Cited by 119Cancer Cells and MetastasisTGF-β signaling in diseasesCellular Mechanics and Interactions

The DOI matches its Crossref record; 51 of the 52 references it cites were found in a registry or an index.

Tumor-Secreted LOXL2 Activates Fibroblasts through FAK Signaling

Open access

Barker, Holly E., Bird, Demelza, Lang, Georgina, Erler, Janine T.·2013·Molecular Cancer Research

DOI 10.1158/1541-7786.mcr-13-0033-tPMC PMC3833835

Published version of a preprint

Open this paper in CoChat — free account

Abstract

Cancer-associated fibroblasts enhance cancer progression when activated by tumor cells through mechanisms not yet fully understood. Blocking mammary tumor cell–derived lysyl oxidase-like 2 (LOXL2) significantly inhibited mammary tumor cell invasion and metastasis in transgenic and orthotopic mouse models. Here, we discovered that tumor-derived LOXL2 directly activated stromal fibroblasts in the tumor microenvironment. Genetic manipulation or antibody inhibition of LOXL2 in orthotopically grown mammary tumors reduced the expression of α-smooth muscle actin (α-SMA). Using a marker for reticular fibroblasts, it was determined that expression of α-SMA was localized to fibroblasts recruited from the host tissue. This marker also revealed that the matrix present in tumors with reduced levels of LOXL2 was more scattered compared with control tumors which exhibited matrices with dense, parallel alignments. Importantly, in vitro assays revealed that tumor-derived LOXL2 and a recombinant LOXL2 protein induced fibroblast branching on collagen matrices, as well as increased fibroblast-mediated collagen contraction and invasion of fibroblasts through extracellular matrix. Moreover, LOXL2 induced the expression of α-SMA in fibroblasts grown on collagen matrices. Mechanistically, it was determined that LOXL2 activated fibroblasts through integrin-mediated focal adhesion kinase activation. These results indicate that inhibition of LOXL2 in tumors not only reduces tumor cell invasion but also attenuates the activation of host cells in the tumor microenvironment. Implications: These findings reveal new insight into the mechanisms of fibroblast activation, a novel function of LOXL2, and further highlight the importance of generating LOXL2-targeted therapies for the prevention of tumor progression and metastasis. Mol Cancer Res; 11(11); 1425–36. ©2013 AACR.

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

Crossref · 10.1158/1541-7786.mcr-13-0033-t

Cites

51 of 51 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

1 retracted

Lysyl oxidase is essential for hypoxia-induced metastasis
Erler, J. T., Bennewith, K. L., Nicolau, M., Dornhöfer, N., Kong, C., Le, Q.-T., Chi, J.-T. A., Jeffrey, S. S., & Giaccia, A. J. (2006) · Nature · doi:10.1038/nature04695 · Cited by 1,309
Self-citation
Retracted
Calcium's Role in Mechanotransduction during Muscle Development
Damm, T. B., & Egli, M. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000356667 · Cited by 14,552
Integrins: Versatility, modulation, and signaling in cell adhesion
Hynes, R. O. (1992) · Cell · doi:10.1016/0092-8674(92)90115-s · Cited by 9,857
Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin
Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323
Fibroblasts in cancer
Kalluri, R., & Zeisberg, M. (2006) · Nature Reviews Cancer · doi:10.1038/nrc1877 · Cited by 4,538
Myofibroblasts and mechano-regulation of connective tissue remodelling
Tomasek, J. J., Gabbiani, G., Hinz, B., Chaponnier, C., & Brown, R. A. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm809 · Cited by 4,290
Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling
Levental, K. R., Yu, H., Kass, L., Lakins, J. N., Egeblad, M., Erler, J. T., Fong, S. F. T., Csiszar, K., Giaccia, A., Weninger, W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.027 · Cited by 4,101
Self-citation
Stromal Fibroblasts Present in Invasive Human Breast Carcinomas Promote Tumor Growth and Angiogenesis through Elevated SDF-1/CXCL12 Secretion
Orimo, A., Gupta, P. B., Sgroi, D. C., Arenzana-Seisdedos, F., Delaunay, T., Naeem, R., Carey, V. J., Richardson, A. L., & Weinberg, R. A. (2005) · Cell · doi:10.1016/j.cell.2005.02.034 · Cited by 3,759
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
Stromal fibroblasts in cancer initiation and progression
Bhowmick, N. A., Neilson, E. G., & Moses, H. L. (2004) · Nature · doi:10.1038/nature03096 · Cited by 2,350

