journal article Nov 21, 2014

Remodelling the extracellular matrix in development and disease

Topics

No keywords indexed for this article. Browse by subject →

References
161
[1]
The Extracellular Matrix: Not Just Pretty Fibrils

Richard O. Hynes

Science 2009 10.1126/science.1176009
[2]
Jarvelainen, H., Sainio, A., Koulu, M., Wight, T. N. & Penttinen, R. Extracellular matrix molecules: potential targets in pharmacotherapy. Pharmacol. Rev. 61, 198–223 (2009). 10.1124/pr.109.001289
[3]
Bateman, J. F., Boot-Handford, R. P. & Lamande, S. R. Genetic diseases of connective tissues: cellular and extracellular effects of ECM mutations. Nature Rev. Genet. 10, 173–183 (2009). 10.1038/nrg2520
[4]
Rozario, T. & DeSimone, D. W. The extracellular matrix in development and morphogenesis: a dynamic view. Dev. Biol. 341, 126–140 (2010). 10.1016/j.ydbio.2009.10.026
[5]
Hynes, R. O. & Naba, A. Overview of the matrisome—an inventory of extracellular matrix constituents and functions. Cold Spring Harb. Perspect. Biol. 4, a004903 (2012). This review gives a complete list of ECM proteins that are part of the matrisome, and describes the ECM structure and function modifiers and the evolution of the matrisome. 10.1101/cshperspect.a004903
[6]
Lu, P., Takai, K., Weaver, V. M. & Werb, Z. Extracellular matrix degradation and remodeling in development and disease. Cold Spring Harb. Perspect. Biol. 3, a005058 (2011).
[7]
The extracellular matrix at a glance

Christian Frantz, Kathleen M. Stewart, Valerie M. Weaver

Journal of Cell Science 2010 10.1242/jcs.023820
[8]
Zhen, G. & Cao, X. Targeting TGFβ signaling in subchondral bone and articular cartilage homeostasis. Trends Pharmacol. Sci. 35, 227–236 (2014). 10.1016/j.tips.2014.03.005
[9]
Gross, J. & Lapiere, C. M. Collagenolytic activity in amphibian tissues: a tissue culture assay. Proc. Natl Acad. Sci. USA 48, 1014–1022 (1962). 10.1073/pnas.48.6.1014
[10]
Hite, L. A., Shannon, J. D., Bjarnason, J. B. & Fox, J. W. Sequence of a cDNA clone encoding the zinc metalloproteinase hemorrhagic toxin e from Crotalus atrox: evidence for signal, zymogen, and disintegrin-like structures. Biochemistry 31, 6203–6211 (1992). 10.1021/bi00142a005
[11]
Kuno, K. et al. Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene. J. Biol. Chem. 272, 556–562 (1997). 10.1074/jbc.272.1.556
[12]
Murphy, G. The ADAMs: signalling scissors in the tumour microenvironment. Nature Rev. Cancer 8, 929–941 (2008). 10.1038/nrc2459
[13]
White, J. M. ADAMs: modulators of cell-cell and cell–matrix interactions. Curr. Opin. Cell Biol. 15, 598–606 (2003). 10.1016/j.ceb.2003.08.001
[14]
Apte, S. S. A disintegrin-like and metalloprotease (reprolysin-type) with thrombospondin type 1 motif (ADAMTS) superfamily: functions and mechanisms. J. Biol. Chem. 284, 31493–31497 (2009). 10.1074/jbc.r109.052340
[15]
