Quantitative measurement of invadopodia-mediated extracellular matrix proteolysis in single and multicellular contexts

Journal of Visualized Experiments

Volumn , Issue 66, 2012, Pages

  Martin, Karen H ^a   Hayes, Karen E ^a   Walk, Elyse L ^a   Ammer, Amanda Gatesman ^a   Markwell, Steven M ^a   Weed, Scott A ^a  

^a WEST VIRGINIA UNIVERSITY   (United States)

Author keywords

Anatomy; Biochemistry; Cancer biology; Cellular biology; Confocal microscopy; Extracellular matrix; Gelatin; Invadopodia; Issue 66; Molecular biology; Oregon green; Quantification

Indexed keywords

CARBOXYLIC ACID; MATRIX METALLOPROTEINASE; OREGON GREEN 488 CARBOXYLIC ACID; SCLEROPROTEIN;

ARTICLE; CELL SURFACE; CHEMISTRY; EXTRACELLULAR MATRIX; FLUORESCENCE MICROSCOPY; INSTRUMENTATION; METABOLISM; METHODOLOGY; PROTEIN DEGRADATION;

CARBOXYLIC ACIDS; CELL SURFACE EXTENSIONS; EXTRACELLULAR MATRIX; EXTRACELLULAR MATRIX PROTEINS; MATRIX METALLOPROTEINASES; MICROSCOPY, FLUORESCENCE; PROTEOLYSIS;

EID: 84868283372     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/4119     Document Type: Article

References (28)

