Correction: Vimentin knockout results in increased expression of sub-endothelial basement membrane components and carotid stiffness in mice (Scientific Reports (2017) DOI: 10.1038/s41598-017-12024-z);Vimentin knockout results in increased expression of sub-endothelial basement membrane components and carotid stiffness in mice

Scientific Reports

Volumn 7, Issue 1, 2017, Pages

  Langlois, Benoit ^a   Belozertseva, Ekaterina ^a   Parlakian, Ara ^b   Bourhim, Mustapha ^a   Gao Li, Jacqueline ^b   Blanc, Jocelyne ^b   Tian, Lei ^b   Coletti, Dario ^b   Labat, Carlos ^a   Ramdame Cherif, Zhor ^a   Challande, Pascal ^b   Regnault, Véronique ^a   Lacolley, Patrick ^a   Zhenlin, Li ^b  

^a UNIVERSITÉ DE LORRAINE   (France)

^b SORBONNE UNIVERSITÉ   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; CELL ADHESION MOLECULE; VIMENTIN;

ANIMAL; ARTERIAL STIFFNESS; BASEMENT MEMBRANE; BLOOD PRESSURE; CAROTID ARTERY DISEASE; CONFOCAL MICROSCOPY; DEFICIENCY; DISEASE MODEL; ENDOTHELIUM; FLUORESCENT ANTIBODY TECHNIQUE; GENE EXPRESSION REGULATION; GENETICS; INTERMEDIATE FILAMENT; KNOCKOUT MOUSE; MECHANICS; METABOLISM; MOUSE; PATHOPHYSIOLOGY; VASODILATATION;

ANIMALS; BASEMENT MEMBRANE; BIOMARKERS; BLOOD PRESSURE; CAROTID ARTERY DISEASES; CELL ADHESION MOLECULES; DISEASE MODELS, ANIMAL; ENDOTHELIUM; FLUORESCENT ANTIBODY TECHNIQUE; GENE EXPRESSION REGULATION; INTERMEDIATE FILAMENTS; MECHANICAL PHENOMENA; MICE; MICE, KNOCKOUT; MICROSCOPY, CONFOCAL; VASCULAR STIFFNESS; VASODILATION; VIMENTIN;

EID: 85029502983     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-018-22187-y     Document Type: Erratum

References (63)