Bond, J. S., Rojas, K., Overhauser, J., Zoghbi, H. Y. & Jiang, W. The structural genes, MEP1A and MEP1B, for the α and β subunits of the metalloendopeptidase meprin map to human chromosomes 6p and 18q, respectively. Genomics 25, 300–303 (1995). 10.1016/0888-7543(95)80142-9
[16]
Bertenshaw, G. P., Norcum, M. T. & Bond, J. S. Structure of homo- and hetero-oligomeric meprin metalloproteases. Dimers, tetramers, and high molecular mass multimers. J. Biol. Chem. 278, 2522–2532 (2003). 10.1074/jbc.m208808200
[17]
Herzog, C., Haun, R. S., Ludwig, A., Shah, S. V. & Kaushal, G. P. ADAM10 is the major sheddase responsible for the release of membrane-associated meprin A. J. Biol. Chem. 289, 13308–13322 (2014). 10.1074/jbc.m114.559088
[18]
Kruse, M. N. et al. Human meprin α and β homo-oligomers: cleavage of basement membrane proteins and sensitivity to metalloprotease inhibitors. Biochem. J. 378, 383–389 (2004). 10.1042/bj20031163
[19]
Broder, C. et al. Metalloproteases meprinα and meprinβ are C- and N-procollagen proteinases important for collagen assembly and tensile strength. Proc. Natl Acad. Sci. USA 110, 14219–14224 (2013). 10.1073/pnas.1305464110
[20]
Jefferson, T. et al. The substrate degradome of meprin metalloproteases reveals an unexpected proteolytic link between meprin β and ADAM10. Cell. Mol. Life Sci. 70, 309–333 (2013). 10.1007/s00018-012-1106-2
[21]
Geurts, N. et al. Meprins process matrix metalloproteinase-9 (MMP-9)/gelatinase B and enhance the activation kinetics by MMP-3. FEBS Lett. 586, 4264–4269 (2012). 10.1016/j.febslet.2012.10.033
[22]
Khokha, R., Murthy, A. & Weiss, A. Metalloproteinases and their natural inhibitors in inflammation and immunity. Nature Rev. Immunol. 13, 649–665 (2013). 10.1038/nri3499
[23]
Baker, A. H., Edwards, D. R. & Murphy, G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J. Cell Sci. 115, 3719–3727 (2002). 10.1242/jcs.00063
[24]
Smith, H. W. & Marshall, C. J. Regulation of cell signalling by uPAR. Nature Rev. Mol. Cell. Biol. 11, 23–36 (2010). 10.1038/nrm2821
[25]
Bonnefoy, A. & Legrand, C. Proteolysis of subendothelial adhesive glycoproteins (fibronectin, thrombospondin, and von Willebrand factor) by plasmin, leukocyte cathepsin G, and elastase. Thromb. Res. 98, 323–332 (2000). 10.1016/s0049-3848(99)00242-x
[26]
Giuffrida, P., Biancheri, P. & MacDonald, T. T. Proteases and small intestinal barrier function in health and disease. Curr. Opin. Gastroenterol. 30, 147–153 (2014). 10.1097/mog.0000000000000042
[27]
Mohamed, M. M. & Sloane, B. F. Cysteine cathepsins: multifunctional enzymes in cancer. Nature Rev. Cancer 6, 764–775 (2006). 10.1038/nrc1949
[28]
Fonovic, M. & Turk, B. Cysteine cathepsins and extracellular matrix degradation. Biochim. Biophys. Acta 1840, 2560–2570 (2014). 10.1016/j.bbagen.2014.03.017
[29]
Uchimura, K. et al. HSulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparin-bound growth factors and chemokines: effects on VEGF, FGF-1, and SDF-1. BMC Biochem. 7, 2 (2006). 10.1186/1471-2091-7-2
[30]
Identification of stem cells in small intestine and colon by marker gene Lgr5

