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CD151 Accelerates Breast Cancer by Regulating α6 Integrin Function, Signaling, and Molecular Organization
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Abstract
CD151, a master regulator of laminin-binding integrins (alpha(6)beta(4), alpha(6)beta(1), and alpha(3)beta(1)), assembles these integrins into complexes called tetraspanin-enriched microdomains. CD151 protein expression is elevated in 31% of human breast cancers and is even more elevated in high-grade (40%) and estrogen receptor-negative (45%) subtypes. The latter includes triple-negative (estrogen receptor, progesterone receptor, and HER2 negative) basal-like tumors. CD151 ablation markedly reduced basal-like mammary cell migration, invasion, spreading, and signaling (through FAK, Rac1, and lck) while disrupting epidermal growth factor receptor (EGFR)-alpha(6) integrin collaboration. Underlying these defects, CD151 ablation redistributed alpha(6)beta(4) integrins subcellularly and severed molecular links between integrins and tetraspanin-enriched microdomains. In a prototypical basal-like mammary tumor line, CD151 ablation notably delayed tumor progression in ectopic and orthotopic xenograft models. These results (a) establish that CD151-alpha(6) integrin complexes play a functional role in basal-like mammary tumor progression; (b) emphasize that alpha(6) integrins function via CD151 linkage in the context of tetraspanin-enriched microdomains; and (c) point to potential relevance of CD151 as a high-priority therapeutic target, with relative selectivity (compared with laminin-binding integrins) for pathologic rather than normal physiology.
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“ITGB1 and CD151 are known to be pro-tumorigenic by enhancing cell migration and stromal invasion (Reuter et al., 2009, White et al., 2004, Yang et al., 2008, Zijlstra et al., 2008).”
From Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma (2020) · cites this paper as Yang et al., 2008
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Molecular portraits of human breast tumours
Perou, C., Sørlie, T., Eisen, M., van de Rijn, M., Jeffrey, S., Rees, C. A., Pollack, J., Ross, D., Johnsen, H., Akslen, L., et al. (2000) · Nature · doi:10.1038/35021093 · Cited by 16,551
A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes
Neve, R. M., Chin, K., Fridlyand, J., Yeh, J., Baehner, F. L., Fevr, T., Clark, L., Bayani, N., Coppé, J., Tong, F. K., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.10.008 · Cited by 3,224
Focal adhesion kinase: in command and control of cell motility
Mitra, S. K., Hanson, D. A., & Schlaepfer, D. D. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1549 · Cited by 2,657
Tetraspanin functions and associated microdomains
Hemler, M. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1736 · Cited by 1,355 · cited 1×
“CD151 may link laminin-binding integrins to other proteins within the plasma membrane (38, 39).”
BackgroundSelf-citationHemler, M. E. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111301.153609 · Cited by 831
Self-citationActivation of Phosphoinositide 3-OH Kinase by the α6β4 Integrin Promotes Carcinoma Invasion
Shaw, L. M., Rabinovitz, I., Wang, H. H.-F., Toker, A., & Mercurio, A. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80486-9 · Cited by 613
Complexes of tetraspanins with integrins: more than meets the eye
Berditchevski, F. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.23.4143 · Cited by 597
Genetic programs of epithelial cell plasticity directed by transforming growth factor-β
Zavadil, J., Bitzer, M., Liang, D., Yang, Y.-C., Massimi, A. B., Kneitz, S., Piek, E., & Böttinger, E. P. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111614398 · Cited by 534
Control of motile and invasive cell phenotypes by focal adhesion kinase
Schlaepfer, D. D., Mitra, S. K., & Ilić, D. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.04.008 · Cited by 475
β4 Integrin Amplifies ErbB2 Signaling to Promote Mammary Tumorigenesis
Guo, W., Pylayeva, Y., Pepe, A., Yoshioka, T., Muller, W. J., Inghirami, G., & Giancotti, F. G. (2006) · Cell · doi:10.1016/j.cell.2006.05.047 · Cited by 466
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Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma
Ji, A. L., Rubin, A. J., Thrane, K., Jiang, S., Reynolds, D. L., Meyers, R. M., Guo, M. G., George, B. M., Mollbrink, A., Bergenstråhle, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.039 · Cited by 1,117
“ITGB1 andCD151 are known to be pro-tumorigenic by enhancing cell migration and stromal invasion (Reuter et al., 2009; White et al., 2004; Yang et al., 2008; Zijlstra et al., 2008).”