Show all 52 references

Research works printed but not linked: 1

Tarin, 1969, Ultrastructural features of wound healing in mouse skin, J Anat, 105, 189

Sorted by citations

FAK in cancer: mechanistic findings and clinical applications
Sulzmaier, F. J., Jean, C., & Schlaepfer, D. D. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3792 · Cited by 1,381
TGFβ biology in cancer progression and immunotherapy
Derynck, R., Turley, S. J., & Akhurst, R. J. (2021) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-020-0403-1 · Cited by 944
Cancer-associated fibroblasts in desmoplastic tumors: emerging role of integrins
Zeltz, C., Primac, I., Erusappan, P., Alam, J., Noel, A., & Gullberg, D. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.08.004 · Cited by 290
Targeting ECM Disrupts Cancer Progression
Venning, F. A., Wullkopf, L., & Erler, J. T. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00224 · Cited by 256
Self-citation
Tissue Force Programs Cell Fate and Tumor Aggression
Northey, J. J., Przybyla, L., & Weaver, V. M. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0733 · Cited by 242
Emerging Roles of Focal Adhesion Kinase in Cancer
Tai, Y.-L., Chen, L., & Shen, T. (2015) · BioMed Research International · doi:10.1155/2015/690690 · Cited by 226
Melanoma miRNA trafficking controls tumour primary niche formation
Dror, S., Sander, L., Doron, H., Sheinboim, D., Barzilai, A., Dishon, Y., Apcher, S., Golan, T., Greenberger, S., Barshack, I., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3399 · Cited by 214
ZEB1 induces LOXL2-mediated collagen stabilization and deposition in the extracellular matrix to drive lung cancer invasion and metastasis
Peng, D. H., Ungewiss, C., Tong, P., Byers, L. A., Wang, J., Canales, J. R., Villalobos, P. A., Uraoka, N., Mino, B., Behrens, C., et al. (2016) · Oncogene · doi:10.1038/onc.2016.358 · Cited by 211
Tumor-Derived Osteopontin Reprograms Normal Mammary Fibroblasts to Promote Inflammation and Tumor Growth in Breast Cancer
Sharon, Y., Raz, Y., Cohen, N., Ben‐Shmuel, A., Doron, H., Geiger, T., & Erez, N. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-1990 · Cited by 175
Hypoxia and loss of PHD2 inactivate stromal fibroblasts to decrease tumour stiffness and metastasis
Madsen, C. D., Pedersen, J. T., Venning, F. A., Singh, L. B., Moeendarbary, E., Charras, G., Cox, T. R., Sahai, E., & Erler, J. T. (2015) · The EMBO Reports · doi:10.15252/embr.201540107 · Cited by 157
Self-citation
Human lysyl oxidase-like 2
Moon, H.-J., Finney, J., Ronnebaum, T. A., & Mure, M. (2014) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2014.07.003 · Cited by 138
Tumor Cell Invasion Can Be Blocked by Modulators of Collagen Fibril Alignment That Control Assembly of the Extracellular Matrix
Grossman, M., Ben‐Chetrit, N., Zhuravlev, A., Afik, R., Bassat, E., Solomonov, I., Yarden, Y., & Sagi, I. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2813 · Cited by 134
Comparative analysis of lysyl oxidase (like) family members in pulmonary fibrosis
Aumiller, V., Strobel, B., Romeike, M., Schuler, M. J., Stierstorfer, B., & Kreuz, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-00270-0 · Cited by 136
Exosomes from hypoxic endothelial cells have increased collagen crosslinking activity through up‐regulation of lysyl oxidase‐like 2
de Jong, O. G., van Balkom, B. W. M., Gremmels, H., & Verhaar, M. C. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12730 · Cited by 135
Lysyl Oxidase Isoforms and Potential Therapeutic Opportunities for Fibrosis and Cancer
Trackman, P. C. (2016) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2016.1151003 · Cited by 133
The lysyl oxidase like 2/3 enzymatic inhibitor, PXS‐5153A, reduces crosslinks and ameliorates fibrosis
Schilter, H. C., Findlay, A. D., Perryman, L., Yow, T. T., Moses, J., Zahoor, A., Turner, C. I., Deodhar, M., Foot, J. S., Zhou, W., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.14074 · Cited by 118
