Thrombospondin 1 and Its Diverse Roles as a Regulator of Extracellular Matrix in Fibrotic Disease

Signal integration in the endoplasmic reticulum unfolded protein response

Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,431

Mechanisms of fibrosis: therapeutic translation for fibrotic disease

Wynn, T. A., & Ramalingam, T. R. (2012) · Nature Medicine · doi:10.1038/nm.2807 · Cited by 3,541

Thrombospondin-1 Is a Major Activator of TGF-β1 In Vivo

Crawford, S. E., Stellmach, V. M., Murphy-Ullrich, J. E., Ribeiro, S. M. F., Lawler, J., Hynes, R. O., Boivin, G. P., & Bouck, N. (1998) · Cell · doi:10.1016/s0092-8674(00)81460-9 · Cited by 1,176

End-stage renal failure in type 2 diabetes: A medical catastrophe of worldwide dimensions

Ritz, E., Rychlík, I., Locatelli, F., & Halimi, S. (1999) · American Journal of Kidney Diseases · doi:10.1016/s0272-6386(99)70035-1 · Cited by 811

Diversity of function is inherent in matricellular proteins: an appraisal of thrombospondin 1.

Bornstein, P. (1995) · The Journal of cell biology · doi:10.1083/jcb.130.3.503 · Cited by 666

Hyperglycemia and Diabetic Kidney Disease: The Case for Transforming Growth Factor–β as a Key Mediator

Sharma, K., & Ziyadeh, F. N. (1995) · Diabetes · doi:10.2337/diab.44.10.1139 · Cited by 576

Clinical development of galunisertib (LY2157299 monohydrate), a small molecule inhibitor of transforming growth factor-beta signaling pathway

Lahn, M. M. F., Herbertz, S., Sawyer, J. S., Stauber, A. J., Gueorguieva, I., Driscoll, K. E., Estrem, S. T., Cleverly, A., Desaiah, D., Guba, S. C., et al. (2015) · Drug Design Development and Therapy · doi:10.2147/dddt.s86621 · Cited by 571

Mice That Lack Thrombospondin 2 Display Connective Tissue Abnormalities That Are Associated with Disordered Collagen Fibrillogenesis, an Increased Vascular Density, and a Bleeding Diathesis

Kyriakides, T. R., Zhu, Y.-H., Smith, L. T., Bain, S. D., Yang, Z., Lin, M. T., Danielson, K. G., Iozzo, R. V., LaMarca, M. E., McKinney, C. E., et al. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.2.419 · Cited by 503

Lung Stem Cell Differentiation in Mice Directed by Endothelial Cells via a BMP4-NFATc1-Thrombospondin-1 Axis

Lee, J., Bhang, D. H., Beede, A. M., Huang, T. L., Stripp, B. R., Bloch, K. D., Wagers, A. J., Tseng, Y., Ryeom, S. W., & Kim, C. F. (2014) · Cell · doi:10.1016/j.cell.2013.12.039 · Cited by 494

The de-adhesive activity of matricellular proteins: is intermediate cell adhesion an adaptive state?

Murphy-Ullrich, J. E. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12609 · Cited by 483

Thrombospondins as matricellular modulators of cell function

BORNSTEIN, P. K. (2001) · Journal of Clinical Investigation · doi:10.1172/jci12749 · Cited by 470

Thrombospondin causes activation of latent transforming growth factor- beta secreted by endothelial cells by a novel mechanism [published erratum appears in J Cell Biol 1993 Sep;122(5):following 1143]

Schultz‐Cherry, S. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.122.4.923 · Cited by 468

The ThrombospondinsPreprint

Adams, J. C., & Lawler, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a009712 · Cited by 468

Mediators of Diabetic Renal Disease: The Case for TGF-β as the Major Mediator

Ziyadeh, F. N. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000093460.24823.5b · Cited by 463

Regulation of Transforming Growth Factor-β Activation by Discrete Sequences of Thrombospondin 1

Schultz‐Cherry, S., Chen, H., Mosher, D. F., Misenheimer, T. M., Krutzsch, H. C., Roberts, D. D., & Murphy-Ullrich, J. E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7304 · Cited by 424

Revisiting the matricellular concept

Murphy-Ullrich, J. E., & Sage, E. H. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.07.005 · Cited by 401

The big five in fibrosis: Macrophages, myofibroblasts, matrix, mechanics, and miscommunication

Pakshir, P., & Hinz, B. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.01.019 · Cited by 396

Pathogenesis of the Podocytopathy and Proteinuria in Diabetic Glomerulopathy

Ziyadeh, F. N., & Wolf, G. (2008) · Current Diabetes Reviews · doi:10.2174/157339908783502370 · Cited by 383

Endoplasmic Reticulum Chaperones GRP78 and Calreticulin Prevent Oxidative Stress, Ca2+ Disturbances, and Cell Death in Renal Epithelial Cells

Liu, H., Bowes, R. C., van de Water, B., Sillence, C., Nagelkerke, J. F., & Stevens, J. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.35.21751 · Cited by 373

The Activation Sequence of Thrombospondin-1 Interacts with the Latency-associated Peptide to Regulate Activation of Latent Transforming Growth Factor-β

Ribeiro, S. M. F., Poczatek, M. H., Schultz‐Cherry, S., Villain, M., & Murphy-Ullrich, J. E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13586 · Cited by 355

Thrombospondin-1 regulation of latent TGF-β activation: A therapeutic target for fibrotic disease

Murphy-Ullrich, J. E., & Suto, M. J. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.12.009 · Cited by 352

COMP Acts as a Catalyst in Collagen Fibrillogenesis

Halász, K., Kassner, A., Mörgelin, M., & Heinegård, D. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705735200 · Cited by 328

The RAAS in the pathogenesis and treatment of diabetic nephropathy

Ruggenenti, P. L., Cravedi, P., & Remuzzi, G. (2010) · Nature Reviews Nephrology · doi:10.1038/nrneph.2010.58 · Cited by 319

Anti–TGF-β1 Antibody Therapy in Patients with Diabetic Nephropathy

Voelker, J. R., Berg, P. H., Sheetz, M. J., Duffin, K. L., Shen, T., Moser, B. A., Greene, T., Blumenthal, S. S., Rychlík, I., Yagil, Y., et al. (2016) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015111230 · Cited by 288

Impaired angiogenesis in the aging kidney: Vascular endothelial growth factor and Thrombospondin-1 in renal disease

Kang, D., Anderson, S., Kim, Y.-G., Mazzalli, M., Suga, S., Jefferson, J. A., GORDON, K. L., Oyama, T., Hughes, J., Hugo, C., et al. (2001) · American Journal of Kidney Diseases · doi:10.1053/ajkd.2001.22087 · Cited by 283

Targeting TGF-β signaling for the treatment of fibrosis

Györfi, A., Matei, A., & Distler, J. H. W. (2018) · Matrix Biology · doi:10.1016/j.matbio.2017.12.016 · Cited by 283

TGF-β signaling in the kidney: profibrotic and protective effects

Sureshbabu, A., Muhsin, S. A., & Choi, M. E. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00365.2015 · Cited by 281

Thrombospondin modulates focal adhesions in endothelial cells.

