The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Stimulated Shedding of Vascular Cell Adhesion Molecule 1 (VCAM-1) Is Mediated by Tumor Necrosis Factor-α-converting Enzyme (ADAM 17)
Open accessAbstract
A variety of cell surface adhesion molecules can exist as both transmembrane proteins and soluble circulating forms. Increases in the levels of soluble adhesion molecules have been correlated with a variety of inflammatory diseases, suggesting a pathological role. Although soluble forms are thought to result from proteolytic cleavage from the cell surface, relatively little is known about the proteases responsible for their release. In this report we demonstrate that under normal culture conditions, cells expressing vascular cell adhesion molecule 1 (VCAM-1) release a soluble form of the extracellular domain that is generated by metalloproteinase-mediated cleavage. VCAM-1 release can be rapidly simulated by phorbol 12-myristate 13-acetate (PMA), and this induced VCAM-1 shedding is mediated by metalloproteinase cleavage of VCAM-1 near the transmembrane domain. PMA-induced VCAM-1 shedding occurs as the result of activation of a specific pathway, as the generation of soluble forms of three other adhesion molecules, E-selectin, platelet-endothelial cell adhesion molecule 1, and intercellular adhesion molecule 1, are not altered by PMA stimulation. Using cells derived from genetically deficient mice, we identify tumor necrosis factor-alpha-converting enzyme (TACE or ADAM 17) as the protease responsible for PMA-induced VCAM-1 release, including shedding of endogenously expressed VCAM-1 by murine endothelial cells. Therefore, TACE-mediated shedding of VCAM-1 may be important for the regulation of VCAM-1 function at the cell surface.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Of interest, circulating VCAM1 is shed by the metalloproteinase ADAM metallopeptidase domain 17 (ADAM17, AKA TNF alpha-converting enzyme (TACE)) which is activated by inflammatory stimuli [81].”
From “Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels (2017) · cites this paper as [81]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149
An Essential Role for Ectodomain Shedding in Mammalian Development
Peschon, J. J., Slack, J. L., Reddy, P., Stocking, K. L., Sunnarborg, S. W., Lee, D. C., Russell, W. E., Castner, B. J., Johnson, R. S., Fitzner, J. N., et al. (1998) · Science · doi:10.1126/science.282.5392.1281 · Cited by 1,622
Circulating adhesion molecules in disease
Gearing, A. J. H., & Newman, W. (1993) · Immunology Today · doi:10.1016/0167-5699(93)90267-o · Cited by 1,371
A Novel Proteolytic Cleavage Involved in Notch Signaling
Brou, C., Logeat, F., Gupta-Rossi, N., Chable-Bessia, C., Bail, O. L., Doedens, J. R., Cumano, A., Roux, P., Black, R. A., & Israël, A. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80417-7 · Cited by 1,115
Neutrophil Mac-1 and MEL-14 Adhesion Proteins Inversely Regulated by Chemotactic Factors
Kishimoto, T., Jutila, M. A., Berg, E. L., & Butcher, E. C. (1989) · Science · doi:10.1126/science.2551036 · Cited by 1,089
Buxbaum, J. D., Liu, K.-N., Luo, Y., Slack, J. L., Stocking, K. L., Peschon, J. J., Johnson, R. S., Castner, B. J., Cerretti, D. P., & Black, R. A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.27765 · Cited by 952
Membrane-Type 1 Matrix Metalloproteinase Cleaves Cd44 and Promotes Cell Migration
Kajita, M., Itoh, Y., Chiba, T., Mori, H., Okada, A., Kinoh, H., & Seiki, M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.5.893 · Cited by 746
Garton, K. J., Gough, P. J., Blobel, C., Murphy, G., Greaves, D. R., Dempsey, P. J., & Raines, E. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106434200 · Cited by 653