Pre-clinical evaluation of small molecule LOXL2 inhibitors in breast cancer
Chang, J., Lucas, M. C., Leonte, L. E., García-Montolio, M., Singh, L. B., Findlay, A. D., Deodhar, M., Foot, J. S., Jarolimek, W., Timpson, P., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.15257 · Cited by 113
Self-citation
LOXL2 in cancer: regulation, downstream effectors and novel roles
Wen, B., Xu, L., & Li, E. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188435 · Cited by 113
Targeting Lysyl Oxidase Family Meditated Matrix Cross-Linking as an Anti-Stromal Therapy in Solid Tumours
Setargew, Y. F. I., Wyllie, K., Grant, R. D., Chitty, J. L., & Cox, T. R. (2021) · Cancers · doi:10.3390/cancers13030491 · Cited by 114
The hallmarks of CAFs in cancer invasion
Atieh, Y., & Vignjevic, D. M. (2016) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2016.07.004 · Cited by 118
Proteomic Profiling of Human Prostate Cancer-associated Fibroblasts (CAF) Reveals LOXL2-dependent Regulation of the Tumor Microenvironment
Nguyen, E. V., Pereira, B. A., Lawrence, M. G., Ma, X., Rebello, R. J., Chan, H., Niranjan, B., Wu, Y., Ellem, S., Guan, X., et al. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001496 · Cited by 107
FAK activity in cancer‐associated fibroblasts is a prognostic marker and a druggable key metastatic player in pancreatic cancer
Zaghdoudi, S., Decaup, E., Belhabib, I., Samain, R., Cassant‐Sourdy, S., Rochotte, J., Brunel, A., Schlaepfer, D. D., Cros, J. F., Neuzillet, C., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012010 · Cited by 109
Emerging Roles of Extracellular Hsp90 in Cancer
Wong, D. S., & Jay, D. G. (2016) · Advances in cancer research · doi:10.1016/bs.acr.2016.01.001 · Cited by 99
Lysyl oxidase‐like 2 represses Notch1 expression in the skin to promote squamous cell carcinoma progression
Martín, A. L., Salvador, F., Moreno‐Bueno, G., Floristán, A., Ruiz‐Herguido, C., Cuevas, E. P., Morales, S., Santos, V., Csiszár, K., Dubus, P. R., et al. (2015) · The EMBO Journal · doi:10.15252/embj.201489975 · Cited by 93
Melanoma‐derived extracellular vesicles instigate proinflammatory signaling in the metastatic microenvironment
Lahav, T. G., Adler, O., Zait, Y., Shani, O., Amer, M., Doron, H., Abramovitz, L., Yofe, I., Cohen, N., & Erez, N. (2019) · International Journal of Cancer · doi:10.1002/ijc.32521 · Cited by 92
Evolving roles of lysyl oxidase family in tumorigenesis and cancer therapy
Ye, M., Song, Y., Pan, S., Chu, M., Wang, Z. P., & Zhu, X. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107633 · Cited by 89
Lysyl Oxidase Family Enzymes and Their Role in Tumor Progression
Liburkin-Dan, T., Toledano, S., & Neufeld, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116249 · Cited by 88
Tamoxifen mechanically reprograms the tumor microenvironment via HIF‐1A and reduces cancer cell survival
Cortés, E., Lachowski, D., Robinson, B. K., Sarper, M., Teppo, J., Thorpe, S. D., Lieberthal, T. J., Iwamoto, K., Lee, D. A., Okada, M., et al. (2018) · EMBO Reports · doi:10.15252/embr.201846557 · Cited by 84
Lysyl oxidase-like 2 (LOXL2) from stromal fibroblasts stimulates the progression of gastric cancer
Kasashima, H., Yashiro, M., Kinoshita, H., Fukuoka, T., Morisaki, T., Masuda, G., Sakurai, K., Kubo, N., Ohira, M., & Hirakawa, K. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.08.014 · Cited by 82
Collagen code in tumor microenvironment: Functions, molecular mechanisms, and therapeutic implications
Zhang, Q., An, Z.-Y., Jiang, W. G., Jin, W., & He, X. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115390 · Cited by 79
Interplay Between LOX Enzymes and Integrins in the Tumor Microenvironment
Amendola, P. G., Reuten, R., & Erler, J. T. (2019) · Cancers · doi:10.3390/cancers11050729 · Cited by 76
Self-citation
Fibroblast activation and heterogeneity in fibrotic disease
Zhang, X., Zhang, Y., & Liu, Y. (2025) · Nature Reviews Nephrology · doi:10.1038/s41581-025-00969-8 · Cited by 82