Murphy-Ullrich, J. E., & Höök, M. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.3.1309 · Cited by 274

Thrombospondin binds and activates the small and large forms of latent transforming growth factor-beta in a chemically defined system.

Schultz‐Cherry, S., Ribeiro, S. M. F., Gentry, L. E., & Murphy-Ullrich, J. E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47086-x · Cited by 272

Current understanding of the thrombospondin-1 interactome

Resovi, A., Pinessi, D., Chiorino, G., & Taraboletti, G. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.01.012 · Cited by 270

Proteinuria and Hyperglycemia Induce Endoplasmic Reticulum Stress

Lindenmeyer, M. T., Rastaldi, M. P., Ikehata, M., Neusser, M. A., Kretzler, M., Cohen, C. D., & Diaeresis]ndorff, D. S. (2008) · Journal of the American Society of Nephrology · doi:10.1681/asn.2007121313 · Cited by 270

Transforming growth factor-beta complexes with thrombospondin.

Murphy-Ullrich, J. E., Schultz‐Cherry, S., & Höök, M. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.2.181 · Cited by 258

Thrombospondin1 in tissue repair and fibrosis: TGF-β-dependent and independent mechanisms

Sweetwyne, M. T., & Murphy-Ullrich, J. E. (2012) · Matrix Biology · doi:10.1016/j.matbio.2012.01.006 · Cited by 248

Endoplasmic reticulum stress in pulmonary fibrosis

Burman, A., Tanjore, H., & Blackwell, T. S. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.015 · Cited by 242

The role of angiotensin II in diabetic nephropathy: Emphasis on nonhemodynamic mechanisms

Wolf, G., & Ziyadeh, F. N. (1997) · American Journal of Kidney Diseases · doi:10.1016/s0272-6386(97)90023-8 · Cited by 234

A Thrombospondin-Dependent Pathway for a Protective ER Stress Response

Lynch, J. M., Maillet, M., Vanhoutte, D., Schloemer, A. J., Sargent, M. A., Blair, N. S., Lynch, K. A., Okada, T., Aronow, B. J., Osińska, H. E., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.050 · Cited by 228

The glomerular response to injury: Progression or resolution?

Johnson, R. J. (1994) · Kidney International · doi:10.1038/ki.1994.230 · Cited by 224

The role of thrombospondins 1 and 2 in the regulation of cell–matrix interactions, collagen fibril formation, and the response to injury

BORNSTEIN, P. K., Agah, A., & Kyriakides, T. R. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.01.012 · Cited by 217

Proteostasis in endoplasmic reticulum—new mechanisms in kidney disease

Inagi, R., Ishimoto, Y., & Nangaku, M. (2014) · Nature Reviews Nephrology · doi:10.1038/nrneph.2014.67 · Cited by 216

ADAMTS1 mediates the release of antiangiogenic polypeptides from TSP1 and 2

Lee, N. V., Sato, M., Annis, D. S., Loo, J. A., Wu, L., Mosher, D. F., & Iruela‐Arispe, M. L. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601400 · Cited by 212

Unifying mechanism for different fibrotic diseases

Wernig, G., Chen, S.-Y., Cui, L., Neste, C. V., Tsai, J. M., Kambham, N., Vogel, H. S., Natkunam, Y., Gilliland, D. G., Nolan, G. P., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1621375114 · Cited by 211

Transforming growth factor-β1 and diabetic nephropathy

Chang, A. S., Hathaway, C. K., Smithies, O., & Kakoki, M. (2015) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00502.2015 · Cited by 193

The SGLT2 inhibitor empagliflozin ameliorates early features of diabetic nephropathy in BTBR ob/ob type 2 diabetic mice with and without hypertension

Gembardt, F., Bartaun, C., Jarzebska, N., Mayoux, E., Todorov, V., Hohenstein, B., & Hugo, C. (2014) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00145.2014 · Cited by 192

Add-On Anti–TGF-β Antibody to ACE Inhibitor Arrests Progressive Diabetic Nephropathy in the Rat

Benigni, A., Zoja, C., Corna, D., Zatelli, C., Conti, S., Campana, M., Gagliardini, E., Rottoli, D., Zanchi, C., Abbate, M., et al. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000074238.61967.b7 · Cited by 176

Thrombospondin signaling through the calreticulin/LDL receptor-related protein co-complex stimulates random and directed cell migration

Orr, A. W., Elzie, C. A., Kucik, D. F., & Murphy-Ullrich, J. E. (2003) · Journal of Cell Science · doi:10.1242/jcs.00600 · Cited by 174

Endoplasmic reticulum stress in proteinuric kidney disease

Cybulsky, A. V. (2009) · Kidney International · doi:10.1038/ki.2009.389 · Cited by 171

Low density lipoprotein receptor–related protein is a calreticulin coreceptor that signals focal adhesion disassembly

Orr, A. W., Pedraza, C. E., Pallero, M. A., Elzie, C. A., Goicoechea, S. M., Strickland, D. K., & Murphy-Ullrich, J. E. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302069 · Cited by 168

Involvement of Endoplasmic Reticulum Stress in Myofibroblastic Differentiation of Lung Fibroblasts

Baek, H. A., Kim, D. S., Park, H. S., Jang, K. Y., Kang, M. J., Lee, D. G., Moon, W. S., Chae, H., & Chung, M. J. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2011-0121oc · Cited by 165

Progression of chronic kidney disease: too much cellular talk causes damage

Gewin, L. S., Zent, R., & Pozzi, A. (2016) · Kidney International · doi:10.1016/j.kint.2016.08.025 · Cited by 158

Angiotensin II induces thrombospondin-1 production in human mesangial cells via p38 MAPK and JNK: a mechanism for activation of latent TGF-β1

Naito, T., Masaki, T., Nikolic‐Paterson, D. J., Tanji, C., Yorioka, N., & Kohno, N. (2004) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00139.2003 · Cited by 158

Endoplasmic Reticulum Stress Implicated in the Development of Renal Fibrosis

Chiang, C., Hsu, S. P., Wu, C.-T., Huang, J., Cheng, H., Chang, Y.-W., Hung, K., Wu, K.-D., & Liu, S. (2011) · Molecular Medicine · doi:10.2119/molmed.2011.00131 · Cited by 156

Heparin-binding peptides from thrombospondins 1 and 2 contain focal adhesion-labilizing activity.