BackgroundCharrin, S., Jouannet, S., Boucheix, C., & Rubinstein, E. (2014) · Journal of Cell Science · doi:10.1242/jcs.154906 · Cited by 481
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Charrin, S., Naour, F. L., Silvie, O., Milhiet, P., Boucheix, C., & Rubinstein, E. (2009) · Biochemical Journal · doi:10.1042/bj20082422 · Cited by 440
Tetraspanin proteins promote multiple cancer stages
Hemler, M. E. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3640 · Cited by 403
Self-citationTargeting of tetraspanin proteins — potential benefits and strategies
Hemler, M. E. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2659 · Cited by 345
Self-citationSignal co-operation between integrins and other receptor systems
Streuli, C. H., & Akhtar, N. (2009) · Biochemical Journal · doi:10.1042/bj20081948 · Cited by 317
Shema, E., Tirosh, I., Aylon, Y., Huang, J. L., Ye, C., Moskovits, N. B.-C., Raver-Shapira, N., Minsky, N., Pirngruber, J., Tarcic, G., et al. (2008) · Genes & Development · doi:10.1101/gad.1703008 · Cited by 290
Spoden, G. A., Freitag, K., Husmann, M., Böller, K., Sapp, M. J., Lambert, C., & Florin, L. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003313 · Cited by 238
Surviladze, Z., Sterk, R. T., DeHaro, S. A., & Ozbun, M. A. (2012) · Journal of Virology · doi:10.1128/jvi.02319-12 · Cited by 225
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Stipp, C. S. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001355 · Cited by 165
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Yousefi, H., Vatanmakanian, M., Mahdiannasser, M., Mashouri, L., Alahari, N. V., Monjezi, M. R., Ilbeigi, S., & Alahari, S. K. (2021) · Oncogene · doi:10.1038/s41388-020-01588-2 · Cited by 146
Tran, M., Freitas, T. C., Cooper, L. T., Gaze, S. T., Gatton, M. L., Jones, M., Lovas, E. M., Pearce, E. J., & Loukas, A. C. (2010) · QUT ePrints (Queensland University of Technology) · Cited by 138
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Perentes, J. Y., Kirkpatrick, N. D., Nagano, S., Smith, E. Y., Shaver, C. M., Sgroi, D. C., Garkavtsev, I., Munn, L. L., Jain, R. K., & Boucher, Y. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-4376 · Cited by 123
Zhu, G., Huang, C., Qiu, Z., Liu, J., Zhang, Z., Zhao, N., Feng, Z.-Z., & Lv, X.-H. (2010) · Digestive Diseases and Sciences · doi:10.1007/s10620-010-1416-x · Cited by 108
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Rubinstein, E. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390501 · Cited by 103
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Bassani, S., & Cingolani, L. A. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.01.020 · Cited by 102
Shen, B., Vardy, K., Hughes, P., Tasdogan, A., Zhao, Z., Yue, R., Crane, G. M., & Morrison, S. J. (2019) · eLife · doi:10.7554/elife.42274 · Cited by 98
Controlling cell surface dynamics and signaling: How CD82/KAI1 suppresses metastasis
Miranti, C. K. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.08.023 · Cited by 100
Detchokul, S., Williams, E. D., Parker, M. W., & Frauman, A. (2013) · British Journal of Pharmacology · doi:10.1111/bph.12260 · Cited by 95
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Wang, H.-X., Li, Q., Sharma, C., Knoblich, K., & Hemler, M. E. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390547 · Cited by 95
Self-citationMitchell, K., Svenson, K. B., Longmate, W. M., Gkirtzimanaki, K., Sądej, R., Wang, X., Zhao, J., Eliopoulos, A. G., Berditchevski, F., & DiPersio, C. M. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4283 · Cited by 97