1. Gruenbaum, Y. & Aebi, U. Intermediate filaments: A dynamic network that controls cell mechanics. F1000Prime Rep 6, 54, https://doi.org/10.12703/P6-54 (2014).
2. Kim, S. & Coulombe, P. A. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev 21, 1581-1597, https://doi.org/10.1101/gad.1552107 (2007).
3. Snider, N. T. & Omary, M. B. Post-translational modifications of intermediate filament proteins: Mechanisms and functions. Nat Rev Mol Cell Biol 15, 163-177, https://doi.org/10.1038/nrm3753 (2014).
4. Winter, D. L., Paulin, D., Mericskay, M. & Li, Z. Posttranslational modifications of desmin and their implication in biological processes and pathologies. Histochem Cell Biol 141, 1-16, https://doi.org/10.1007/s00418-013-1148-z (2014).
5. Gregor, M., et al. Mechanosensing through focal adhesion-anchored intermediate filaments. FASEB J 28, 715-729, https://doi.org/10.1096/fj.13-231829 (2014).
6. Leube, R. E., Moch, M. & Windoffer, R. Intermediate filaments and the regulation of focal adhesion. Curr Opin Cell Biol 32, 13-20, https://doi.org/10.1016/j.ceb.2014.09.011 (2015).
7. Maniotis, A. J., Chen, C. S. & Ingber, D. E. Demonstration of mechanical connections between integrins, cytoskeletal filaments, and nucleoplasm that stabilize nuclear structure. Proc Natl Acad Sci USA 94, 849-854 (1997).
8. Johansson, B., Eriksson, A., Virtanen, I. & Thornell, L. E. Intermediate filament proteins in adult human arteries. Anat Rec 247, 439-448 (1997).
9. Wede, O. K., Lofgren, M., Li, Z., Paulin, D. & Arner, A. Mechanical function of intermediate filaments in arteries of different size examined using desmin deficient mice. J Physiol 540, 941-949 (2002).
10. Izmiryan, A., Franco, C. A., Paulin, D., Li, Z. & Xue, Z. Synemin isoforms during mouse development: Multiplicity of partners in vascular and neuronal systems. Exp Cell Res 315, 769-783, https://doi.org/10.1016/j.yexcr.2008.12.009 (2009).
11. Small, J. V. & Gimona, M. The cytoskeleton of the vertebrate smooth muscle cell. Acta Physiol Scand 164, 341-348, https://doi.org/10.1046/j.1365-201X.1998.00441.x (1998).
12. Sun, N., Critchley, D. R., Paulin, D., Li, Z. & Robson, R. M. Human alpha-synemin interacts directly with vinculin and metavinculin. Biochem J 409, 657-667, https://doi.org/10.1042/BJ20071188 (2008).
13. Sun, N., Critchley, D. R., Paulin, D., Li, Z. & Robson, R. M. Identification of a repeated domain within mammalian alpha-synemin that interacts directly with talin. Exp Cell Res 314, 1839-1849, https://doi.org/10.1016/j.yexcr.2008.01.034 (2008).
14. Sun, N., Huiatt, T. W., Paulin, D., Li, Z. & Robson, R. M. Synemin interacts with the LIM domain protein zyxin and is essential for cell adhesion and migration. Exp Cell Res 316, 491-505, https://doi.org/10.1016/j.yexcr.2009.10.015 (2010).
15. Uyama, N., et al. Hepatic stellate cells express synemin, a protein bridging intermediate filaments to focal adhesions. Gut 55, 1276-1289, https://doi.org/10.1136/gut.2005.078865 (2006).
16. Bhattacharya, R., et al. Recruitment of vimentin to the cell surface by beta3 integrin and plectin mediates adhesion strength. J Cell Sci 122, 1390-1400. https://doi.org/10.1242/jcs.043042 (2009).
17. Esue, O., Carson, A. A., Tseng, Y. & Wirtz, D. A direct interaction between actin and vimentin filaments mediated by the tail domain of vimentin. J Biol Chem 281, 30393-30399, https://doi.org/10.1074/jbc.M605452200 (2006).
18. Kreis, S., Schonfeld, H. J., Melchior, C., Steiner, B. & Kieffer, N. The intermediate filament protein vimentin binds specifically to a recombinant integrin alpha2/beta1 cytoplasmic tail complex and co-localizes with native alpha2/beta1 in endothelial cell focal adhesions. Exp Cell Res 305, 110-121, https://doi.org/10.1016/j.yexcr.2004.12.023 (2005).
19. Tsuruta, D. & Jones, J. C. The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress. J Cell Sci 116, 4977-4984, https://doi.org/10.1242/jcs.00823 (2003).
20. Gonzales, M., et al. Structure and function of a vimentin-associated matrix adhesion in endothelial cells. Mol Biol Cell 12, 85-100 (2001).