Murphy-Ullrich, J. E., Gurusiddappa, S., Frazier, W. A., & Höök, M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74381-6 · Cited by 156

Endoplasmic reticulum stress is activated in post-ischemic kidneys to promote chronic kidney disease

Shu, S., Zhu, J., Liu, Z., Tang, C., Cai, J., & Dong, Z. (2018) · EBioMedicine · doi:10.1016/j.ebiom.2018.10.006 · Cited by 155

Endoplasmic reticulum stress as a pro-fibrotic stimulus

Tanjore, H., Lawson, W. E., & Blackwell, T. S. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.11.011 · Cited by 151

Thrombospondin-1 is a major activator of TGF-β in fibrotic renal disease in the rat in vivo

Daniel, C., Wiede, J., Krutzsch, H. C., Ribeiro, S. M. F., Roberts, D. D., Murphy-Ullrich, J. E., & Hugo, C. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.00395.x · Cited by 142

Glomerular expression of thrombospondin-1, transforming growth factor beta and connective tissue growth factor at different stages of diabetic nephropathy and their interdependent roles in mesangial response to diabetic stimuli

Wahab, N. A., Schaefer, L., Weston, B. S., Yiannikouris, O., Wright, A., Bábelová, A., Schaefer, R. M., & Mason, R. M. (2005) · Diabetologia · doi:10.1007/s00125-005-0006-5 · Cited by 139

SGLT2 Inhibition for the Prevention and Treatment of Diabetic Kidney Disease: A Review

Alicic, R. Z., Johnson, E. J., & Tuttle, K. R. (2018) · American Journal of Kidney Diseases · doi:10.1053/j.ajkd.2018.03.022 · Cited by 136

Attenuation of endoplasmic reticulum stress using the chemical chaperone 4-phenylbutyric acid prevents cardiac fibrosis induced by isoproterenol

Ayala, P., Montenegro, J., Vivar, R., Letelier, A., Aránguiz, P., Copaja, M., Pivet, D., Humeres, C. D., Troncoso, R., Vicencio, J. M., et al. (2011) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2011.10.012 · Cited by 123

Interaction of human thrombospondin with types I-V collagen: direct binding and electron microscopy.

Galvin, N. J., Vance, P., Dixit, V. M., Fink, B., & Frazier, W. A. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.104.5.1413 · Cited by 121

Tissue-type plasminogen activator promotes murine myofibroblast activation through LDL receptor–related protein 1–mediated integrin signaling

Hu, K., Wu, C., Mars, W. M., & Liu, Y. (2007) · Journal of Clinical Investigation · doi:10.1172/jci32301 · Cited by 119

Molecular Interactions That Confer Latency to Transforming Growth Factor-β

Young, G. D., & Murphy-Ullrich, J. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405658200 · Cited by 118

A Thrombospondin-1 Antagonist of Transforming Growth Factor-β Activation Blocks Cardiomyopathy in Rats with Diabetes and Elevated Angiotensin II

Belmadani, S., Bernal, J., Wei, C., Pallero, M. A., Dell’Italia, L. J., Murphy-Ullrich, J. E., & Berecek, K. H. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070056 · Cited by 118

Influence of genetic background on albuminuria and kidney injury in Ins2+/C96Y (Akita) mice

Gurley, S. B., Mach, C. L., Stegbauer, J., Yang, J., Snow, K. P., Hu, A., Meyer, T. W., & Coffman, T. M. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90515.2008 · Cited by 116

Thrombospondin 1 mediates angiotensin II induction of TGF-β activation by cardiac and renal cells under both high and low glucose conditions

Zhou, Y., Poczatek, M. H., Berecek, K. H., & Murphy-Ullrich, J. E. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.11.060 · Cited by 114

Glycated albumin stimulates TGF-βbgr;1 production and protein kinase C activity in glomerular endothelial cells

Chen, S., Cohen, M. P., Lautenslager, G. T., Shearman, C. W., & Ziyadeh, F. N. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.059002673.x · Cited by 113

Glucose Up-regulates Thrombospondin 1 Gene Transcription and Transforming Growth Factor-β Activity through Antagonism of cGMP-dependent Protein Kinase Repression via Upstream Stimulatory Factor 2

Wang, S., Skorczewski, J., Feng, X., Mei, L., & Murphy-Ullrich, J. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401629200 · Cited by 112

Thrombospondin-1 promotes matrix homeostasis by interacting with collagen and lysyl oxidase precursors and collagen cross-linking sites

Rosini, S., Pugh, N., Bonna, A., HULMES, D. J. S., Farndale, R. W., & Adams, J. C. (2018) · Science Signaling · doi:10.1126/scisignal.aar2566 · Cited by 112

COMP mutations, chondrocyte function and cartilage matrix

Hecht, J. T., HAYES, E., HAYNES, R., & COLE, W. (2004) · Matrix Biology · doi:10.1016/j.matbio.2004.09.006 · Cited by 112

The Anti-adhesive Activity of Thrombospondin Is Mediated by the N-terminal Domain of Cell Surface Calreticulin

Goicoechea, S. M., Pallero, M. A., Eggleton, P., Michalak, M., & Murphy-Ullrich, J. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202200200 · Cited by 110

Calreticulin Enhances Porcine Wound Repair by Diverse Biological Effects

Nanney, L. B., Woodrell, C. D., Greives, M. R., Cardwell, N. L., Pollins, A. C., Bancroft, T. A., Chesser, A. S., Michalak, M., Rahman, M. M., Siebert, J. W., et al. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.071027 · Cited by 109

The release of heparin binding peptides from platelet thrombospondin by proteolytic action of thrombin, plasmin and trypsin