Self-citationHooper, N. M., Karran, E. H., & Turner, A. J. (1997) · Biochemical Journal · doi:10.1042/bj3210265 · Cited by 613
Lévesque, J.-P., Takamatsu, Y., Nilsson, S. K., Haylock, D. N., & Simmons, P. J. (2001) · Blood · doi:10.1182/blood.v98.5.1289 · Cited by 486
Cited by
Sorted by citations
Edwards, D. R., Handsley, M. M., & Pennington, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,163
Lambert, D., Yarski, M., Warner, F. J., Thornhill, P., Parkin, E. T., Smith, A. I., Hooper, N. M., & Turner, A. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505111200 · Cited by 713
Cook‐Mills, J. M., Marchese, M. E., & Abdala‐Valencia, H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3522 · Cited by 597
Lü, X., Mu, E. W., Wei, Y., Riethdorf, S., Yang, Q., Yuan, M., Yan, J., Hua, Y., Tiede, B., Lu, X., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.11.002 · Cited by 515
Shedding light on ADAM metalloproteinases
Huovila, A. J., Turner, A. J., Pelto‐Huikko, M., Kärkkäinen, I., & Ortiz, R. M. (2005) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.05.006 · Cited by 448
Yousef, H., Czupalla, C. J., Lee, D., Chen, M. B., Burke, A. N., Zera, K. A., Zandstra, J., Berber, E., Lehallier, B., Mathur, V., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0440-4 · Cited by 442
Reiß, K., & Säftig, P. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.11.002 · Cited by 419
ADAM-17: the enzyme that does it all
Gooz, M. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409231003628015 · Cited by 377
Ectodomain shedding and ADAMs in development
Weber, S., & Säftig, P. (2012) · Development · doi:10.1242/dev.076398 · Cited by 259
Gough, P. J., Garton, K. J., Wille, P. T., Rychlewski, M., Dempsey, P. J., & Raines, E. W. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.6.3678 · Cited by 263
Self-citationPruessmeyer, J., & Ludwig, A. (2008) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2008.09.005 · Cited by 248
Matsuura, K., Honda, A., Nagai, T., Fukushima, N., Iwanaga, K., Tokunaga, M., Shimizu, T., Okano, T., Kasanuki, H., Hagiwara, N., et al. (2009) · Journal of Clinical Investigation · doi:10.1172/jci37456 · Cited by 234
L-selectin: mechanisms and physiological significance of ectodomain cleavage
Smalley, D. M., & Ley, K. F. (2005) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2005.tb00354.x · Cited by 232
Brownlee, I. A., Moore, C. S., Chatfield, M. D., Richardson, D. P., Ashby, P., Kuznesof, S. A., Jebb, S. A., & Seal, C. J. (2010) · British Journal Of Nutrition · doi:10.1017/s0007114510000644 · Cited by 231
Schlesinger, M., & Bendas, G. (2014) · International Journal of Cancer · doi:10.1002/ijc.28927 · Cited by 232
Bergmeier, W., Piffath, C. L., Cheng, G., Dole, V. S., Zhang, Y., von Andrian, U. H., & Wagner, D. D. (2004) · Circulation Research · doi:10.1161/01.res.0000143899.73453.11 · Cited by 227
VCAM-1 as a predictor biomarker in cardiovascular disease
Troncoso, M. F., Ortiz‐Quintero, J., Garrido‐Moreno, V., Sanhueza‐Olivares, F., Guerrero‐Moncayo, A., Chiong, M., Castro, P., Garcı́a, L., Gabrielli, L., Corbalan, R. L., et al. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2021.166170 · Cited by 233
Emerging roles for ectodomain shedding in the regulation of inflammatory responses
Garton, K. J., Gough, P. J., & Raines, E. W. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0106038 · Cited by 222
Self-citationThe role of ADAM-mediated shedding in vascular biology
Yildiz, D., Pruessmeyer, J., Groth, E., & Ludwig, A. (2011) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2011.09.003 · Cited by 222