Nick Barker, Johan H. van Es, Jeroen Kuipers et al.

Nature 2007 10.1038/nature06196
[31]
Hasebe, T. et al. Thyroid hormone-induced cell–cell interactions are required for the development of adult intestinal stem cells. Cell Biosci. 3, 18 (2013). 10.1186/2045-3701-3-18
[32]
Su, Y., Shi, Y., Stolow, M. A. & Shi, Y. B. Thyroid hormone induces apoptosis in primary cell cultures of tadpole intestine: cell type specificity and effects of extracellular matrix. J. Cell Biol. 139, 1533–1543 (1997). 10.1083/jcb.139.6.1533
[33]
Patterton, D., Hayes, W. P. & Shi, Y. B. Transcriptional activation of the matrix metalloproteinase gene stromelysin-3 coincides with thyroid hormone-induced cell death during frog metamorphosis. Dev. Biol. 167, 252–262 (1995). 10.1006/dbio.1995.1021
[34]
Ishizuya-Oka, A. et al. Requirement for matrix metalloproteinase stromelysin-3 in cell migration and apoptosis during tissue remodeling in Xenopus laevis. J. Cell Biol. 150, 1177–1188 (2000). This paper showed that MMP11 is required for cell fate determination and cell migration during morphogenesis, most probably through ECM remodelling. 10.1083/jcb.150.5.1177
[35]
Amano, T., Kwak, O., Fu, L., Marshak, A. & Shi, Y. B. The matrix metalloproteinase stromelysin-3 cleaves laminin receptor at two distinct sites between the transmembrane domain and laminin binding sequence within the extracellular domain. Cell Res. 15, 150–159 (2005). 10.1038/sj.cr.7290280
[36]
Fujimoto, K., Nakajima, K. & Yaoita, Y. Expression of matrix metalloproteinase genes in regressing or remodeling organs during amphibian metamorphosis. Dev. Growth Differ. 49, 131–143 (2007). 10.1111/j.1440-169x.2007.00916.x
[37]
Hasebe, T., Hartman, R., Fu, L., Amano, T. & Shi, Y. B. Evidence for a cooperative role of gelatinase A and membrane type-1 matrix metalloproteinase during Xenopus laevis development. Mech. Dev. 124, 11–22 (2007). 10.1016/j.mod.2006.09.001
[38]
Simon-Assmann, P., Kedinger, M., De Arcangelis, A., Rousseau, V. & Simo, P. Extracellular matrix components in intestinal development. Experientia 51, 883–900 (1995). 10.1007/bf01921739
[39]
Simon-Assmann, P., Kedinger, M. & Haffen, K. Immunocytochemical localization of extracellular-matrix proteins in relation to rat intestinal morphogenesis. Differentiation 32, 59–66 (1986). 10.1111/j.1432-0436.1986.tb00556.x
[40]
Simon-Assmann, P., Bouziges, F., Freund, J. N., Perrin-Schmitt, F. & Kedinger, M. Type IV collagen mRNA accumulates in the mesenchymal compartment at early stages of murine developing intestine. J. Cell Biol. 110, 849–857 (1990). 10.1083/jcb.110.3.849
[41]
Simon-Assmann, P. et al. The laminins: role in intestinal morphogenesis and differentiation. Ann. NY Acad. Sci. 859, 46–64 (1998). 10.1111/j.1749-6632.1998.tb11110.x
[42]
Mahoney, Z. X., Stappenbeck, T. S. & Miner, J. H. Laminin α 5 influences the architecture of the mouse small intestine mucosa. J. Cell Sci. 121, 2493–2502 (2008). 10.1242/jcs.025528
[43]
Beaulieu, J. F. Integrins and human intestinal cell functions. Front. Biosci. 4, D310–D321 (1999). 10.2741/a429
[44]
Benoit, Y. D. et al. Integrin α8β1 regulates adhesion, migration and proliferation of human intestinal crypt cells via a predominant RhoA/ROCK-dependent mechanism. Biol. Cell 101, 695–708 (2009). 10.1042/bc20090060
[45]
Benoit, Y. D. et al. Integrin α8β1 confers anoikis susceptibility to human intestinal epithelial crypt cells. Biochem. Biophys. Res. Commun. 399, 434–439 (2010). 10.1016/j.bbrc.2010.07.107
[46]
Groulx, J. F. et al. Collagen VI is a basement membrane component that regulates epithelial cell-fibronectin interactions. Matrix Biol. 30, 195–206 (2011). 10.1016/j.matbio.2011.03.002
[47]
Henning, S. J. et al. Meprin mRNA in rat intestine during normal and glucocorticoid-induced maturation: divergent patterns of expression of α and β subunits. FEBS Lett. 462, 368–372 (1999). 10.1016/s0014-5793(99)01558-6
[48]
Sato, T. & Clevers, H. Growing self-organizing mini-guts from a single intestinal stem cell: mechanism and applications. Science 340, 1190–1194 (2013). 10.1126/science.1234852
[49]
Kim, H. Y. & Nelson, C. M. Extracellular matrix and cytoskeletal dynamics during branching morphogenesis. Organogenesis 8, 56–64 (2012). 10.4161/org.19813
[50]
Grobstein, C. & Cohen, J. Collagenase: effect on the morphogenesis of embryonic salivary epithelium in vitro. Science 150, 626–628 (1965). 10.1126/science.150.3696.626

Showing 50 of 161 references

Cited By
3,772
Journal of Oral Biosciences
Astrocytes and Alcohol Throughout the Lifespan

Marina Guizzetti, Regina A. Mangieri · 2026

Biological Psychiatry
Journal of the Mechanics and Physic...
Science and Technology of Advanced...
Nature
Matrisome Transcriptome Dynamics during Tissue Aging

Zulfiya G. Guvatova, Anastasiya A. Kobelyatskaya · 2024

Life
ACS Biomaterials Science & Engi...
Science Translational Medicine
Matrix scaffolds for endometrium-derived organoid models

Silke De Vriendt, Celia Mesias Casares · 2023

Frontiers in Endocrinology
Metrics
3,772
Citations
161
References
Details
Published
Nov 21, 2014
Vol/Issue
15(12)
Pages
786-801
License
View
Cite This Article
Caroline Bonnans, Jonathan Chou, Zena Werb (2014). Remodelling the extracellular matrix in development and disease. Nature Reviews Molecular Cell Biology, 15(12), 786-801. https://doi.org/10.1038/nrm3904
Related

You May Also Like

Shedding light on the cell biology of extracellular vesicles

Guillaume van Niel, Gisela D'Angelo · 2018

7,167 citations

Molecular mechanisms of epithelial–mesenchymal transition

Samy Lamouille, Jian Xu · 2014

6,770 citations

Ferroptosis: mechanisms, biology and role in disease

Xuejun Jiang, Brent R. Stockwell · 2021

6,426 citations

Membrane lipids: where they are and how they behave

Gerrit van Meer, Dennis R. Voelker · 2008

6,295 citations

Biomolecular condensates: organizers of cellular biochemistry

Salman F. Banani, Hyun O. Lee · 2017

5,869 citations