Proteomic landscape of the extracellular matrix in the fibrotic kidney
Li, L., He, M., Tang, X., Huang, J., Li, J., Hong, X., Fu, H., & Liu, Y. (2023) · Kidney International · doi:10.1016/j.kint.2023.01.021 · Cited by 74
Inhibition of Lysyl Oxidase and Lysyl Oxidase-Like Enzymes Has Tumour-Promoting and Tumour-Suppressing Roles in Experimental Prostate Cancer
Nilsson, M., Adamo, H. H., Bergh, A. R. J., & Bergström, S. H. (2016) · Scientific Reports · doi:10.1038/srep19608 · Cited by 66
Lysyl Oxidase Family Proteins: Prospective Therapeutic Targets in Cancer
Wang, W., Wang, X., Yao, F., & Huang, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012270 · Cited by 63
Emerging role of LOXL2 in the promotion of pancreas cancer metastasis
Park, J. S., Lee, J.-H., Lee, Y. S., Kim, J. K., Dong, S. M., & Yoon, D. S. (2016) · Oncotarget · doi:10.18632/oncotarget.9918 · Cited by 58
Novel mechanism for OSM-promoted extracellular matrix remodeling in breast cancer: LOXL2 upregulation and subsequent ECM alignment
Dinca, S. C., Greiner, D., Weidenfeld, K., Bond, L., Barkan, D., & Jorcyk, C. L. (2021) · Breast Cancer Research · doi:10.1186/s13058-021-01430-x · Cited by 58
Stroma as an Active Player in the Development of the Tumor Microenvironment
Vannucci, L. E. (2014) · Cancer Microenvironment · doi:10.1007/s12307-014-0150-x · Cited by 56
Lysyl oxidases: linking structures and immunity in the tumor microenvironment
Tenti, P., & Vannucci, L. E. (2019) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-019-02404-x · Cited by 55
Cancer-Associated Fibroblasts in the Breast Tumor Microenvironment
Giorello, M. B., Borzone, F. R., Labovsky, V., Piccioni, F., & Chasseing, N. A. (2021) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-020-09475-y · Cited by 58
Hypoxic Signalling in Tumour Stroma
Laitala, A., & Erler, J. T. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00189 · Cited by 55
Self-citation
Targeting cancer-associated fibroblasts: Challenges, opportunities and future directions
Jenkins, B. H., Buckingham, J. F., Hanley, C. J., & Thomas, G. J. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108231 · Cited by 55
Lysyl Oxidase in Cancer Research
Perryman, L., & Erler, J. T. (2014) · Future Oncology · doi:10.2217/fon.14.39 · Cited by 53
Self-citation
Focal Adhesion Kinase Fine Tunes Multifaced Signals toward Breast Cancer Progression
Rigiracciolo, D. C., Cirillo, F., Talia, M., Muglia, L., Gutkind, J. S., Maggiolini, M., & Lappano, R. (2021) · Cancers · doi:10.3390/cancers13040645 · Cited by 55
Hematopoietic stem cell-derived adipocytes and fibroblasts in the tumor microenvironment
Xiong, Y. (2015) · World Journal of Stem Cells · doi:10.4252/wjsc.v7.i2.253 · Cited by 51
Lysyl Oxidase-Like Protein 2 Promotes Tumor Lymphangiogenesis and Lymph Node Metastasis in Breast Cancer
Wang, C., Xu, S., Tian, Y., Ju, A., Hou, Q., Liu, J., Fu, Y., & Luo, Y. (2019) · Neoplasia · doi:10.1016/j.neo.2019.03.003 · Cited by 48
Magnetic Resonance Elastography Shear Wave Velocity Correlates with Liver Fibrosis and Hepatic Venous Pressure Gradient in Adults with Advanced Liver Disease
Gharib, A. M., Han, M. A. T., Meissner, E. G., Kleiner, D. E., Zhao, X., McLaughlin, M. E., Matthews, L., Rizvi, B., Abd‐Elmoniem, K. Z., Sinkus, R., et al. (2017) · BioMed Research International · doi:10.1155/2017/2067479 · Cited by 44
Scavenger Receptor Cysteine-Rich domains of Lysyl Oxidase-Like2 regulate endothelial ECM and angiogenesis through non-catalytic scaffolding mechanisms
Umaña-Diaz, C., Pichol-Thievend, C., Marchand, M. F., Atlas, Y., Salza, R., Malbouyres, M., Barret, A., Teillon, J., Ardidie‐Robouant, C., Ruggiero, F., et al. (2019) · Matrix Biology · doi:10.1016/j.matbio.2019.11.003 · Cited by 44
Mechanobiology of Cancer Stem Cells and Their Niche
Choudhury, A. R., Gupta, S., Chaturvedi, P. K., Kumar, N., & Pandey, D. (2019) · Cancer Microenvironment · doi:10.1007/s12307-019-00222-4 · Cited by 43