Metalloproteinases Shed TREM-1 Ectodomain from Lipopolysaccharide-Stimulated Human Monocytes1
Gómez-Piña, V., Soares-Schanoski, A., Rodríguez-Rojas, A., del Fresno, C., García, F., Vallejo-Cremades, M. T., Fernández-Ruíz, I., Arnalich, F., Fuentes-Prior, P., & López-Collazo, E. (2007) · Journal of Immunology · doi:10.4049/jimmunol.179.6.4065 · Cited by 208
Molecular and Cellular Mechanisms of Ectodomain Shedding
Hayashida, K., Bartlett, A. H., Chen, Y., & Park, P. W. (2010) · The Anatomical Record · doi:10.1002/ar.20757 · Cited by 198
Moss, M. L., Sklair‐Tavron, L., & Nudelman, R. (2008) · Nature Clinical Practice Rheumatology · doi:10.1038/ncprheum0797 · Cited by 195
“Pumping iron”—how macrophages handle iron at the systemic, microenvironmental, and cellular levels
Nairz, M., Theurl, I., Swirski, F. K., & Weiss, G. (2017) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-017-1944-8 · Cited by 178
Hundhausen, C., Schulte, A., Schulz, B., Andrzejewski, M. G., Schwarz, N., von Hundelshausen, P., Winter, U., Paliga, K., Reiß, K., Säftig, P., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.12.8064 · Cited by 182
Tsakadze, N. L., Sithu, S. D., Sen, U., English, W., Murphy, G., & D’Souza, S. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m510797200 · Cited by 178
Koenen, R. R., Pruessmeyer, J., Soehnlein, O., Fraemohs, L., Zernecke, A., Schwarz, N., Reiß, K., Sarabi, A., Lindbom, L., Hackeng, T. M., et al. (2009) · Blood · doi:10.1182/blood-2008-04-152330 · Cited by 175
Deciphering the human platelet sheddome
Fong, K. P., Barry, C. G., Tran, A. N., Traxler, E. A., Wannemacher, K. M., Tang, H., Speicher, K. D., Blair, I. A., Speicher, D. W., Großer, T., et al. (2010) · Blood · doi:10.1182/blood-2010-05-283838 · Cited by 174
Transmembrane chemokines: Versatile ‘special agents’ in vascular inflammation
Weber, C., & Ludwig, A. (2007) · Thrombosis and Haemostasis · doi:10.1160/th07-01-0035 · Cited by 175
ADAM17 as a Therapeutic Target in Multiple Diseases
Arribas, J., & Esselens, C. W. (2009) · Current Pharmaceutical Design · doi:10.2174/138161209788682398 · Cited by 171
Yan, F., Liu, L., Dempsey, P. J., Tsai, Y.-H., Raines, E. W., Wilson, C. L., Cao, H., Cao, Z., Liu, L., & Polk, D. B. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.492397 · Cited by 174
Self-citationMechanisms of Soluble Cytokine Receptor Generation
Levine, S. J. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.9.5343 · Cited by 166
Fabre-Lafay, S., Garrido‐Urbani, S., Reymond, N., Gonçalvès, A., Dubreuil, P. C., & Lopez, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410943200 · Cited by 163
Dusso, A., & Tokumoto, M. (2011) · Kidney International · doi:10.1038/ki.2010.543 · Cited by 156
Luplerdlop, N., Missé, D., Bray, D. H., Deleuze, V., Gonzalez, J., Leardkamolkarn, V., Yssel, H., & Veas, F. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400814 · Cited by 154
The shedding activity of ADAM17 is sequestered in lipid rafts
Tellier, E., Canault, M., Rebsomen, L., Bonardo, B., Juhan-Vague, I., Nalbone, G., & Peiretti, F. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.08.027 · Cited by 155
ADAM-family metalloproteinases in lung inflammation: potential therapeutic targets
Yildiz, D., Uhlig, S., & Ludwig, A. (2014) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00294.2014 · Cited by 145
Wang, Y., & Sul, H. S. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02437-05 · Cited by 140
Sheets, S. M., Potempa, J., Travis, J. W., Casiano, C. A., & Fletcher, H. M. (2005) · Infection and Immunity · doi:10.1128/iai.73.3.1543-1552.2005 · Cited by 139
Reiß, K., Ludwig, A., & Säftig, P. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.02.009 · Cited by 136
