The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Clinical, Cellular, and Molecular Aspects of Cancer Invasion
Abstract
Invasion causes cancer malignancy. We review recent data about cellular and molecular mechanisms of invasion, focusing on cross-talk between the invaders and the host. Cancer disturbs these cellular activities that maintain multicellular organisms, namely, growth, differentiation, apoptosis, and tissue integrity. Multiple alterations in the genome of cancer cells underlie tumor development. These genetic alterations occur in varying orders; many of them concomitantly influence invasion as well as the other cancer-related cellular activities. Examples discussed are genes encoding elements of the cadherin/catenin complex, the nonreceptor tyrosine kinase Src, the receptor tyrosine kinases c-Met and FGFR, the small GTPase Ras, and the dual phosphatase PTEN. In microorganisms, invasion genes belong to the class of virulence genes. There are numerous clinical and experimental observations showing that invasion results from the cross-talk between cancer cells and host cells, comprising myofibroblasts, endothelial cells, and leukocytes, all of which are themselves invasive. In bone metastases, host osteoclasts serve as targets for therapy. The molecular analysis of invasion-associated cellular activities, namely, homotypic and heterotypic cell-cell adhesion, cell-matrix interactions and ectopic survival, migration, and proteolysis, reveal branching signal transduction pathways with extensive networks between individual pathways. Cellular responses to invasion-stimulatory molecules such as scatter factor, chemokines, leptin, trefoil factors, and bile acids or inhibitory factors such as platelet activating factor and thrombin depend on activation of trimeric G proteins, phosphoinositide 3-kinase, and the Rac and Rho family of small GTPases. The role of proteolysis in invasion is not limited to breakdown of extracellular matrix but also causes cleavage of proinvasive fragments from cell surface glycoproteins.
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.
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
Angiogenesis in cancer, vascular, rheumatoid and other disease
Folkman, J. (1995) · Nature Medicine · doi:10.1038/nm0195-27 · Cited by 7,627
New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108
Leptin and the regulation of body weight in mammals
Friedman, J. M., & Halaas, J. L. (1998) · Nature · doi:10.1038/27376 · Cited by 5,405
Li, J., Yen, C., Liaw, D., Podsypanina, K., Bose, S., Wang, S. I., Puc, J., Miliaresis, C., Rodgers, L., McCombie, R., et al. (1997) · Science · doi:10.1126/science.275.5308.1943 · Cited by 4,785
Tumors: Wounds That Do Not Heal
Flier, J. S., Underhill, L. H., & Dvorak, H. F. (1986) · New England Journal of Medicine · doi:10.1056/nejm198612253152606 · Cited by 4,391
Giancotti, F. G., & Ruoslahti, E. (1999) · Science · doi:10.1126/science.285.5430.1028 · Cited by 3,869
Blume-Jensen, P., & Hunter, T. (2001) · Nature · doi:10.1038/35077225 · Cited by 3,738
Polakis, P. (2000) · Genes & Development · doi:10.1101/gad.14.15.1837 · Cited by 3,183
Functional interaction of β-catenin with the transcription factor LEF-1
Behrens, J., von Kries, J. P., Kühl, M., Bruhn, L., Wedlich, D., Grosschedl, R., & Birchmeier, W. (1996) · Nature · doi:10.1038/382638a0 · Cited by 2,912
Vleminckx, K., Vakaet, L., Mareel, M., Fiers, W., & Van Roy, F. (1991) · Cell · doi:10.1016/0092-8674(91)90143-m · Cited by 1,656
Self-citation
Cited by
Role of tissue stroma in cancer cell invasion
De Wever, O., & Mareel, M. (2003) · The Journal of Pathology · doi:10.1002/path.1398 · Cited by 1,042
Self-citationActin and Actin-Binding Proteins
Pollard, T. D. (2016) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018226 · Cited by 912
The role of disturbed pH dynamics and the Na+/H+ exchanger in metastasis