Identification of a novel lysyl oxidase-like 2 alternative splicing isoform, LOXL2 Δe13, in esophageal squamous cell carcinoma
Lv, G.-Q., Zou, H., Liao, L., Cao, H., Zeng, F., Wu, B., Xie, J., Fang, W., Xu, L., & Li, E. (2014) · Biochemistry and Cell Biology · doi:10.1139/bcb-2014-0046 · Cited by 40
Lysyl oxidase-like 2 inhibition ameliorates glomerulosclerosis and albuminuria in diabetic nephropathy
Stangenberg, S., Saad, S., Schilter, H. C., Zaky, A. A., Gill, A. J., Pollock, C. A., & Wong, M. G. (2018) · Scientific Reports · doi:10.1038/s41598-018-27462-6 · Cited by 42
LOXL2 in Cancer: A Two-Decade Perspective
Cano, A., Eraso, P., Mazón, M. J., & Portillo, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241814405 · Cited by 40
Extracellular Processing of Lysyl Oxidase-like 2 and Its Effect on Amine Oxidase Activity
Okada, K., Moon, H.-J., Finney, J., Meier, A. A., & Mure, M. (2018) · Biochemistry · doi:10.1021/acs.biochem.8b01008 · Cited by 36
Targeting focal adhesion kinase boosts immune response in KRAS/LKB1 co-mutated lung adenocarcinoma via remodeling the tumor microenvironment
Qiao, M., Zhou, F., Liu, X., Jiang, T., Wang, H., Li, X., Zhao, C., Cheng, L., Chen, X., Ren, S., et al. (2024) · Experimental Hematology and Oncology · doi:10.1186/s40164-023-00471-6 · Cited by 35
LOXL2, a copper-dependent monoamine oxidase, activates lung fibroblasts through the TGF-β/Smad pathway
Wen, X., Liu, Y., Bai, Y. Z., Li, M., Fu, Q., & Zheng, Y. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3927 · Cited by 32
Loss of LOXL2 Promotes Uterine Hypertrophy and Tumor Progression by Enhancing H3K36ac-Dependent Gene Expression
Lu, X., Xin, D. E., Du, J. K., Zou, Q. C., Wu, Q. Y., Zhang, Y. S., Deng, W., Yue, J., Fan, X. S., Zeng, Y., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-22-0848 · Cited by 32
The interplay between extracellular matrix remodelling and kinase signalling in cancer progression and metastasis
Skhinas, J. N., & Cox, T. R. (2017) · Cell Adhesion & Migration · doi:10.1080/19336918.2017.1405208 · Cited by 31
Epithelial–mesenchymal transition and metastasis of colon cancer cells induced by the FAK pathway in cancer-associated fibroblasts
Xuefeng, X., Hou, M., Yang, Z., Agudamu, A., Wang, F., Su, X., Li, X., Shi, L., Terigele, T., Bao, L., et al. (2020) · Journal of International Medical Research · doi:10.1177/0300060520931242 · Cited by 30
Lysyl Oxidase Like‐2 (LOXL2): An Emerging Oncology Target
Chopra, V., Sangarappillai, R. M., Romero‐Canelón, I., & Jones, A. M. (2020) · Advanced Therapeutics · doi:10.1002/adtp.201900119 · Cited by 25
Multiple Roles of LOXL2 in the Progression of Hepatocellular Carcinoma and Its Potential for Therapeutic Targeting
Radić, J., Kožik, B., Nikolić, I., Kolarov-Bjelobrk, I., Vasiljević, T., Vranjković, B., & Despotović, S. Z. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241411745 · Cited by 23
Targeting cancer metastasis with antibody therapeutics
Hui-lin, Y., Kuo, Y., Smith, Z., & Spangler, J. B. (2021) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1698 · Cited by 22
Clinical relevance of lysyl oxidase-like 2 and functional mechanisms in glioma
Du, X., & Zhu, M.-J. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s164056 · Cited by 22
Silencing of lysyl oxidase‑like 2 inhibits the migration, invasion and epithelial‑to‑mesenchymal transition of renal cell carcinoma cells through the Src/FAK signaling pathway
Hong, X., & Yu, J. (2019) · International Journal of Oncology · doi:10.3892/ijo.2019.4726 · Cited by 20
Lysyl oxidase-like 2 is expressed in kidney tissue and is associated with the progression of tubulointerstitial fibrosis
Choi, S., Jeon, N., Choi, H. Y., Shin, J. I., Jeong, H. J., & Lim, B. J. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6918 · Cited by 19
Inhibition of Lysyl Oxidases Impairs Migration and Angiogenic Properties of Tumor-Associated Pericytes
Ribeiro, A. L., Kaid, C., Silva, P. B. G., Cortez, B. A., & Okamoto, O. K. (2017) · Stem Cells International · doi:10.1155/2017/4972078 · Cited by 18