21. Ivaska, J., Pallari, H. M., Nevo, J. & Eriksson, J. E. Novel functions of vimentin in cell adhesion, migration, and signaling. Exp Cell Res 313, 2050-2062, https://doi.org/10.1016/j.yexcr.2007.03.040 (2007).
22. Humphrey, J. D., Harrison, D. G., Figueroa, C. A., Lacolley, P. & Laurent, S. Central Artery Stiffness in Hypertension and Aging: A Problem With Cause and Consequence. Circ Res 118, 379-381, https://doi.org/10.1161/CIRCRESAHA.115.307722 (2016).
23. Lacolley, P., et al. Increased carotid wall elastic modulus and fibronectin in aldosterone-salt-treated rats: Effects of eplerenone. Circulation 106, 2848-2853 (2002).
24. Zhu, Y., et al. Temporal analysis of vascular smooth muscle cell elasticity and adhesion reveals oscillation waveforms that differ with aging. Aging Cell 11, 741-750, https://doi.org/10.1111/j.1474-9726.2012.00840.x (2012).
25. Qiu, H., et al. Short communication: Vascular smooth muscle cell stiffness as a mechanism for increased aortic stiffness with aging. Circ Res 107, 615-619, https://doi.org/10.1161/CIRCRESAHA.110.221846 (2010).
26. Sehgel, N. L., et al. Increased vascular smooth muscle cell stiffness: A novel mechanism for aortic stiffness in hypertension. Am J Physiol Heart Circ Physiol 305, H1281-1287, https://doi.org/10.1152/ajpheart.00232.2013 (2013).
27. Sehgel, N. L., Vatner, S. F. & Meininger, G. A. "Smooth Muscle Cell Stiffness Syndrome"-Revisiting the Structural Basis of Arterial Stiffness. Front Physiol 6, 335, https://doi.org/10.3389/fphys.2015.00335 (2015).
28. Lacolley, P., Li, Z., Challande, P. & Regnault, V. SRF/myocardin: A novel molecular axis regulating vascular smooth muscle cell stiffening in hypertension. Cardiovasc Res 113, 120-122, https://doi.org/10.1093/cvr/cvw253 (2017).
29. Zhou, N., et al. Inhibition of SRF/myocardin reduces aortic stiffness by targeting vascular smooth muscle cell stiffening in hypertension. Cardiovasc Res 113, 171-182, https://doi.org/10.1093/cvr/cvw222 (2017).
30. Galmiche, G., et al. Inactivation of serum response factor contributes to decrease vascular muscular tone and arterial stiffness in mice. Circ Res 112, 1035-1045, https://doi.org/10.1161/CIRCRESAHA.113.301076 (2013).
31. Laurent, S. & Boutouyrie, P. The structural factor of hypertension: Large and small artery alterations. Circ Res 116, 1007-1021, https://doi.org/10.1161/CIRCRESAHA.116.303596 (2015).
32. Brandes, R. P., Fleming, I. & Busse, R. Endothelial aging. Cardiovasc Res 66, 286-294, https://doi.org/10.1016/j.cardiores.2004.12.027 (2005).
33. Lacolley, P., et al. Mechanical properties and structure of carotid arteries in mice lacking desmin. Cardiovasc Res 51, 178-187 (2001).
34. Terriac, E., et al. Vimentin Levels and Serine 71 Phosphorylation in the Control of Cell-Matrix Adhesions, Migration Speed, and Shape of Transformed Human Fibroblasts. Cells 6, https://doi.org/10.3390/cells6010002 (2017).
35. Eckes, B., et al. Impaired mechanical stability, migration and contractile capacity in vimentin-deficient fibroblasts. J Cell Sci 111(Pt 13), 1897-1907 (1998).
36. Mendez, M. G., Restle, D. & Janmey, P. A. Vimentin enhances cell elastic behavior and protects against compressive stress. Biophys J 107, 314-323, https://doi.org/10.1016/j.bpj.2014.04.050 (2014).
37. Trachet, B., et al. Performance comparison of ultrasound-based methods to assess aortic diameter and stiffness in normal and aneurysmal mice. PLoS One 10, e0129007, https://doi.org/10.1371/journal.pone.0129007 (2015).
38. Bezie, Y., et al. Fibronectin expression and aortic wall elastic modulus in spontaneously hypertensive rats. Arterioscler Thromb Vasc Biol 18, 1027-1034 (1998).
39. Khanamiryan, L., Li, Z., Paulin, D. & Xue, Z. Self-assembly incompetence of synemin is related to the property of its head and rod domains. Biochemistry 47, 9531-9539, https://doi.org/10.1021/bi800912w (2008).
40. Xue, Z. G., et al. The mouse synemin gene encodes three intermediate filament proteins generated by alternative exon usage and different open reading frames. Exp Cell Res 298, 431-444, https://doi.org/10.1016/j.yexcr.2004.04.023 (2004).
41. Li, Z., et al. Synemin acts as a regulator of signalling molecules during skeletal muscle hypertrophy. J Cell Sci 127, 4589-4601, https://doi.org/10.1242/jcs.143164 (2014).