Regulation of angiogenesis: apoptotic cues from the ECM
Cheresh, D. A., & Stupack, D. G. (2008) · Oncogene · doi:10.1038/onc.2008.304 · Cited by 140
Luplertlop, N., Missé, D., Bray, D. H., Deleuze, V., Gonzalez, J., Leardkamolkarn, V., Yssel, H., & Veas, F. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400868 · Cited by 134
Kenchappa, R. S., Tep, C., Korade, Ž., Urra, S., Bronfman, F. C., Yoon, S. O., & Carter, B. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.082834 · Cited by 126
Davis, G. E., Koh, W., & Stratman, A. N. (2007) · Birth Defects Research Part C Embryo Today Reviews · doi:10.1002/bdrc.20107 · Cited by 129
ADAM17 deficiency by mature neutrophils has differential effects on L-selectin shedding
Li, Y., Brazzell, J. L., Herrera, A. H., & Walcheck, B. K. (2006) · Blood · doi:10.1182/blood-2006-02-005827 · Cited by 121
SINGH, R., Mason, J. C., Lidington, E. C., Edwards, D. R., Nuttall, R. K., Khokha, R., Knäuper, V., MURPHY, G., & Gavrilović, J. (2005) · Cardiovascular Research · doi:10.1016/j.cardiores.2005.02.020 · Cited by 117
Matías-Román, S., Gálvez, B. G., Genís, L., Yáñez‐Mó, M., de la Rosa, G., Sánchez‐Mateos, P., Sánchez‐Madrid, F., & Arroyo, A. G. (2005) · Blood · doi:10.1182/blood-2004-06-2382 · Cited by 119
Qu, D., WANG, Y., Esmon, N. L., & Esmon, C. T. (2007) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2007.02347.x · Cited by 120
Yan, F., Cao, H., Chaturvedi, R., Krishna, U. S., Hobbs, S. S., Dempsey, P. J., Peek, R. M., Cover, T. L., Washington, M. K., Wilson, K. T., et al. (2009) · Gastroenterology · doi:10.1053/j.gastro.2008.12.059 · Cited by 111
Self-citationCanault, M., Leroyer, A. S., Peiretti, F., Lesèche, G., Tedgui, A., Bonardo, B., Alessi, M., Boulanger, C. M., & Nalbone, G. (2007) · American Journal Of Pathology · doi:10.2353/ajpath.2007.070021 · Cited by 111
Staphylococcus aureus protein A activates TACE through EGFR‐dependent signaling
Gómez, M. I., Seaghdha, M. O., & Prince, A. S. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601554 · Cited by 108
Sanderson, M. P., Erickson, S. N., Gough, P. J., Garton, K. J., Wille, P. T., Raines, E. W., Dunbar, A. J., & Dempsey, P. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408804200 · Cited by 111
Self-citationEvidence for a Role of ADAM17 (TACE) in the Regulation of Platelet Glycoprotein V
Rabie, T., Strehl, A., Ludwig, A., & Nieswandt, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500041200 · Cited by 106
Argast, G. M., Campbell, J. S., Brooling, J. T., & Fausto, N. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405703200 · Cited by 104
Endothelial Signaling by Ig-Like Cell Adhesion Molecules
van Buul, J. D., Kanters, E., & Hordijk, P. L. (2007) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.107.145821 · Cited by 101
Kalus, I., Bormann, U., Mzoughi, M., Schachner, M., & KLEENE, R. B. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03847.x · Cited by 96
Clipping, shedding and RIPping keep immunity on cue
Murphy, G., Murthy, A., & Khokha, R. (2008) · Trends in Immunology · doi:10.1016/j.it.2007.10.009 · Cited by 96
Chodavarapu, H., Grobe, N., Somineni, R. P., Salem, E., Madhu, M. N., & Elased, K. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062833 · Cited by 90
Warner, E. F., Zhang, Q., Raheem, S., O’Hagan, D., O'Connell, M. A., & Kay, C. D. (2016) · Journal of Nutrition · doi:10.3945/jn.115.217943 · Cited by 86
ADAM17 at the interface between inflammation and autoimmunity
Lisi, S., D’Amore, M., & Sisto, M. (2014) · Immunology Letters · doi:10.1016/j.imlet.2014.08.008 · Cited by 88
ADAM17 upregulation in human renal disease: a role in modulating TGF-α availability?