IKKβ/NFκBp65 activated by interleukin-13 targets the autophagy-related genes LC3B and beclin 1 in fibroblasts co-cultured with breast cancer cells
Li, W., Xiong, L., Shi, X., Liang, X., QI, G.-Y., & MENG, C. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.3054 · Cited by 17
Second-Harmonic Generation Imaging Reveals Changes in Breast Tumor Collagen Induced by Neoadjuvant Chemotherapy
Desa, D. E., Wu, W., Brown, R. M., Brown, E. B., Hill, R. L., Turner, B. M., & Brown, E. B. (2022) · Cancers · doi:10.3390/cancers14040857 · Cited by 16
CLIM-TIME identifies metastatic microenvironment modulators for T cell therapy response
Wang, Y., Hu, W., Xia, R., Yang, X., Gu, Y., Ning, Z., Yang, T., Yu, C., Zhang, L., Li, D., et al. (2026) · Cell · doi:10.1016/j.cell.2025.12.042 · Cited by 14
Biophysical perspectives to understanding cancer-associated fibroblasts
Devarasou, S., Kang, M., & Shin, J. H. (2024) · APL Bioengineering · doi:10.1063/5.0199024 · Cited by 12
The role of the LOX family in cancer
Boaru, D. L., León-Oliva, D. D., Fraile‐Μartinez, O., Castro-Martinez, P. D., Montero, C. G., Ferrara-Coppola, C., Alhaddadin, M. N. M., Barrena-Blázquez, S., Peñas-González, C. D. L., Holgado-Tirado, N., et al. (2025) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2025.151527 · Cited by 13
A 3D–Predicted Structure of the Amine Oxidase Domain of Lysyl Oxidase–Like 2
Meier, A. A., Kuczera, K., & Mure, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232113385 · Cited by 12
A Comprehensive Review of Protein Biomarkers for Invasive Lung Cancer
Mezentsev, A., Durymanov, M. O., & Макаров, В. А. (2024) · Current Oncology · doi:10.3390/curroncol31090360 · Cited by 11
Significance of HIF-1α Expression and LOXL-2 Localization in Progression of Oral Squamous Cell Carcinoma
Bharti, A., Urs, A. B., & Kumar, P. (2021) · Asian Pacific Journal of Cancer Prevention · doi:10.31557/apjcp.2021.22.2.341 · Cited by 11
Exposure to oxLDL impairs TGF-β activity in human tendon cells
Mousavizadeh, R., Waugh, C., DeBruin, E., McCormack, R. G., Duronio, V., & Scott, A. (2023) · BMC Musculoskeletal Disorders · doi:10.1186/s12891-023-06308-x · Cited by 9
Divergent roles of lysyl oxidase family members in ornithine decarboxylase- and RAS-transformed mouse fibroblasts and human melanoma cells
Kielosto, M., Eriksson, J., Nummela, P., Yin, M., & Hölttä, E. (2018) · Oncotarget · doi:10.18632/oncotarget.26508 · Cited by 9
The role of LOXL2 in tumor progression, immune response and cellular senescence: a comprehensive analysis
Ye, C., Jiang, S., Zeng, T., He, S., Cao, J., & Xiao, J. (2024) · Discover Oncology · doi:10.1007/s12672-024-01107-9 · Cited by 8
Denatured collagen inhibits neuroblastoma tumor-sphere migration and growth via the LOX/LOXL2 – FAK signaling pathway
Bui, C., To, K. D., Vu, D. M., Nguyen, Q.-G., Nguyen, H. T., & Nguyen, S.-B. (2023) · Journal of Thermal Biology · doi:10.1016/j.jtherbio.2023.103624 · Cited by 8
Circulating tumor cells and the metastatic process: the complexity of malignancy
Raimo, T. D., Santis, E. D., Coppola, L., D'Andrea, M. R., & Angelini, F. (2018) · Journal of Cancer Metastasis and Treatment · doi:10.20517/2394-4722.2018.50 · Cited by 7
Neural Wiskott-Aldrich syndrome protein (N-WASP) promotes distant metastasis in pancreatic ductal adenocarcinoma via activation of LOXL2
Kim, H. S., Yun Sun, L. E. E., Dong, S. M., Kim, H. J., Lee, D. E., Kang, H. W., KIM, M. J., & Park, J. S. (2024) · Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics · doi:10.32604/or.2024.044029 · Cited by 7
Oxidative stress and copper smelter workers
Malekırad, A. A., Hassani, S., & Abdollahi, M. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-819092-0.00013-3 · Cited by 6
Knock-Out of the Five Lysyl-Oxidase Family Genes Enables Identification of Lysyl-Oxidase Pro-Enzyme Regulated Genes
Liburkin-Dan, T., Nir-Zvi, I., Razon, H., Kessler, O., & Neufeld, G. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911322 · Cited by 5