42. Brown, M. J., Hallam, J. A., Colucci-Guyon, E. & Shaw, S. Rigidity of circulating lymphocytes is primarily conferred by vimentin intermediate filaments. J Immunol 166, 6640-6646 (2001).
43. Lu, Y. B., et al. Reactive glial cells: Increased stiffness correlates with increased intermediate filament expression. FASEB J 25, 624-631, https://doi.org/10.1096/fj.10-163790 (2011).
44. Wang, N. & Stamenovic, D. Contribution of intermediate filaments to cell stiffness, stiffening, and growth. Am J Physiol Cell Physiol 279, C188-194 (2000).
45. Ofek, G., Wiltz, D. C. & Athanasiou, K. A. Contribution of the cytoskeleton to the compressive properties and recovery behavior of single cells. Biophys J 97, 1873-1882, https://doi.org/10.1016/j.bpj.2009.07.050 (2009).
46. Lacolley, P., Challande, P., Osborne-Pellegrin, M. & Regnault, V. Genetics and pathophysiology of arterial stiffness. Cardiovasc Res 81, 637-648, https://doi.org/10.1093/cvr/cvn353 (2009).
47. Candiello, J., et al. Biomechanical properties of native basement membranes. FEBS J 274, 2897-2908, https://doi.org/10.1111/j.1742-4658.2007.05823.x (2007).
48. Candiello, J., Cole, G. J. & Halfter, W. Age-dependent changes in the structure, composition and biophysical properties of a human basement membrane. Matrix Biol 29, 402-410, https://doi.org/10.1016/j.matbio.2010.03.004 (2010).
49. Halfter, W., et al. The bi-functional organization of human basement membranes. PLoS One 8, e67660, https://doi.org/10.1371/journal.pone.0067660 (2013).
50. Henrich, P. B., et al. Nanoscale topographic and biomechanical studies of the human internal limiting membrane. Invest Ophthalmol Vis Sci 53, 2561-2570, https://doi.org/10.1167/iovs.11-8502 (2012).
51. Halfter, W., et al. New concepts in basement membrane biology. FEBS J 282, 4466-4479, https://doi.org/10.1111/febs.13495 (2015).
52. Yang, X., et al. Basement membrane stiffening promotes retinal endothelial activation associated with diabetes. FASEB J 30, 601-611, https://doi.org/10.1096/fj.15-277962 (2016).
53. Boutouyrie, P., et al. In vivo/in vitro comparison of rat abdominal aorta wall viscosity. Influence of endothelial function. Arterioscler Thromb Vasc Biol 17, 1346-1355 (1997).
54. Svitkina, T. M., Verkhovsky, A. B. & Borisy, G. G. Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. J Cell Biol 135, 991-1007 (1996).
55. Jiu, Y., et al. Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA. J Cell Sci 130, 892-902, https://doi.org/10.1242/jcs.196881 (2017).
56. Kowalczyk, A. P., et al. VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: A pivotal role for plakoglobin in the recruitment of desmoplakin to intercellular junctions. J Cell Sci 111(Pt 20), 3045-3057 (1998).
57. Saphirstein, R. J., et al. The focal adhesion: A regulated component of aortic stiffness. PLoS One 8, e62461, https://doi.org/10.1371/journal.pone.0062461 (2013).
58. Thomas, M., et al. Angiopoietin-2 stimulation of endothelial cells induces alphavbeta3 integrin internalization and degradation. J Biol Chem 285, 23842-23849, https://doi.org/10.1074/jbc.M109.097543 (2010).
59. Wei, J., et al. Overexpression of vimentin contributes to prostate cancer invasion and metastasis via src regulation. Anticancer Res 28, 327-334 (2008).
60. Tian, Y., Gawlak, G., O'Donnell, J. J. 3rd, Birukova, A. A. & Birukov, K. G. Activation of Vascular Endothelial Growth Factor (VEGF) Receptor 2 Mediates Endothelial Permeability Caused by Cyclic Stretch. J Biol Chem 291, 10032-10045, https://doi.org/10.1074/jbc.M115.690487 (2016).
61. Lange, K., et al. Endothelin receptor type B counteracts tenascin-C-induced endothelin receptor type A-dependent focal adhesion and actin stress fiber disorganization. Cancer Res 67, 6163-6173, https://doi.org/10.1158/0008-5472.CAN-06-3348 (2007).
62. Colucci-Guyon, E., et al. Mice lacking vimentin develop and reproduce without an obvious phenotype. Cell 79, 679-694 (1994).
63. Louis, H., et al. Role of alpha1beta1-integrin in arterial stiffness and angiotensin-induced arterial wall hypertrophy in mice. Am J Physiol Heart Circ Physiol 293, H2597-2604, https://doi.org/10.1152/ajpheart.00299.2007 (2007).