Melenhorst, W. B. W. H., Visser, L., Timmer, A., van den Heuvel, M. C., Stegeman, C. A., & van Goor, H. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.90610.2008 · Cited by 84
Sackstein, R. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2009.00792.x · Cited by 84
Owen, C. A. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.01.020 · Cited by 84
Integrin α5β1 and ADAM-17 Interact in Vitro and Co-localize in Migrating HeLa Cells
Bax, D. V., Messent, A., Tart, J., Hoang, M. V., Kott, J., Maciewicz, R. A., & Humphries, M. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400180200 · Cited by 81
ADAM-Integrin Interactions: Potential Integrin Regulated Ectodomain Shedding Activity
Bridges, L. C., & Bowditch, R. D. (2005) · Current Pharmaceutical Design · doi:10.2174/1381612053381747 · Cited by 81
Düsterhöft, S., Hoebel, K., Oldefest, M., Lokau, J., Waetzig, G. H., Chalaris, A., Garbers, C., Scheller, J., Rose‐John, S., Lorenzen, I., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.557322 · Cited by 75
Guo, Q., Furuta, K., Islam, S., Caporarello, N., Kostallari, E., Dielis, K., Tschumperlin, D. J., Hirsova, P., & Ibrahim, S. H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.983255 · Cited by 73
Adam17 Deficiency Promotes Atherosclerosis by Enhanced TNFR2 Signaling in Mice
Nicolaou, A., Zhao, Z., Northoff, B. H., Sass, K., Herbst, A., Kohlmaier, A., Chalaris, A., Wolfrum, C., Weber, C., Steffens, S., et al. (2016) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.116.308682 · Cited by 69
Vitamin D inhibition of TACE and prevention of renal osteodystrophy and cardiovascular mortality
Dusso, A., Arcidiacono, M. V., Yang, J., & Tokumoto, M. (2010) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2010.03.064 · Cited by 68
TCR Stimulation Drives Cleavage and Shedding of the ITIM Receptor CD31
Fornasa, G., Groyer, É., Clément, M., Dimitrov, J. D., Compain, C., Gaston, A., Varthaman, A., Khallou‐Laschet, J., Newman, D. K., Graff‐Dubois, S., et al. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0902219 · Cited by 67
Mishra, H. K., Ma, J., & Walcheck, B. K. (2017) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2017.00138 · Cited by 66
Mishra, A., Guo, Y., Zhang, L., More, S., Weng, T., Chintagari, N. R., Huang, C., Liang, Y., Pushparaj, S., Gou, D., et al. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501041 · Cited by 65
Tumour necrosis factor‐α stimulates expression of TNF‐α converting enzyme in endothelial cells
Bzowska, M., Jura, N., Lassak, A., Black, R. A., & Bereta, J. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04215.x · Cited by 65
Li, H., Peng, W., Jian, W., Li, Y., Li, Q., Li, W., & Xu, Y. (2012) · Cardiovascular Diabetology · doi:10.1186/1475-2840-11-65 · Cited by 62
Parodis, I., Gokaraju, S., Zickert, A., Vanarsa, K., Zhang, T., Habazi, D., Botto, J., Alves, C. S., Giannopoulos, P., Larsson, A. O., et al. (2019) · Rheumatology · doi:10.1093/rheumatology/kez528 · Cited by 61
The secretome mouse provides a genetic platform to delineate tissue-specific in vivo secretion
Liu, J., Jang, J. Y., Pirooznia, M., Liu, S., & Finkel, T. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2005134118 · Cited by 62
ADAM17 activity during human neutrophil activation and apoptosis