Lawler, J., & Slayter, H. S. (1981) · Thrombosis Research · doi:10.1016/0049-3848(81)90119-5 · Cited by 109

Involvement of Calcineurin in Transforming Growth Factor-β-mediated Regulation of Extracellular Matrix Accumulation

Gooch, J. L., Gorin, Y. C., Zhang, B.-X., & Abboud, H. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308759200 · Cited by 106

Glucose Stimulation of Transforming Growth Factor-β Bioactivity in Mesangial Cells Is Mediated by Thrombospondin-1

Poczatek, M. H., Hugo, C., Darley-Usmar, V. M., & Murphy-Ullrich, J. E. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64649-4 · Cited by 105

Thrombospondin-1 Is an Endogenous Activator of TGF-β in Experimental Diabetic Nephropathy In Vivo

Daniel, C., Schaub, K., Amann, K., Lawler, J., & Hugo, C. (2007) · Diabetes · doi:10.2337/db07-0551 · Cited by 105

Thrombospondin and Apoptosis: Molecular Mechanisms and Use for Design of Complementation Treatments

Mirochnik, Y., Kwiatek, A. M., & Volpert, O. V. (2008) · Current Drug Targets · doi:10.2174/138945008785909347 · Cited by 104

Glycosylation Mediates Up-regulation of a Potent Antiangiogenic and Proatherogenic Protein, Thrombospondin-1, by Glucose in Vascular Smooth Muscle Cells

Raman, P., Krukovets, I., Marinic, T. E., BORNSTEIN, P. K., & Stenina‐Adognravi, O. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m610965200 · Cited by 99

Targeting CD47: the achievements and concerns of current studies on cancer immunotherapy

Huang, Y.-T., Ma, Y., Gao, P., & Yao, Z. (2017) · Journal of Thoracic Disease · doi:10.21037/jtd.2017.02.30 · Cited by 99

Thrombospondin 1 precedes and predicts the development of tubulointerstitial fibrosis in glomerular disease in the rat

Hugo, C., Shankland, S. J., Pichler, R. H., Couser, W. G., & Johnson, R. J. (1998) · Kidney International · doi:10.1046/j.1523-1755.1998.00774.x · Cited by 98

Thrombospondin1 Deficiency Reduces Obesity-Associated Inflammation and Improves Insulin Sensitivity in a Diet-Induced Obese Mouse Model

Li, Y., Tong, X., Rumala, C., Clemons, K., & Wang, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026656 · Cited by 97

Thrombospondin Stimulates Focal Adhesion Disassembly through Gi- and Phosphoinositide 3-Kinase-dependent ERK Activation

Orr, A. W., Pallero, M. A., & Murphy-Ullrich, J. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112091200 · Cited by 93

Blockade of TSP1-Dependent TGF-β Activity Reduces Renal Injury and Proteinuria in a Murine Model of Diabetic Nephropathy

Lu, A., Miao, M., Schoeb, T. R., Agarwal, A., & Murphy-Ullrich, J. E. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.02.039 · Cited by 92

Thrombospondin-1 Is the Key Activator of TGF-β1 in Human Mesangial Cells Exposed to High Glucose

Yevdokimova, N. Y., Wahab, N. A., & Mason, R. M. (2001) · Journal of the American Society of Nephrology · doi:10.1681/asn.v124703 · Cited by 92

Skeletal Abnormalities in Mice Lacking Extracellular Matrix Proteins, Thrombospondin-1, Thrombospondin-3, Thrombospondin-5, and Type IX Collagen

Posey, K. L., Hankenson, K. D., Veerisetty, A. C., BORNSTEIN, P. K., Lawler, J., & Hecht, J. T. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.071094 · Cited by 90

The Physiological Function of Store-operated Calcium Entry

Putney, J. W. (2011) · Neurochemical Research · doi:10.1007/s11064-010-0383-0 · Cited by 90

The Tryptophan-rich Motifs of the Thrombospondin Type 1 Repeats Bind VLAL Motifs in the Latent Transforming Growth Factor-β Complex

Young, G. D., & Murphy-Ullrich, J. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404918200 · Cited by 89

Calreticulin, PDI, Grp94 and BiP chaperone proteins are associated with retained COMP in pseudoachondroplasia chondrocytes

Hecht, J. T., Hayes, E., Snuggs, M. B., Decker, G. L., Montufar‐Solis, D., Doege, K. J., Mwalle, F., Poole, R., Stevens, J. W., & Duke, P. J. (2001) · Matrix Biology · doi:10.1016/s0945-053x(01)00136-6 · Cited by 89

High glucose inhibits renal proximal tubule cell proliferation and involves PKC, oxidative stress, and TGF-β1

Park, S. H., Choi, H.-J., Lee, J., Woo, C.-H., Kim, J., & Han, H. J. (2001) · Kidney International · doi:10.1046/j.1523-1755.2001.0590051695.x · Cited by 89

Capillary rarefaction from the kidney point of view

Afşar, B., Afşar, R. E., Dağel, T., Kaya, E., Erus, S., Ortíz, A., Covic, A. C., & Kanbay, M. (2017) · Clinical Kidney Journal · doi:10.1093/ckj/sfx133 · Cited by 88

CD47 regulates renal tubular epithelial cell self-renewal and proliferation following renal ischemia reperfusion

Rogers, N. M., Zhang, Z. J., Wang, J.-J., Thomson, A. W., & Isenberg, J. S. (2016) · Kidney International · doi:10.1016/j.kint.2016.03.034 · Cited by 87

NFAT2 inhibitor ameliorates diabetic nephropathy and podocyte injury in db/db mice

Zhang, L., Li, R., Shi, W., Liang, X., Liu, S., Ye, Z., Yu, C., Chen, Y., Zhang, B., Wang, W., et al. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12292 · Cited by 86

Thrombospondin 1 binding to calreticulin‐LRP1 signals resistance to anoikis

Pallero, M. A., Elzie, C. A., Chen, J., Mosher, D. F., & Murphy-Ullrich, J. E. (2008) · The FASEB Journal · doi:10.1096/fj.07-104802 · Cited by 86

Nitric Oxide and cGMP-dependent Protein Kinase Regulation of Glucose-mediated Thrombospondin 1-dependent Transforming Growth Factor-β Activation in Mesangial Cells

Wang, S., Shiva, S., Poczatek, M. H., Darley-Usmar, V. M., & Murphy-Ullrich, J. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108360200 · Cited by 85