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Han, Z., Yang, Z., Chi, Y., Zhang, L., Wang, Y., Ji, Y., Wang, J., Zhao, H., & Han, Z. (2013) · Cellular Physiology and Biochemistry · doi:10.1159/000350100 · Cited by 90
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Sądej, R., Romańska, H., Baldwin, G., Gkirtzimanaki, K., Novitskaya, V., Filer, A. D., Krcova, Z., Kusińska, R., Ehrmann, J., Buckley, C. D., et al. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0574 · Cited by 89
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Romańska, H., & Berditchevski, F. (2010) · The Journal of Pathology · doi:10.1002/path.2779 · Cited by 89
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Deng, X., Li, Q., Hoff, J. J., Novak, M., Yang, H. L., Jin, H., Erfani, S., Sharma, C., Zhou, P., Rabinovitz, I., et al. (2012) · Neoplasia · doi:10.1593/neo.12922 · Cited by 86
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Lafleur, M. A., Xu, D., & Hemler, M. E. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-11-1149 · Cited by 85
Self-citationClinical significance of CD151 overexpression in subtypes of invasive breast cancer
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Johnson, J. L., Winterwood, N. E., DeMali, K. A., & Stipp, C. S. (2009) · Journal of Cell Science · doi:10.1242/jcs.045997 · Cited by 77
Xu, B., Lefringhouse, J., Liu, Z., Piecoro, D. W., Baldwin, L. A., Ou, C., Chen, L., Napier, D. L., Chaiswing, L., Brewer, L. D., et al. (2017) · Oncogenesis · doi:10.1038/oncsis.2016.86 · Cited by 76
Self-citationIntegrin-mediated regulation of epidermal wound functions
DiPersio, C. M., Zheng, R., Kenney, J., & Water, L. V. D. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2446-2 · Cited by 76
Amin, M. K. B. A., Shimizu, A., Zankov, D. P., Sato, A., Kurita, S., Ito, M., Maeda, T., Yoshida, T., Sakaue, T., Higashiyama, S., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0286-0 · Cited by 71
Wang, Y., Shenouda, S. K., Baranwal, S., Rathinam, R., Jain, P., Bao, L., Hazari, S., Dash, S., & Alahari, S. K. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-84 · Cited by 75
Zhou, P., Erfani, S., Liu, Z., Jia, C., Chen, Y., Xu, B., Deng, X., Alfaro, J., Chen, L., Napier, D. L., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4896 · Cited by 72
Self-citationTetraspanin CD151 plays a key role in skin squamous cell carcinoma
Li, Q., Yang, X. H., Xu, F., Sharma, C., Wang, H.-X., Knoblich, K., Rabinovitz, I., Granter, S. R., & Hemler, M. E. (2012) · Oncogene · doi:10.1038/onc.2012.205 · Cited by 73
Self-citationLi, S., Li, X., Yang, S., Li, Z., Li, Z., Yao, P., Wang, Q., Wang, Q., Shen, P., Ji, J., et al. (2021) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2021.100121 · Cited by 70
Regulation of CD151 by Hypoxia Controls Cell Adhesion and Metastasis in Colorectal Cancer
Chien, C., Lin, S., Lai, Y.-Y., Lin, B.-W., Lin, S.-C., Lee, J., & Tsai, S. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1651 · Cited by 72
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Jiang, X., Zhang, J., & Huang, Y. (2015) · Cell Adhesion & Migration · doi:10.1080/19336918.2015.1005465 · Cited by 71
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Self-citationDiminished metastasis in tetraspanin CD151–knockout mice
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Huang, X., Ke, A., Shi, G., Ding, Z., Devbhandari, R. P., Gu, F., Li, Q., Dai, Z., Zhou, J., & Fan, J. (2010) · Cancer · doi:10.1002/cncr.25485 · Cited by 57