Walcheck, B. K., Herrera, A. H., Hill, C. S., Mattila, P. E., Whitney, A. R., & DeLeo, F. R. (2006) · European Journal of Immunology · doi:10.1002/eji.200535257 · Cited by 61
Contribution of ADAM17 and related ADAMs in cardiovascular diseases
Kawai, T., Elliott, K. J., Scalia, R. G., & Eguchi, S. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03779-w · Cited by 62
Tissue Inhibitor of Metalloproteinase-3 (TIMP-3) Regulates Hematopoiesis and Bone Formation In Vivo
Shen, Y., Winkler, I. G., Barbier, V., Sims, N. A., Hendy, J., & Lévesque, J.-P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013086 · Cited by 61
Taking the stock of granule cargo: Platelet releasate proteomics
Pagel, O., Walter, E., Jurk, K., & Zahedi, R. P. (2016) · Platelets · doi:10.1080/09537104.2016.1254762 · Cited by 66
Arnold, P., Boll, I., Rothaug, M., Schumacher, N., Schmidt, F., Wichert, R., Schneppenheim, J., Lokau, J., Pickhinke, U., Koudelka, T., et al. (2017) · Scientific Reports · doi:10.1038/srep44053 · Cited by 59
Vanderstocken, G., Bondue, B., Horckmans, M., Pietrantonio, L. D., Robaye, B., Boeynaems, J.-M., & Communi, D. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.0903908 · Cited by 59
Novak, U. (2003) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2003.10.006 · Cited by 58
ADAM-17 regulates endothelial cell morphology, proliferation, and in vitro angiogenesis
Göőz, P., Gooz, M. B., Baldys, A., & Hoffman, S. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.013 · Cited by 58
VCAM-1 Target in Non-Invasive Imaging for the Detection of Atherosclerotic Plaques
Thayse, K., Kindt, N., Laurent, S., & CARLIER, S. G. (2020) · Biology · doi:10.3390/biology9110368 · Cited by 59
Eosinophils Adhere to Vascular Cell Adhesion Molecule-1 via Podosomes
Johansson, M. W., Lye‐Barthel, M., Barthel, S. R., Duffy, A., Annis, D. S., & Mosher, D. F. (2004) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2004-0099oc · Cited by 57
The Balance Between Metalloproteinases and TIMPs
Masciantonio, M. G., Lee, C. K. S., Arpino, V., Mehta, S., & Gill, S. E. (2017) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2017.01.001 · Cited by 56
ADAM17 mediates Nox4 expression and NADPH oxidase activity in the kidney cortex of OVE26 mice
Ford, B. M., Eid, A. A., Gooz, M. B., Barnes, J. L., Gorin, Y. C., & Abboud, H. E. (2013) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00522.2012 · Cited by 54
van der Vorst, E. P. C., Keijbeck, A. A., de Winther, M. P. J., & Donners, M. M. P. C. (2012) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2012.04.023 · Cited by 52
Deciphering the Role of the ADAM17-Dependent Secretome in Cell Signaling
Kawahara, R., Lima, R. N., Domingues, R. R., Pauletti, B. A., Meirelles, G. V., de Assis, M. A., Figueira, A. C. M., & Leme, A. F. P. (2014) · Journal of Proteome Research · doi:10.1021/pr401224u · Cited by 52
Choi, J.-Y., Park, H.-J., Lee, Y.-J., Byun, J., Youn, Y.-S., Choi, J. H., Woo, S., & Kang, J. L. (2012) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.199778 · Cited by 49
Adu‐Amankwaah, J., Adzika, G. K., Adekunle, A. O., Noah, M. L. N., Mprah, R., Bushi, A., Akhter, N., Huang, F., Xu, Y., Adzraku, S. Y., et al. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.732952 · Cited by 53