Peters Plus Syndrome Mutations Disrupt a Noncanonical ER Quality-Control Mechanism

Vasudevan, D., Takeuchi, H., Johar, S. S., Majerus, E., & Haltiwanger, R. S. (2015) · Current Biology · doi:10.1016/j.cub.2014.11.049 · Cited by 84

Invoking the power of thrombospondins: Regulation of thrombospondins expression

Stenina‐Adognravi, O. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.02.001 · Cited by 83

Stress Signal Network between Hypoxia and ER Stress in Chronic Kidney Disease

Maekawa, H., & Inagi, R. (2017) · Frontiers in Physiology · doi:10.3389/fphys.2017.00074 · Cited by 83

Transient potential receptor channel 4 controls thrombospondin‐1 secretion and angiogenesis in renal cell carcinoma

Veliceasa, D., Ivanovic, M., Schulze-Hoepfner, F. T., Thumbikat, P., Volpert, O. V., & Smith, N. D. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.06159.x · Cited by 83

Chemical chaperon 4-phenylbutyrate protects against the endoplasmic reticulum stress-mediated renal fibrosisin vivoandin vitro

Liu, S., Yang, C.-C., Chan, D., Wu, C., Chen, L., Huang, J., Hung, K., & Chiang, C. (2016) · Oncotarget · doi:10.18632/oncotarget.7904 · Cited by 82

The N-terminus of thrombospondin: the domain stands apart

Elzie, C. A., & Murphy-Ullrich, J. E. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2003.12.012 · Cited by 79

Twenty years after ACEIs and ARBs: emerging treatment strategies for diabetic nephropathy

Johnson, S. A., & Spurney, R. F. (2015) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00266.2015 · Cited by 76

Thrombospondin 1 activates the macrophage Toll-like receptor 4 pathway

Li, Y., Qi, X., Tong, X., & Wang, S. (2013) · Cellular and Molecular Immunology · doi:10.1038/cmi.2013.32 · Cited by 72

Anti-fibrotic treatments: A review of clinical evidence

Allinovi, M., Chiara, L. D., Angelotti, M. L., Becherucci, F., & Romagnani, P. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.02.017 · Cited by 71

Endoplasmic reticulum stress and kidney dysfunction

Gallazzini, M., & Pallet, N. (2018) · Biology of the Cell · doi:10.1111/boc.201800019 · Cited by 71

Thrombospondin Induces RhoA Inactivation through FAK-dependent Signaling to Stimulate Focal Adhesion Disassembly

Orr, A. W., Pallero, M. A., Xiong, W., & Murphy-Ullrich, J. E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404881200 · Cited by 71

Calcineurin is activated in diabetes and is required for glomerular hypertrophy and ECM accumulation

Gooch, J. L., Barnes, J. L., Garcia, S., & Abboud, H. E. (2003) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00158.2002 · Cited by 70

Developing Treatments for Chronic Kidney Disease in the 21st Century

Breyer, M. D., & Suszták, K. (2016) · Seminars in Nephrology · doi:10.1016/j.semnephrol.2016.08.001 · Cited by 68

Renal fibrosis: Recent translational aspects

François, H., & Chatziantoniou, C. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.12.013 · Cited by 68

Antisense Oligonucleotides Against Thrombospondin-1 Inhibit Activation of TGF-β in Fibrotic Renal Disease in the Rat in Vivo

Daniel, C., Takabatake, Y., Mizui, M., Isaka, Y., Kawashi, H., Rupprecht, H., Imai, E., & Hugo, C. (2003) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63478-5 · Cited by 66

Thrombospondin 1 protects pancreatic β-cells from lipotoxicity via the PERK–NRF2 pathway

Cunha, D. A., Cito, M., Carlsson, P., Vanderwinden, J., Molkentin, J. D., Bugliani, M., Marchetti, P., Eizirik, D. L., & Cnop, M. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.89 · Cited by 66

Altered expression of calreticulin during the development of fibrosis

Kypreou, K. P., Kavvadas, P., Karamessinis, P. M., Peroulis, M., Alberti, A., Sideras, P., Psarras, S., Capetanaki, Y., Politis, P. K., & CHARONIS, A. S. (2008) · PROTEOMICS · doi:10.1002/pmic.200700831 · Cited by 66

Calreticulin Regulates Transforming Growth Factor-β-stimulated Extracellular Matrix Production

Zimmerman, K. A., Graham, L. V. D., Pallero, M. A., & Murphy-Ullrich, J. E. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.447243 · Cited by 65

Fibroblast growth factor-2 binding to the thrombospondin-1 type III repeats, a novel antiangiogenic domain

Margosio, B., Rusnati, M., Bonezzi, K., Cordes, B.-L. A., Annis, D. S., Urbinati, C., Giavazzi, R., Presta, M., Ribatti, D., Mosher, D. F., et al. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.10.002 · Cited by 64

Thrombospondin Signaling of Focal Adhesion Disassembly Requires Activation of Phosphoinositide 3-Kinase

Greenwood, J. A., Pallero, M. A., Theibert, A. B., & Murphy-Ullrich, J. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1755 · Cited by 62

Expression of Constitutively Active cGMP-Dependent Protein Kinase Prevents Glucose Stimulation of Thrombospondin 1 Expression and TGF-β Activity

Wang, S., Wu, X., Lincoln, T., & Murphy-Ullrich, J. E. (2003) · Diabetes · doi:10.2337/diabetes.52.8.2144 · Cited by 61

Inhibition of the Unfolded Protein Response Mechanism Prevents Cardiac Fibrosis

Groenendyk, J., Lee, D., Jung, J., Dyck, J. R. B., Lopaschuk, G. D., Agellon, L. B., & Michalak, M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0159682 · Cited by 61

Synergistic role of HSP90α and HSP90β to promote myofibroblast persistence in lung fibrosis

Bellaye, P., Shimbori, C., Yanagihara, T., Carlson, D. A., Hughes, P. F., Upagupta, C., Sato, S., Wheildon, N., Haystead, T., Ask, K., et al. (2018) · European Respiratory Journal · doi:10.1183/13993003.00386-2017 · Cited by 61

Thrombospondin secretion by cultured human glomerular mesangial cells.