Beyond adhesion: emerging roles for integrins in control of the tumor microenvironment
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Palmer, T. D., Martínez, C. H., Vásquez, C., Hebron, K. E., Jones‐Paris, C. R., Arnold, S. A., Chan, S. M., Chalasani, V., Gomez-Lemus, J. A., Williams, A. K., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0275 · Cited by 56
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Franco, M., Muratori, C., Corso, S., Tenaglia, E., Bertotti, A., Capparuccia, L., Trusolino, L., Comoglio, P. M., & Tamagnone, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145417 · Cited by 54
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Zhang, Y., Cheng, K., Xu, B., Shi, J., Qiang, J., Shi, S., Yi, Y., Li, H., Jin, T., Guo, R., et al. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00652 · Cited by 53
Self-citationZevian, S., Winterwood, N. E., & Stipp, C. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173583 · Cited by 53
Fujita, M., Ieguchi, K., Davari, P., Yamaji, S., Taniguchi, Y., Sekiguchi, K., Takada, Y. K., & Takada, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.304170 · Cited by 52
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Self-citationNovitskaya, V., Romańska, H., Dawoud, M., Jones, J. L., & Berditchevski, F. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4330 · Cited by 47
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Dutta, U., & Shaw, L. M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-2125 · Cited by 44
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Suzuki, S., Miyazaki, T., Tanaka, N., Sakai, M., Sano, A., Inose, T., Sohda, M., Nakajima, M., Kato, H., & Kuwano, H. (2010) · Annals of Surgical Oncology · doi:10.1245/s10434-010-1387-3 · Cited by 43
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Devbhandari, R. P., Shi, G., Ke, A., Wu, F., Huang, X., Wang, X., Shi, Y., Ding, Z., Xu, Y., Dai, Z., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024901 · Cited by 39
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Huang, R., Li, J., Pan, F., Zhang, B., & Yao, Y. (2020) · PubMed Central · Cited by 39
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Scholz, C. J., Jacob, C., Buttenschøn, H. N., Kittel‐Schneider, S., Boreatti‐Hümmer, A., Zimmer, M., Walter, U., Lesch, K., Mors, O. N., Kneitz, S., et al. (2010) · American Journal of Medical Genetics Part B Neuropsychiatric Genetics · doi:10.1002/ajmg.b.31057 · Cited by 36
CD151 expression can predict cancer progression in clear cell renal cell carcinoma
Yoo, S. H., Lee, K., Chae, J. Y., & Moon, K. C. (2011) · Histopathology · doi:10.1111/j.1365-2559.2011.03752.x · Cited by 33
TSPAN1, a novel tetraspanin member highly involved in carcinogenesis and chemoresistance
Garcia‐Mayea, Y., Mir, C., Carballo-Perich, L., Sánchez-García, A., Bataller, M., & LLeonart, M. E. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188674 · Cited by 32
Zhou, Z., Yang, Z., Zhou, L., Yang, M., & He, S. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00995-8 · Cited by 32
Tetraspanin 1 promotes invasiveness of cervical cancer cells
Hölters, S., Anacker, J., Jansen, L., Beer‐Grondke, K., Dürst, M., & Rubio, I. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1980 · Cited by 30
Nankivell, P., Williams, H., McConkey, C., Webster, K., High, A. S., Maclennan, K. A., Şengüven, B., Rabbitts, P. H., & Mehanna, H. M. (2013) · British Journal of Cancer · doi:10.1038/bjc.2013.600 · Cited by 29
Malla, R. R., Gopinath, S., Alapati, K., Gorantla, B., Gondi, C. S., & Rao, J. S. (2012) · Molecular Carcinogenesis · doi:10.1002/mc.21915 · Cited by 29