1. Ridley, A.J. Life at the leading edge. Cell. 145, 1012-1022, [pii] S0092-8674(11)00652-0 doi:10.1016/j.cell.2011.06.010 (2011).
2. Murphy, D.A. & Courtneidge, S.A. The 'ins' and 'outs' of podosomes and invadopodia: characteristics, formation and function. Nat. Rev. Mol. Cell Biol. 12, 413-426, [pii] nrm3141 doi:10.1038/nrm3141 (2011).
3. Linder, S., Wiesner, C., & Himmel, M. Degrading Devices: Invadosomes in Proteolytic Cell Invasion. Annu. Rev. Cell. Dev. Biol., doi:10.1146/annurev-cellbio-092910-154216 (2010).
4. Chen, W.T., Chen, J.M., Parsons, S.J., & Parsons, J.T. Local degradation of fibronectin at sites of expression of the transforming gene product pp60src. Nature. 316, 156-158 (1985).
5. Artym, V.V., Zhang, Y., Seillier-Moiseiwitsch, F., Yamada, K.M., & Mueller, S.C. Dynamic interactions of cortactin and membrane type 1 matrix metalloproteinase at invadopodia: defining the stages of invadopodia formation and function. Cancer Res. 66, 3034-3043, [pii] 66/6/3034 doi:10.1158/0008-5472.CAN-05-2177 (2006).
6. Ayala, I., et al. Multiple regulatory inputs converge on cortactin to control invadopodia biogenesis and extracellular matrix degradation. J. Cell Sci., (2008).
7. Ammer, A.G., et al. Saracatinib impairs head and neck squamous cell carcinoma invasion by disrupting invadopodia function. J. Cancer Sci. Ther. 1, 52-61, doi:10.4172/1948-5956.1000009 (2009).
8. Seals, D.F., et al. The adaptor protein Tks5/Fish is required for podosome formation and function, and for the protease-driven invasion of cancer cells. Cancer Cell. 7, 155-165 (2005).
9. Yamaguchi, H., et al. Molecular mechanisms of invadopodium formation: the role of the N-WASP-Arp2/3 complex pathway and cofilin. J. Cell Biol. 168, 441-452 (2005).
10. Kopp, P., et al. The kinesin KIF1C and microtubule plus ends regulate podosome dynamics in macrophages. Mol. Biol. Cell. 17, 2811-2823, [pii] E05-11-1010 doi:10.1091/mbc.E05-11-1010 (2006).
11. Oser, M., et al. Cortactin regulates cofilin and N-WASp activities to control the stages of invadopodium assembly and maturation. J. Cell. Biol. 186, 571-587 (2009).
12. Rasband, W.S. Image J. U.S. National Institutes of Health., (1997-2011).
13. Kelley, L.C., et al. Oncogenic Src requires a wild-type counterpart to regulate invadopodia maturation. J. Cell Sci. 123, 3923-3932, [pii] jcs.075200 doi:10.1242/jcs.075200 (2010).
14. Chen, W.T. & Singer, S.J. Fibronectin is not present in the focal adhesions formed between normal cultured fibroblasts and their substrata. Proc. Natl. Acad. Sci. U.S.A. 77, 7318-7322 (1980).
15. Chen, W.T., Olden, K., Bernard, B.A., & Chu, F.F. Expression of transformation-associated protease(s) that degrade fibronectin at cell contact sites. J. Cell Biol. 98, 1546-1555 (1984).
16. Bharti, S., et al. Src-dependent phosphorylation of ASAP1 regulates podosomes. Mol. Cell Biol. 27, 8271-8283 (2007).
17. Albrechtsen, R., Stautz, D., Sanjay, A., Kveiborg, M., & Wewer, U. M. Extracellular engagement of ADAM12 induces clusters of invadopodia with localized ectodomain shedding activity. Exp. Cell Res. 317, 195-209, [pii] S0014-4827(10)00457-X doi:10.1016/j.yexcr.2010.10.003 (2011).
18. Scott, R.W., et al. LIM kinases are required for invasive path generation by tumor and tumor-associated stromal cells. J. Cell Biol. 191, 169-185, [pii] jcb.201002041 doi:10.1083/jcb.201002041 (2010).
19. Mueller, S.C., Yeh, Y., & Chen, W.T. Tyrosine phosphorylation of membrane proteins mediates cellular invasion by transformed cells. J. Cell. Biol. 119, 1309-1325 (1992).
20. Bowden, E.T., Coopman, P.J., & Mueller, S.C. Invadopodia: unique methods for measurement of extracellular matrix degradation in vitro. Methods Cell Biol. 63, 613-627 (2001).
21. Baldassarre, M., et al. Dynamin participates in focal extracellular matrix degradation by invasive cells. Mol. Biol. Cell. 14, 1074-1084 (2003).
22. Alexander, N.R., et al. Extracellular matrix rigidity promotes invadopodia activity. Curr. Biol. 18, 1295-1299, [pii] S0960-9822(08)01035-X doi:10.1016/j.cub.2008.07.090 (2008).
23. Artym, V.V., Yamada, K.M., & Mueller, S.C. ECM degradation assays for analyzing local cell invasion. Methods Mol. Biol. 522, 211-219, doi:10.1007/978-1-59745-413-1_15 (2009).
24. Schoumacher, M., Goldman, R.D., Louvard, D., & Vignjevic, D.M. Actin, microtubules, and vimentin intermediate filaments cooperate for elongation of invadopodia. J. Cell Biol. 189, 541-556, [pii] jcb.200909113 doi:10.1083/jcb.200909113 (2010).
25. Clark, E.S., Whigham, A.S., Yarbrough, W.G., & Weaver, A.M. Cortactin is an essential regulator of matrix metalloproteinase secretion and extracellular matrix degradation in invadopodia. Cancer Res. 67, 4227-4235, [pii] 67/9/4227 doi:10.1158/0008-5472.CAN-06-3928 (2007).
26. Yamaguchi, H., et al. Phosphoinositide 3-kinase signaling pathway mediated by p110alpha regulates invadopodia formation. J. Cell Biol. 193, 1275-1288, [pii] jcb.201009126 doi:10.1083/jcb.201009126 (2011).
27. Li, A., et al. The actin-bundling protein fascin stabilizes actin in invadopodia and potentiates protrusive invasion. Curr. Biol. 20, 339-345, [pii] S0960-9822(09)02159-9 doi:10.1016/j.cub.2009.12.035 (2010).
28. Yamaguchi, H., et al. Phosphatidylinositol 4,5-bisphosphate and PIP5-kinase Ialpha are required for invadopodia formation in human breast cancer cells. Cancer Sci. [pii] CAS1574 doi:10.1111/j.1349-7006.2010.01574.x (2010).