Raugi, G. J., & Lovett, D. H. (1987) · PubMed Central · Cited by 60

Thrombospondin in Renal Disease

Hugo, C., & Daniel, C. (2009) · Nephron Experimental Nephrology · doi:10.1159/000198235 · Cited by 58

Intracellular Calreticulin Regulates Multiple Steps in Fibrillar Collagen Expression, Trafficking, and Processing into the Extracellular Matrix

Graham, L. V. D., Sweetwyne, M. T., Pallero, M. A., & Murphy-Ullrich, J. E. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.006841 · Cited by 56

Safer approaches to therapeutic modulation of TGF-β signaling for respiratory disease

Lachapelle, P., Li, M., Douglass, J. A., & Stewart, A. G. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.02.010 · Cited by 54

Thrombospondin-2 regulates extracellular matrix production, LOX levels, and cross-linking via downregulation of miR-29

Calabro, N. E., Barrett, A. S., Chamorro-Jorganes, A., Tam, S. N., Kristofik, N. J., Xing, H., Loye, A. M., Sessa, W. C., Hansen, K. C., & Kyriakides, T. R. (2019) · Matrix Biology · doi:10.1016/j.matbio.2019.03.002 · Cited by 53

Antioxidant for treatment of diabetic nephropathy: A systematic review and meta-analysis

Kandhare, A. D., Mukherjee-Kandhare, A. A., & Bodhankar, S. L. (2017) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2017.10.031 · Cited by 52

Unraveling reno-protective effects of SGLT2 inhibition in human proximal tubular cells

Pirklbauer, M., Schupart, R., Fuchs, L., Staudinger, P., Corazza, U., Sallaberger, S., Leierer, J., Mayer, G. J., & Schramek, H. (2018) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00431.2018 · Cited by 52

Hypertension and Diabetes: Role of the Renin-Angiotensin System

Jandeleit-Dahm, K. A. M., & Cooper, M. E. (2006) · Endocrinology and Metabolism Clinics of North America · doi:10.1016/j.ecl.2006.06.007 · Cited by 51

Thrombospondin-1 promotes mesenchymal stromal cell functions via TGFβ and in cooperation with PDGF

Belotti, D., Capelli, C., Resovi, A., Introna, M., & Taraboletti, G. (2016) · Matrix Biology · doi:10.1016/j.matbio.2016.03.003 · Cited by 50

Correlation of enhanced thrombospondin-1 expression, TGF- signalling and proteinuria in human type-2 diabetic nephropathy

Hohenstein, B., Daniel, C., Hausknecht, B., Boehmer, K., Riess, R. H., Amann, K., & Hugo, C. P. M. (2008) · Nephrology Dialysis Transplantation · doi:10.1093/ndt/gfn399 · Cited by 49

Pancreatic β-cell protection from inflammatory stress by the endoplasmic reticulum proteins thrombospondin 1 and mesencephalic astrocyte-derived neutrotrophic factor (MANF)

Cunha, D. A., Cito, M., Grieco, F. A., Cosentino, C., Danilova, T., Ladrière, L., Lindahl, M., Domanskyi, A., Bugliani, M., Marchetti, P., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.769877 · Cited by 48

LRP1: A chameleon receptor of lung inflammation and repair

Wujak, L. A., Schnieder, J., Schaefer, L., & Wygrecka, M. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.12.007 · Cited by 48

LSKL, a peptide antagonist of thrombospondin-1, attenuates renal interstitial fibrosis in rats with unilateral ureteral obstruction

Xie, X., Li, F., Liu, H., Deng, Y. L., Li, Z., & Fan, J. (2010) · Archives of Pharmacal Research · doi:10.1007/s12272-010-0213-6 · Cited by 48

Thrombospondin 1 mediates renal dysfunction in a mouse model of high-fat diet-induced obesity

Cui, W., Maimaitiyiming, H., Qi, X., Norman‐Burgdolf, H., & Wang, S. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00209.2013 · Cited by 47

Endoplasmic reticulum stress inhibition attenuates hypertensive chronic kidney disease through reduction in proteinuria

Mohammed‐Ali, Z., Lü, C., Marway, M. K., Carlisle, R. E., Ask, K., Lukic, D., Krepinsky, J. C., & Dickhout, J. G. (2017) · Scientific Reports · doi:10.1038/srep41572 · Cited by 46

Induction of Thrombospondin Expression in Vascular Smooth Muscle Cells by Angiotensin II

Scott‐Burden, T., Resink, T. J., Hahn, A. W. A., & Bühler, F. R. (1990) · Journal of Cardiovascular Pharmacology · doi:10.1097/00005344-199000167-00007 · Cited by 45

Thrombospondin 2 Functions as an Endogenous Regulator of Angiogenesis and Inflammation in Experimental Glomerulonephritis in Mice

Daniel, C., Amann, K., Hohenstein, B., BORNSTEIN, P. K., & Hugo, C. (2007) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006080873 · Cited by 44

Thrombospondin in human glomerulopathies. A marker of inflammation and early fibrosis.

McGregor, B., Colon, S., Mutin, M., Chignier, E., Zech, P. Y., & McGregor, J. L. (1994) · PubMed Central · Cited by 44

Store-Operated Ca2+ Entry (SOCE) contributes to angiotensin II-induced cardiac fibrosis in cardiac fibroblasts

Zhang, B., Jiang, J., Yue, Z., Liu, S., Ma, Y., Yu, N., Gao, Y., Sun, S., Chen, S., & Liu, P. (2016) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2016.05.008 · Cited by 44

Identification and Characterization of Novel Matrix-Derived Bioactive Peptides: A Role for Collagenase from Santyl® Ointment in Post-Debridement Wound Healing?

Sheets, A. R., Demidova‐Rice, T. N., Shi, L., Ronfard, V., Grover, K. V., & Herman, I. M. (2016) · PLoS ONE · doi:10.1371/journal.pone.0159598 · Cited by 44

The calcium-binding type III repeats domain of thrombospondin-2 binds to fibroblast growth factor 2 (FGF2)

Rusnati, M., Borsotti, P., Moroni, E., Foglieni, C., Chiodelli, P., Carminati, L., Pinessi, D., Annis, D. S., Paiardi, G., Bugatti, A., et al. (2018) · Angiogenesis · doi:10.1007/s10456-018-9644-3 · Cited by 43

Growth factors and the development of diabetic nephropathy

Wolf, G. (2003) · Current Diabetes Reports · doi:10.1007/s11892-003-0012-2 · Cited by 41

Exogenous calreticulin improves diabetic wound healing

Greives, M. R., Samra, F., Pavlides, S. C., Blechman, K. M., Naylor, S., Woodrell, C. D., Cadacio, C., Levine, J. P., Bancroft, T. A., Michalak, M., et al. (2012) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2012.00822.x · Cited by 40

Proteolysis of thrombospondin during cathepsin‐G‐induced platelet aggregation: functional role of the 165‐kDa carboxy‐terminal fragment

Rabhi-Sabile, S., Pidard, D., Lawler, J., Renesto, P., Chignard, M., & Legrand, C. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00408-5 · Cited by 39

Sustained Expression of Thrombospondin-1 Is Associated with the Development of Glomerular and Tubulointerstitial Fibrosis in the Remnant Kidney Model

Hugo, C., Kang, D., & Johnson, R. J. (2002) · The Nephron journals/Nephron journals · doi:10.1159/000054735 · Cited by 38

The Calreticulin-Binding Sequence of Thrombospondin 1 Regulates Collagen Expression and Organization During Tissue Remodeling

Sweetwyne, M. T., Pallero, M. A., Lu, A., Graham, L. V. D., & Murphy-Ullrich, J. E. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090903 · Cited by 36

High Glucose-Induced Podocyte Injury Involves Activation of Mammalian Target of Rapamycin (mTOR)-Induced Endoplasmic Reticulum (ER) Stress

Lei, J., Zhao, L., Zhang, Y., Wu, Y., & Liu, Y. (2018) · Cellular Physiology and Biochemistry · doi:10.1159/000488231 · Cited by 36

Thrombospondin-1 mediates distal tubule hypertrophy induced by glycated albumin

Yang, Y., Chuang, L., Guh, J., Shu-Fen, L. I. U., Hung, M., Liao, T., & Huang, Y.-L. (2004) · Biochemical Journal · doi:10.1042/bj20031730 · Cited by 36

Oncostatin M is a novel inhibitor of TGF-β1-induced matricellular protein expression

Sárközi, R., Hauser, C., Noppert, S.-J., Kronbichler, A., Pirklbauer, M., Haller, V., Grillari, J., Grillari‐Voglauer, R., Mayer, G. J., & Schramek, H. (2011) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00123.2011 · Cited by 36

Mutant cartilage oligomeric matrix protein (COMP) compromises bone integrity, joint function and the balance between adipogenesis and osteogenesis

Coustry, F., Posey, K. L., Maerz, T., Baker, K. C., Abraham, A. M., Ambrose, C. G., Nobakhti, S., Shefelbine, S. J., Bi, X., Newton, M. D., et al. (2018) · Matrix Biology · doi:10.1016/j.matbio.2017.12.014 · Cited by 35

NFATc is required for TGFβ-mediated transcriptional regulation of fibronectin

Cobbs, S. L., & Gooch, J. L. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.07.186 · Cited by 34

Anti-CD47 monoclonal antibody therapy reduces ischemia-reperfusion injury of renal allografts in a porcine model of donation after cardiac death

Xu, M., Wang, X., Banan, B., Chirumbole, D. L., Garcia-Aroz, S., Balakrishnan, A., Nayak, D. K., Zhang, Z., Jia, J., Upadhya, G. A., et al. (2017) · American Journal of Transplantation · doi:10.1111/ajt.14567 · Cited by 34

Thrombospondin-1 Short Hairpin RNA Suppresses Tubulointerstitial Fibrosis in the Kidney of Ureteral Obstruction by Ameliorating Peritubular Capillary Injury

Sun, D., Ma, H., Han, H. X., Yin, Z., Liu, C., Feng, J., Zhou, X., Li, X., Xiao, A., & Yu, R. (2011) · Kidney & Blood Pressure Research · doi:10.1159/000330718 · Cited by 33

Ablation of C/EBP homologous protein attenuates renal fibrosis after ureteral obstruction by reducing autophagy and microtubule disruption

Noh, M. R., Woo, C.-H., Park, M.-J., In Kim, J., & Park, K. M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.02.001 · Cited by 33

Thrombospondin-2 therapy ameliorates experimental glomerulonephritis via inhibition of cell proliferation, inflammation, and TGF-β activation

Daniel, C., Wagner, A., Hohenstein, B., & Hugo, C. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00254.2009 · Cited by 32

Overexpression of upstream stimulatory factor 2 accelerates diabetic kidney injury

Liu, S., Shi, L., & Wang, S. (2007) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00316.2007 · Cited by 31

Members of the thrombospondin gene family bind stromal interaction molecule 1 and regulate calcium channel activity

Duquette, M. A., Nadler, M. J. S., Okuhara, D. Y., Thompson, J. L., Shuttleworth, T. J., & Lawler, J. (2014) · Matrix Biology · doi:10.1016/j.matbio.2014.05.004 · Cited by 31

Insider trading: Extracellular matrix proteins and their non‐canonical intracellular roles

Hellewell, A. L., & Adams, J. C. (2015) · BioEssays · doi:10.1002/bies.201500103 · Cited by 30

The role of the endoplasmic reticulum protein calreticulin in mediating TGF-β-stimulated extracellular matrix production in fibrotic disease

Owusu, B. Y., Zimmerman, K. A., & Murphy-Ullrich, J. E. (2017) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-017-0426-2 · Cited by 30

Interaction of thrombospondin1 and CD36 contributes to obesity-associated podocytopathy

Cui, W., Maimaitiyiming, H., Zhou, Q., Norman‐Burgdolf, H., Zhou, C., & Wang, S. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.03.010 · Cited by 28

BlockingαVβ3 Integrin Ligand Occupancy Inhibits the Progression of Albuminuria in Diabetic Rats

Maile, L. A., Gollahon, K. A., Wai, C., Dunbar, P. R., Busby, W. H., & Clemmons, D. R. (2014) · Journal of Diabetes Research · doi:10.1155/2014/421827 · Cited by 26

The role of plasma membrane STIM1 and Ca2+entry in platelet aggregation. STIM1 binds to novel proteins in human platelets

Ambily, A., Kaiser, W. J., Pierro, C., Chamberlain, E. V., Li, Z., Jones, C. I., Kassouf, N., Gibbins, J. M., & Authi, K. S. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.11.025 · Cited by 25

Thrombospondin peptides are potent inhibitors of mesangial and glomerular endothelial cell proliferation in vitro and in vivo