Premetastatic niche mechanics and organotropism in breast cancer
Libring, S., & Reinhart‐King, C. A. (2025) · npj Biological Physics and Mechanics. · doi:10.1038/s44341-025-00015-5 · Cited by 5
Multi-omics analysis reveals focal adhesion characteristic associated tumor immune microenvironment in colon adenocarcinoma
Xu, X., & Wang, J. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1088091 · Cited by 5
FAK Differentially Mechanoregulates Cell Migration during Wound Closure
Patten, J., Albeltagy, N., Bonadio, J. D., Ortez, A., & Wang, K. (2025) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.5c00667 · Cited by 4
Systematic Characterisation and Analysis of Lysyl Oxidase Family Members as Drivers of Tumour Progression and Multiple Drug Resistance
Liu, H., Sun, X., Dong, B., Zhang, J., Zhang, J., Gu, Y., Chen, L., Pang, X., Ye, J., Wang, X., et al. (2025) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.70536 · Cited by 4
Molecular and Cellular Mechanobiology of Cancer
Fattet, L., & Yang, J. (2016) · Springer eBooks · doi:10.1007/978-1-4939-5617-3_13 · Cited by 3
Correction: Tumor-Secreted LOXL2 Activates Fibroblasts through FAK Signaling
(2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0860 · Cited by 3
Integrins in Cancer: Refocusing on the Tumor Microenvironment
Zeltz, C., Lü, N., Heljäsvaara, R., & Gullberg, D. (2022) · Biology of extracellular matrix · doi:10.1007/978-3-030-99708-3_11 · Cited by 3
Novel mechanism for OSM-promoted extracellular matrix remodeling in breast cancer: LOXL2 upregulation and subsequent ECM alignmentPreprint
Dinca, S. C., Greiner, D., Weidenfeld, K., Bond, L., Barkan, D., & Jorcyk, C. L. (2020) · Research Square · doi:10.21203/rs.3.rs-57684/v1 · Cited by 2
LOXL2 reduces susceptibility to PARP inhibitors by promoting super-enhancer-regulated DNA damage repair in high-grade serous ovarian cancer
Song, C., Lin, Y., Cai, C., Tao, K., Tan, J., Xiong, K., Yang, W., Chi, J., Peng, Z., Zhao, G., et al. (2025) · Oncogene · doi:10.1038/s41388-025-03466-1 · Cited by 1
The prediction value of LOXL-2 in the clinical pathology and prognosis of cancers: A meta-analysis and bioinformatics analysis
Yang, S., Zhang, Q., Ran, Y., & Pan, Y. (2025) · Scientific Reports · doi:10.1038/s41598-025-30923-4 · Cited by 1
Cancer-associated fibroblasts in the lung cancer microenvironment from multi-dimensional mechanisms to therapeutic strategies
Feng, Y., Gu, L., Jia, Z., Zhang, C., & Zhu, Z. (2026) · Frontiers in Oncology · doi:10.3389/fonc.2026.1866753 · Cited by 1
Cross‐Talk Between Hypoxia and the Tumour via Exosomes
Sharma, S., Alharbi, M. G., Lai, A., Kobayashi, M., KLINE, R. C., Wade, K., Rice, G. E., & Salomón, C. (2017) · InTech eBooks · doi:10.5772/65688
Signaling Functions of Extracellular Hsp90 (eHsp90) in Cancer Metastasis
Bernstein, A., & Jay, D. G. (2019) · Heat shock proteins · doi:10.1007/978-3-030-03952-3_17 · Cited by 1
Inhibition of LOXL2 and Other Lysyl Oxidase (Like) Enzymes: Intervention at the Core of Fibrotic Pathology
Findlay, A. D., Turner, C. I., & Hamprecht, D. W. (2020) · Royal Society of Chemistry eBooks · doi:10.1039/9781788015783-00145 · Cited by 1
Microenvironmental Control of Metastatic Progression
Roskelley, C. D. (2014) · Cancer metastasis · doi:10.1007/978-3-319-12136-9_6
Understanding of ‘Networks’ In Vitro and/or In Vivo
Schoof, E. M., Ferkinghoff‐Borg, J., & Linding, R. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.40027-1
Proteomic Signatures of the Colorectal Cancer Desmoplastic Invasion Front
Karagiannis, G. (2014) · TSpace (University of Toronto)
Epidemiological and molecular features of cutaneous squamous cell carcinoma with perineural spread
Warren, T. A. (2017) · The University of Queensland · doi:10.14264/uql.2017.1054
Evaluation der Interaktionen zwischen extrazellulärer Matrix und ausgewählten tumorassoziierten Proteinen mittels Nahinfrarot-Antikörpern
Eckardt, J. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8263