Hernandez, I. M., Moreno, J. L., Zandueta, C., Montuenga, L. M., & Lecanda, F. (2010) · Oncogene · doi:10.1038/onc.2010.130 · Cited by 50
Tang, J., Kozaki, K., Farr, A. G., Martin, P. J., Lindahl, P., Betsholtz, C., & Raines, E. W. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62061-5 · Cited by 49
Self-citationLi, X., & Fan, H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m401690200 · Cited by 48
A panel of urinary proteins predicts active lupus nephritis and response to rituximab treatment
Davies, J. C., Carlsson, E., Midgley, A., Smith, E. M. D., Bruce, I. N., Beresford, M. W., Hedrich, C. M., & Consortia, T. B.-B. A. M. M. (2020) · Lara D. Veeken · doi:10.1093/rheumatology/keaa851 · Cited by 47
Role of ADAM8 in experimental asthma
Matsuno, O., Miyazaki, E., Nureki, S.-I., UENO, T., Kumamoto, T., & HIGUCHI, Y. (2005) · Immunology Letters · doi:10.1016/j.imlet.2005.07.006 · Cited by 47
Scarisbrick, I. A. (2007) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-73677-6_6 · Cited by 49
SEVERE SICKLE CELL ANEMIA IS ASSOCIATED WITH INCREASED PLASMA LEVELS OF TNF-R1 AND VCAM-1
Dworkis, D., Klings, E., Solovieff, N., Li, G.-H., Milton, J., Hartley, S., Melista, E., Parente, J., Sebastiani, P., Steinberg, M. H., et al. (2011) · American journal of hematology/oncology · doi:10.1002/ajh.21928 · Cited by 37
Circulating ADAM17 Level Reflects Disease Activity in Proteinase-3 ANCA-Associated Vasculitis
Bertram, A., Lovric, S., Engel, A., Beese, M., Wyss, K., Hertel, B., Park, J.-K., Becker, J. U., Kegel, J., Haller, H. G., et al. (2015) · Journal of the American Society of Nephrology · doi:10.1681/asn.2014050477 · Cited by 46
Immunomodulatory role of metalloproteinase ADAM17 in tumor development
Wang, K., Xuan, Z., Liu, X., Zheng, M., Yang, C., & Wang, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1059376 · Cited by 45
Metadata
- Authors
- Garton, K. J., Gough, P. J., Philalay, J., Wille, P. T., Blobel, C. P., Whitehead, R. H., Dempsey, P. J., & Raines, E. W.
- Affiliations
- University of Washington (US)
- Memorial Sloan Kettering Cancer Center (US)
- Vanderbilt University (US)
- Corresponding author
- Raines, Elaine W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-09
- Volume
- 278
- Issue
- 39
- Pages
- 37459-37464
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1963691526
- Cited by
- 282
- References
- 27
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 13 · 2023: 9 · 2022: 14 · 2021: 18 · 2020: 15 · 2019: 8 · 2018: 12 · 2017: 10 · 2016: 12 · 2015: 5 · 2014: 9 · 2013: 7 · 2012: 10
- FWCI
- 8.92
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- Amgen
- Fondation pour la Recherche Médicale
- National Institutes of Health (HL 18645)
- National Heart, Lung, and Blood Institute (HL-18645, R01HL067267, HL-67267, P01HL018645)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-59778, R01DK059778, DK-63363, R01DK063363)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Keywords
- VCAM-1, ADAM17, transarterial chemoembolization, phorbol myristate acetate, soluble adhesion molecules, endothelial cells, E-selectin, CD31, ICAM-1
- MeSH terms
- ADAM17 Protein, Animals, Cell Line, Female, Metalloendopeptidases, Tetradecanoylphorbol Acetate, Vascular Cell Adhesion Molecule-1, Metalloproteases, Mice, ADAM Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