Hugo, C., Pichler, R. P., Schulze-Lohoff, E., Pröls, F., Adler, S., Krutsch, H. C., Murphy-Ullrich, J. E., Couser, W. G., Roberts, D. D., & Johnson, R. J. (1999) · Kidney International · doi:10.1046/j.1523-1755.1999.00459.x · Cited by 25

Thrombospondin-1 Deficiency Causes a Shift from Fibroproliferative to Inflammatory Kidney Disease and Delays Onset of Renal Failure

Zeisberg, M., Tampe, B., LeBleu, V. S., Tampe, D., Zeisberg, E. M., & Kalluri, R. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2014.06.014 · Cited by 24

Myeloid-specific deletion of thrombospondin 1 protects against inflammation and insulin resistance in long-term diet-induced obese male mice

Memetimin, H., Li, D., Tan, K., Zhou, C., Liang, Y., Wu, Y., & Wang, S. (2018) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00273.2018 · Cited by 24

The role of CD47 in pathogenesis and treatment of renal ischemia reperfusion injury

Isenberg, J. S., & Roberts, D. D. (2018) · Pediatric Nephrology · doi:10.1007/s00467-018-4123-z · Cited by 24

Tofogliflozin, a selective inhibitor of sodium-glucose cotransporter 2, suppresses renal damage in KKAy/Ta mice, obese and type 2 diabetic animals

Ishibashi, Y., Matsui, T., & Yamagishi, S. (2016) · Diabetes and Vascular Disease Research · doi:10.1177/1479164116657304 · Cited by 24

COMP and TSP-4 interact specifically with the novel GXKGHR motif only found in fibrillar collagens

Gebauer, J. M., Köhler, A., Dietmar, H. F., Gompert, M., Neundorf, I., Zaucke, F., Koch, M., & Baumann, U. (2018) · Scientific Reports · doi:10.1038/s41598-018-35447-8 · Cited by 22

Integrating computational and chemical biology tools in the discovery of antiangiogenic small molecule ligands of FGF2 derived from endogenous inhibitors

Foglieni, C., Pagano, K., Lessi, M., Bugatti, A., Moroni, E., Pinessi, D., Resovi, A., Ribatti, D., Bertini, S., Ragona, L., et al. (2016) · Scientific Reports · doi:10.1038/srep23432 · Cited by 21

Epithelial Calreticulin Up-Regulation Promotes Profibrotic Responses and Tubulointerstitial Fibrosis Development

Prakoura, N., Politis, P. K., Ihara, Y., Michalak, M., & CHARONIS, A. S. (2013) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.07.014 · Cited by 20

Initiation of fibrosis in the integrin Αvβ6 knockout mice

Wu, W., Hutcheon, A. E. K., Sriram, S., Tran, J. A., & Zieske, J. D. (2018) · Experimental Eye Research · doi:10.1016/j.exer.2018.11.027 · Cited by 19

Gene expression patterns in glucose-stimulated podocytes

Han, S. H., Yang, S., Jung, D. S., Li, J. J., Kim, J., Kwak, S. J., Kim, D. K., Moon, S. J., Lee, J. E., Han, D. S., et al. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.121 · Cited by 19

Immunosurveillance by Antiangiogenesis: Tumor Growth Arrest by T Cell–Derived Thrombospondin-1

Schadler, K., Crosby, E. J., Zhou, A. Y., Bhang, D. H., Braunstein, L. Z., Baek, K. H., Crawford, D. A., Crawford, A., Angelosanto, J., Wherry, E. J., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-0094 · Cited by 18

Calreticulin Regulates Neointima Formation and Collagen Deposition following Carotid Artery Ligation

Zimmerman, K. A., Xing, D., Pallero, M. A., Lu, A., Ikawa, M., Black, L. L., Hoyt, K., Kabarowski, J. H. S., Michalak, M., & Murphy-Ullrich, J. E. (2015) · Journal of Vascular Research · doi:10.1159/000443884 · Cited by 18

Antiproteinuric effect of RAS blockade: New mechanisms

Lassila, M., Cooper, M. E., & Jandeleit-Dahm, K. A. M. (2004) · Current Hypertension Reports · doi:10.1007/s11906-004-0058-9 · Cited by 17

Novel Aspects of Transforming Growth Factor-Beta in Diabetic Kidney Disease

Tsuchida, K., Cronin, B., & Sharma, K. (2002) · The Nephron journals/Nephron journals · doi:10.1159/000064486 · Cited by 16

Tissue-type plasminogen activator suppresses activated stellate cells through low-density lipoprotein receptor-related protein 1

Kang, L., Isse, K., Koral, K., Bowen, W. C., Muratoglu, S. C., Strickland, D. K., Michalopoulos, G. K., & Mars, W. M. (2015) · Laboratory Investigation · doi:10.1038/labinvest.2015.94 · Cited by 16

Enhanced Effect of Combined Treatment with SMP-534 (Antifibrotic Agent) and Losartan in Diabetic Nephropathy

Sugaru, E., Nakagawa, T., Ono‐Kishino, M., Nagamine, J., Tokunaga, T., Kitoh, M., Hume, W. E., Nagata, R., & Taiji, M. (2006) · American Journal of Nephrology · doi:10.1159/000091786 · Cited by 16

Long-Term Gene Therapy with Thrombospondin 2 Inhibits TGF-β Activation, Inflammation and Angiogenesis in Chronic Allograft Nephropathy

Daniel, C., Vogelbacher, R., Stief, A., Grigo, C., & Hugo, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0083846 · Cited by 16

Amelioration of Established Diabetic Nephropathy by Combined Treatment with SMP-534 (Antifibrotic Agent) and Losartan in db/db Mice

Sugaru, E., Nakagawa, T., Ono‐Kishino, M., Nagamine, J., Tokunaga, T., Kitoh, M., Hume, W. E., Nagata, R., & Taiji, M. (2006) · Nephron Experimental Nephrology · doi:10.1159/000097603 · Cited by 16

Differential Expression of Thrombospondin and Cellular Fibronectin During Remodeling in Proliferative Glomerulonephritis

Barnes, J. L., Mitchell, R. J., Kanalas, J. J., & Barnes, V. L. (1999) · Journal of Histochemistry & Cytochemistry · doi:10.1177/002215549904700412 · Cited by 16

Rapid hepatic clearance of full length CCN-2/CTGF: a putative role for LRP1-mediated endocytosis

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