RetractedThe role of exosomal tetraspanins and proteases in tumor progression
Yunusova, N. V., Tugutova, E. A., TAMKOVICH, S. N., & Кондакова, И. В. (2018) · Biomeditsinskaya Khimiya · doi:10.18097/pbmc20186402123 · Cited by 27
Erfani, S. F., Hua, H., Pan, Y.-Y., Zhou, B., & Yang, X.-W. H. (2021) · Cancers · doi:10.3390/cancers13092005 · Cited by 20
Self-citationReplication Study Confirms Link between TSPAN18 Mutation and Schizophrenia in Han Chinese
Yuan, J., Jin, C., Qin, H.-D., Wang, J., Sha, W., Wang, M., Zhang, Y., Zhang, F., Li, J., Li, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058785 · Cited by 24
Kong, T., Xu, D., Yu, W., Takakura, A., Boucher, I., Tran, M. T., Kreidberg, J. A., Shah, J. V., Zhou, J., & Denker, B. M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-03-0220 · Cited by 24
Ke, A., Zhang, P.-F., Shen, Y., Gao, P., Dong, Z., Zhang, C., Cai, J.-B., Huang, X., Wu, C., Zhang, L., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.6833 · Cited by 24
Regulation of Glioblastoma Tumor-Propagating Cells by the Integrin Partner Tetraspanin CD151
Tilghman, J. I., Schiapparelli, P. V., Lal, B., Ying, M., Quiñones‐Hinojosa, A., Xia, S., & Laterra, J. (2016) · Neoplasia · doi:10.1016/j.neo.2016.02.003 · Cited by 24
Wong, A. H., & Tran, T. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00064 · Cited by 24
Romańska, H., Potemski, P., Collins, S. I., Williams, H., Parmar, S., & Berditchevski, F. (2012) · Oral Oncology · doi:10.1016/j.oraloncology.2012.09.013 · Cited by 23
Effects of β4 integrin expression on microRNA patterns in breast cancer
Gerson, K. D., Maddula, V. S. R. K., Seligmann, B. E., Shearstone, J. R., Khan, A. A., & Mercurio, A. M. (2012) · Biology Open · doi:10.1242/bio.20121628 · Cited by 23
Malla, R. R., Marni, R., & Chakraborty, A. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188898 · Cited by 22
Metadata
- Authors
- Yang, X. H., Richardson, A. L., Torres-Arzayus, M. I., Zhou, P., Sharma, C., Kazarov, A. R., Andzelm, M. M., Strominger, J. L., Brown, M., & Hemler, M. E.
- Affiliations
- Harvard University (US)
- Brigham and Women's Hospital (US)
- 2Medical Oncology, and
- ORCID
- Venue
- Cancer Research
- Published
- 2008-05-01
- Volume
- 68
- Issue
- 9
- Pages
- 3204-3213
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- PMC
- PMC4764302
- OpenAlex
- W2102040455
- Cited by
- 183
- References
- 53
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 13 · 2020: 8 · 2019: 7 · 2018: 7 · 2017: 9 · 2016: 8 · 2015: 14 · 2014: 7 · 2013: 21 · 2012: 22
- FWCI
- 11.91
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Breast Cancer Research Foundation
- National Institutes of Health
- National Cancer Institute (CA-42368, R01CA042368)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Keywords
- CD151, CD49f, breast cancer, basal-like breast cancer, triple-negative breast cancer, tetraspanin-enriched microdomains, laminin-binding integrins, integrin signaling, tumor progression, EGFR, focal adhesion kinase, Rac1, Lck, tumor cell migration and invasion, therapeutic target
- MeSH terms
- Animals, Breast Neoplasms, Cell Adhesion, Cell Movement, Epidermal Growth Factor, Humans, Mice, Nude, Neoplasm Invasiveness, Protein Binding, Tissue Distribution, Transplantation, Heterologous, Tumor Cells, Cultured, Signal Transduction, Antigens, CD, Gene Expression Regulation, Neoplastic, Disease Progression, Integrin alpha6, Mammary Glands, Human, Mice, Tetraspanin 24
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