Cardone, R. A., Casavola, V., & Reshkin, S. J. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1713 · Cited by 897
Orai1 and STIM1 Are Critical for Breast Tumor Cell Migration and Metastasis
Yang, S., Zhang, J. J., & Huang, X.-Y. (2009) · Cancer Cell · doi:10.1016/j.ccr.2008.12.019 · Cited by 742
Matrix metalloproteinases in cancer: from new functions to improved inhibition strategies
Folgueras, A. R., Pendas, A. M., Sanchez, L. M., & Lopez-Otin, C. (2004) · The International Journal of Developmental Biology · doi:10.1387/ijdb.041811af · Cited by 590
Lefranc, F., Brotchi, J., & Kiss, R. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.03.089 · Cited by 526
TGF-β – an excellent servant but a bad master
Kubiczkova, L., Sedlarikova, L., Hajek, R., & Sevcikova, S. (2012) · Journal of Translational Medicine · doi:10.1186/1479-5876-10-183 · Cited by 511
p53 controls cancer cell invasion by inducing the MDM2-mediated degradation of Slug
Wang, S.-P., Wang, W.-L., Chang, Y.-L., Wu, C.-T., Chao, Y.-C., Kao, S.-H., Yuan, A., Lin, C.-W., Yang, S.-C., Chan, W.-K., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1875 · Cited by 493
Lilien, J., & Balsamo, J. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.08.009 · Cited by 465
Derycke, L. D. M., & Bracke, M. E. (2004) · The International Journal of Developmental Biology · doi:10.1387/ijdb.041793ld · Cited by 408
On the dual roles and polarized phenotypes of neutrophils in tumor development and progression
Piccard, H., Muschel, R. J., & Opdenakker, G. (2012) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2011.06.004 · Cited by 373
A continuum approach to modelling cell–cell adhesion
Armstrong, N. J., Painter, K. J., & Sherratt, J. A. (2006) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2006.05.030 · Cited by 355
Breast Cancer Metastasis to Bone: Mechanisms of Osteolysis and Implications for Therapy
Kozlow, W., & Guise, T. A. (2005) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-005-5399-8 · Cited by 337
Ets proteins in biological control and cancer
Hsu, T., Trojanowska, M., & Watson, D. K. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20012 · Cited by 287
Amatangelo, M. D., Bassi, D. E., Klein-Szanto, A. J. P., & Cukierman, E. (2005) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)62991-4 · Cited by 248
Cannito, S., Novo, E., di Bonzo, L. V., Busletta, C., Colombatto, S., & Parola, M. (2010) · Antioxidants & Redox Signaling · doi:10.1089/ars.2009.2737 · Cited by 239
In vitro model of tumor cell extravasation
Jeon, J. S., Zervantonakis, I. K., Chung, S., Kamm, R. D., & Charest, J. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056910 · Cited by 233
EGFR regulates RhoA-GTP dependent cell motility in E-cadherin mutant cells
Mateus, A. R., Seruca, R., Machado, J. C., Keller, G., Oliveira, M. J., Suriano, G., & Luber, B. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm113 · Cited by 92
A microfluidic model for organ-specific extravasation of circulating tumor cells
Riahi, R., Yang, Y. L., Kim, H., Jiang, L., Wong, P. K., & Zohar, Y. (2014) · Biomicrofluidics · doi:10.1063/1.4868301 · Cited by 60
Generation of rac3 Null Mutant Mice: Role of Rac3 in Bcr/Abl-Caused Lymphoblastic Leukemia
Cho, Y. J., Zhang, B., Kaartinen, V., Haataja, L., de Curtis, I., Groffen, J., & Heisterkamp, N. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.13.5777-5785.2005 · Cited by 50
Xu, C.-X., Jin, H., Chung, Y.-S., Shin, J.-Y., Lee, K.-H., Beck, G. R., Palmos, G. N., Choi, B.-D., & Cho, M.-H. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf801578x · Cited by 24
Metadata
- Authors
- Mareel, M., & Leroy, A.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2003-04-01
- Volume
- 83
- Issue
- 2
- Pages
- 337-376
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W2074413067
- Cited by
- 524
- References
- 20
- FWCI
- 2.42
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
