy promotes intracellular degradation of type I collagen induced by transforming growth factor (TGF)-β1. J. Biol. Chem. 287, 11677–11688 (2012).
Takaesu, G. et al. Activation of p38α/β MAPK in myogenesis via binding of the scaffold protein JLP to the cell surface protein Cdo. J. Cell Biol. 175, 383–388 (2006).
Yang, C. et al. Sperm-associated antigen 9 overexpression correlates with poor prognosis and insensitive to Taxol treatment in breast cancer. Biomarkers 21, 62–67 (2015).