Authors: Barker, H. E., Bird, D., Lang, G., & Erler, J. T.
Affiliations: University of Copenhagen (DK)
Corresponding author: Erler, Janine T.
ORCID: Barker, Holly E.
Erler, Janine T.
Venue: Molecular Cancer Research
Publisher: American Association for Cancer Research (AACR)
Published: 2013-11-01
Volume: 11
Issue: 11
Pages: 1425-1436
ISSN: 1541-7786 (ISSN-L)
1557-3125
DOI: 10.1158/1541-7786.mcr-13-0033-t
PMC: PMC3833835
OpenAlex: W2105524728
Cited by: 119
References: 52
Citations by year: 2026: 4 · 2025: 7 · 2024: 15 · 2023: 8 · 2022: 9 · 2021: 7 · 2020: 10 · 2019: 13 · 2018: 9 · 2017: 10 · 2016: 11 · 2015: 8 · 2014: 8
FWCI: 4.82
Type: journal article
Language: en
Update notices: correction (2019-10-01)
Open access: green
europepmc.org
Locations: Molecular Cancer Research (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Research at the University of Copenhagen (University of Copenhagen) (submittedVersion)
Funders: Cancer Research UK (A11355, A10433)
Topics: Health Sciences › Medicine › Oncology › Cancer Cells and Metastasis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
Keywords: LOXL2, cancer-associated fibroblasts, fibroblast activation, focal adhesion kinase, integrin signaling, tumor microenvironment, mammary tumors, tumor invasion, metastasis, alpha-smooth muscle actin, collagen matrix, extracellular matrix remodeling
MeSH terms: Actins, Amino Acid Oxidoreductases, Animals, Cell Adhesion, Collagen, Extracellular Matrix, Female, Fibroblasts, Mammary Neoplasms, Experimental, Mice, Inbred C57BL, Neoplasm Invasiveness, Signal Transduction, Gene Expression Regulation, Neoplastic, 3T3 Cells, Cell Line, Tumor, Cell Proliferation, Mice, Focal Adhesion Kinase 1, Tumor Microenvironment

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

Tumor-Secreted LOXL2 Activates Fibroblasts through FAK Signaling

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks