Enhanced myostatin expression and signalling promote tubulointerstitial inflammation in diabetic nephropathy.
Cell Line
Cell Proliferation
/ genetics
Diabetic Nephropathies
/ genetics
Epithelial Cells
/ metabolism
Gene Expression Regulation
/ genetics
Glucose
/ metabolism
Humans
Inflammation
/ genetics
Kidney
/ metabolism
Kidney Tubules
/ metabolism
Leukocyte Common Antigens
/ genetics
Myostatin
/ genetics
RNA, Messenger
/ genetics
Signal Transduction
/ genetics
Transforming Growth Factor beta
/ genetics
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
14 04 2020
14 04 2020
Historique:
received:
07
08
2019
accepted:
12
03
2020
entrez:
15
4
2020
pubmed:
15
4
2020
medline:
1
12
2020
Statut:
epublish
Résumé
Myostatin (MSTN), a family member of the transforming growth factor (TGF)-β super family, has been detected in the tubuli of pig kidney, but its role in the human kidney is not known. In this study we observed upregulation of MSTN mRNA (~8 to 10-fold increase) both in the glomeruli and tubulointerstitium in diabetic nephropathy (DN). In DN, immunoreactive MSTN was mainly localized in the tubuli and interstitium (∼4-8 fold increase), where it colocalized in CD45
Identifiants
pubmed: 32286342
doi: 10.1038/s41598-020-62875-2
pii: 10.1038/s41598-020-62875-2
pmc: PMC7156449
doi:
Substances chimiques
Myostatin
0
RNA, Messenger
0
Transforming Growth Factor beta
0
Leukocyte Common Antigens
EC 3.1.3.48
Glucose
IY9XDZ35W2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
6343Références
McPherron, A. C., Lawler, A. M. & Lee, S. J. Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member. Nature 387, 83–90 (1997).
pubmed: 9139826
doi: 10.1038/387083a0
Glass, D. J. Skeletal muscle hypertrophy and atrophy signaling pathways. Int. J. Biochem. Cell Biol. 37, 1974–1984 (2005).
pubmed: 16087388
doi: 10.1016/j.biocel.2005.04.018
Lee, S. J. & McPherron, A. C. Regulation of myostatin activity and muscle growth. Proc. Natl Acad. Sci. USA 98, 9306–9311 (2001).
pubmed: 11459935
doi: 10.1073/pnas.151270098
Rodriguez, J. et al. Myostatin and the skeletal muscle atrophy and hypertrophy signaling pathways. Cell Mol. Life Sci. 71, 4361–4371 (2014).
pubmed: 25080109
doi: 10.1007/s00018-014-1689-x
Dasarathy, S. Myostatin and beyond in cirrhosis: all roads lead to sarcopenia. J. Cachexia Sarcopenia Muscle 8, 864–869 (2017).
pubmed: 29168629
pmcid: 5700432
doi: 10.1002/jcsm.12262
Han, H. Q. et al. Myostatin/activin pathway antagonism: molecular basis and therapeutic potential. Int. J. Biochem. Cell Biol. 45, 2333–2347 (2013).
pubmed: 23721881
doi: 10.1016/j.biocel.2013.05.019
Dong, J. et al. The pathway to muscle fibrosis depends on myostatin stimulating the differentiation of fibro/adipogenic progenitor cells in chronic kidney disease. Kidney Int. 91, 119–128 (2017).
pubmed: 27653838
doi: 10.1016/j.kint.2016.07.029
Zhu, J. et al. Relationships between transforming growth factor-beta1, myostatin, and and decorin: Implications for skeletal muscle fibrosis. J. Biol. Chem. 282, 25852–25863 (2007).
pubmed: 17597062
doi: 10.1074/jbc.M704146200
Jiao, J. et al. Analysis of myostatin and its related factors in various porcine tissues. J. Anim. Sci. 89, 3099–3106 (2011).
pubmed: 21571901
doi: 10.2527/jas.2010-3827
Swindle, M. & Smith, A. Comparative anatomy and physiology of the pig. Scand. J. Lab. Anim. Sci. 25(Suppl. 1), 11–21 (1998).
Zhang, C. et al. Inhibition of myostatin protects against diet-induced obesity by enhancing fatty acid oxidation and promoting a brown adipose phenotype in mice. Diabetologia 55, 183–193 (2012).
pubmed: 21927895
doi: 10.1007/s00125-011-2304-4
Zhang, L. et al. Pharmacological inhibition of myostatin suppresses systemic inflammation and muscle atrophy in mice with chronic kidney disease. FASEB J. 25, 1653–1663 (2011).
pubmed: 21282204
pmcid: 3079306
doi: 10.1096/fj.10-176917
Wilkes, J. J., Lloyd, D. J. & Gekakis, N. Loss-of-function mutation in myostatin reduces tumor necrosis factor alpha production and protects liver against obesity-induced insulin resistance. Diabetes 58, 1133–1143 (2009).
pubmed: 19208906
pmcid: 2671051
doi: 10.2337/db08-0245
Guo, T. et al. Myostatin inhibition in muscle, but not adipose tissue, decreases fat mass and improves insulin sensitivity. PLoS One 4, e4937 (2008).
doi: 10.1371/journal.pone.0004937
Tu, P. et al. Genetic disruption of myostatin reduces the development of proatherogenic dyslipidemia and atherogenic lesions in Ldlr null mice. Diabetes 58, 1739–1748 (2009).
pubmed: 19509018
pmcid: 2712781
doi: 10.2337/db09-0349
Coleman, S. K., Rebalka, I. A. & D’Souza, D. M. Myostatin inhibition therapy for insulin-deficient type 1 diabetes. Sci. Rep. 6, 32495 (2016).
pubmed: 27581061
pmcid: 5007491
doi: 10.1038/srep32495
Brandt, C. et al. Plasma and Muscle Myostatin in Relation to Type 2 Diabetes. PLoS One. 7, e37236 (2012).
pubmed: 22615949
pmcid: 3353926
doi: 10.1371/journal.pone.0037236
Palsgaard, J. et al. Gene expression in skeletal muscle biopsies from people with type 2 diabetes and relatives: differential regulation of insulin signaling pathways. PLoS One 4, e6575 (2009).
pubmed: 19668377
pmcid: 2719801
doi: 10.1371/journal.pone.0006575
Hittel, D. S. et al. Increased secretion and expression of myostatin in skeletal muscle from extremely obese women. Diabetes 58, 30–38 (2009).
pubmed: 18835929
pmcid: 2606890
doi: 10.2337/db08-0943
Verzola, D. et al. Myostatin mediates abdominal aortic atherosclerosis progression by inducing vascular smooth muscle cell dysfunction and monocyte recruitment. Sci. Rep. 13, 46362 (2017).
doi: 10.1038/srep46362
Verzola, D. et al. Enhanced glomerular Toll-like receptor 4 expression and signalling in patients with type 2 diabetic nephropathy and microalbuminuria. Kidney Int. 86, 1229–1243 (2014).
pubmed: 24786705
doi: 10.1038/ki.2014.116
pmcid: 24786705
Banas, M. C. et al. TLR4 links podocytes with the innate immune system to mediate glomerular injury. J. Am. Soc. Nephrol. 19, 704–713 (2008).
pubmed: 18256364
pmcid: 2390962
doi: 10.1681/ASN.2007040395
Wang, C. et al. Deletion of mstna and mstnb impairs the immune system and affects growth performance in zebrafish. Fish. Shellfish. Immunol. 72, 572–580 (2018).
pubmed: 29175471
doi: 10.1016/j.fsi.2017.11.040
pmcid: 29175471
Iwasaki, S. et al. Effect of myostatin on chemokine expression in regenerating skeletal muscle cells. Cell Tissues Organs 198, 66–74 (2013).
doi: 10.1159/000351462
Biesemann, N. et al. Myostatin induces interstitial fibrosis in the heart via TAK1 and p38. Cell Tissue Res. 361, 779–787 (2015).
pubmed: 25725788
doi: 10.1007/s00441-015-2139-2
pmcid: 25725788
Sriram, S., Subramanian, S. & Sathiakumar, D. Modulation of reactive oxygen species in skeletal muscle by myostatin is mediated through NF-κB. Aging Cell 10, 931–948 (2011).
pubmed: 21771249
pmcid: 5028794
doi: 10.1111/j.1474-9726.2011.00734.x
Wada, J. & Makino, H. Innate immunity in diabetes and diabetic nephropathy. Nat. Rev. Nephrol. 12, 13–26 (2016).
pubmed: 26568190
doi: 10.1038/nrneph.2015.175
pmcid: 26568190
Gilbert, R. & Cooper, M. The tubulointerstitium in progressive diabetic kidney disease: more than an aftermath of glomerular injury? Kidney Int. 56, 1627–1637 (1999).
pubmed: 10571771
doi: 10.1046/j.1523-1755.1999.00721.x
Galkina, E. & Ley, K. Leukocyte recruitment and vascular injury in diabetic nephropathy. J. Am. Soc. Nephrol. 17, 368–377 (2006).
pubmed: 16394109
doi: 10.1681/ASN.2005080859
Chow, F. et al. Macrophages in mouse type 2 diabetic nephropathy: Correlation with diabetic state and progressive renal injury. Kidney Int. 65, 116–128 (2004).
pubmed: 14675042
doi: 10.1111/j.1523-1755.2004.00367.x
Zhang, L. et al. Stat3 Activation links a C/EBPδ to Myostatin Pathway to Stimulate Loss of Muscle Mass. Cell Metab. 18, 368–379 (2013).
pubmed: 24011072
pmcid: 3794464
doi: 10.1016/j.cmet.2013.07.012
Lyons, J. A., Haring, J. S. & Biga, P. R. Myostatin expression, lymphocyte population, and potential cytokine production correlate with predisposition to high-fat diet induced obesity in mice. PLoS One 5, e12928 (2010).
pubmed: 20877574
pmcid: 2943928
doi: 10.1371/journal.pone.0012928
Mathews, L. S. et al. Activin receptors and cellular signaling by the receptor serine kinase family. Endocr. Rev. 15, 310–341 (1995).
doi: 10.1210/edrv-15-3-310
Jha, J. C. et al. Genetic targeting or pharmacologic inhibition of NADPH oxidase Nox4 provides renoprotection in long-term diabetic nephropathy. J. Am. Soc. Nephrol. 25, 1237–1254 (2014).
pubmed: 24511132
pmcid: 4033375
doi: 10.1681/ASN.2013070810
Border, W. A. & Noble, N. A. Transforming growth factor beta in tissue fibrosis. N. Engl. J. Med. 331, 1286–1292 (1994).
pubmed: 7935686
doi: 10.1056/NEJM199411103311907
Rockey, D. C., Bell, P. D. & Hill, J. A. Fibrosis — A Common Pathway to Organ Injury and Failure. N. Engl. J. Med. 372, 1138–1149 (2015).
pubmed: 25785971
doi: 10.1056/NEJMra1300575
Rodrıguez-Barbero, A. et al. Transforming growth factor-β1 induces collagen synthesis and accumulation via p38 mitogen-activated protein kinase (MAPK) pathway in cultured L6E9 myoblasts. FEBS letters. 513, 282–288 (2002).
pubmed: 11904165
doi: 10.1016/S0014-5793(02)02337-2
Williams, M. J. et al. The activin receptor is stimulated in the skeleton, vasculature, heart, and kidney during chronic kidney disease. Kidney Int. 93, 147–158 (2018).
pubmed: 28843411
doi: 10.1016/j.kint.2017.06.016
Maeshima, A., Nojima, Y. & Kojima, I. Activin A. An autocrine regulator of cell growth and differentiation in renal proximal tubular cells. Kidney Int. 62, 446–454 (2002).
pubmed: 12110005
doi: 10.1046/j.1523-1755.2002.00463.x
Yamashita, S. et al. Activin A is a Potent Activator of Renal Interstitial Fibroblasts. J. Am. Soc. Nephrol. 15, 91–101 (2004).
pubmed: 14694161
doi: 10.1097/01.ASN.0000103225.68136.E6
pmcid: 14694161
Tervaert, T. et al. Pathologic classification of diabetic nephropathy. J. Am. Soc. Nephrol. 21, 556–563 (2010).
pubmed: 20167701
doi: 10.1681/ASN.2010010010
pmcid: 20167701