@article {296,
	title = {Extracellular matrix degradation and remodeling in development and disease.},
	journal = {Cold Spring Harb Perspect Biol},
	volume = {3},
	year = {2011},
	month = {2011 Dec},
	abstract = {<p>The extracellular matrix (ECM) serves diverse functions and is a major component of the cellular microenvironment. The ECM is a highly dynamic structure, constantly undergoing a remodeling process where ECM components are deposited, degraded, or otherwise modified. ECM dynamics are indispensible during restructuring of tissue architecture. ECM remodeling is an important mechanism whereby cell differentiation can be regulated, including processes such as the establishment and maintenance of stem cell niches, branching morphogenesis, angiogenesis, bone remodeling, and wound repair. In contrast, abnormal ECM dynamics lead to deregulated cell proliferation and invasion, failure of cell death, and loss of cell differentiation, resulting in congenital defects and pathological processes including tissue fibrosis and cancer. Understanding the mechanisms of ECM remodeling and its regulation, therefore, is essential for developing new therapeutic interventions for diseases and novel strategies for tissue engineering and regenerative medicine.</p>
},
	keywords = {Animals, Body Patterning, Cell Differentiation, Extracellular Matrix, Extracellular Matrix Proteins, Mice, Models, Biological, Neoplasms, Peptide Hydrolases, Signal Transduction, Stem Cells, Vertebrates},
	issn = {1943-0264},
	doi = {10.1101/cshperspect.a005058},
	author = {Lu, Pengfei and Takai, Ken and Weaver, Valerie M and Werb, Zena}
}
@article {331,
	title = {The extracellular matrix at a glance.},
	journal = {J Cell Sci},
	volume = {123},
	year = {2010},
	month = {2010 Dec 15},
	pages = {4195-200},
	keywords = {Animals, Extracellular Matrix, Extracellular Matrix Proteins, Fibrosis, Homeostasis, Humans, Neoplasms},
	issn = {1477-9137},
	doi = {10.1242/jcs.023820},
	author = {Frantz, Christian and Stewart, Kathleen M and Weaver, Valerie M}
}
@article {556,
	title = {Tissue phenotype depends on reciprocal interactions between the extracellular matrix and the structural organization of the nucleus.},
	journal = {Proc Natl Acad Sci U S A},
	volume = {95},
	year = {1998},
	month = {1998 Dec 8},
	pages = {14711-6},
	abstract = {<p>What determines the nuclear organization within a cell and whether this organization itself can impose cellular function within a tissue remains unknown. To explore the relationship between nuclear organization and tissue architecture and function, we used a model of human mammary epithelial cell acinar morphogenesis. When cultured within a reconstituted basement membrane (rBM), HMT-3522 cells form polarized and growth-arrested tissue-like acini with a central lumen and deposit an endogenous BM. We show that rBM-induced morphogenesis is accompanied by relocalization of the nuclear matrix proteins NuMA, splicing factor SRm160, and cell cycle regulator Rb. These proteins had distinct distribution patterns specific for proliferation, growth arrest, and acini formation, whereas the distribution of the nuclear lamina protein, lamin B, remained unchanged. NuMA relocalized to foci, which coalesced into larger assemblies as morphogenesis progressed. Perturbation of histone acetylation in the acini by trichostatin A treatment altered chromatin structure, disrupted NuMA foci, and induced cell proliferation. Moreover, treatment of transiently permeabilized acini with a NuMA antibody led to the disruption of NuMA foci, alteration of histone acetylation, activation of metalloproteases, and breakdown of the endogenous BM. These results experimentally demonstrate a dynamic interaction between the extracellular matrix, nuclear organization, and tissue phenotype. They further show that rather than passively reflecting changes in gene expression, nuclear organization itself can modulate the cellular and tissue phenotype.</p>
},
	keywords = {Cell Nucleus, Extracellular Matrix, Extracellular Matrix Proteins, Female, Gene Expression Regulation, Humans, Morphogenesis, Nuclear Proteins, Tumor Cells, Cultured},
	issn = {0027-8424},
	author = {Leli{\`e}vre, S A and Weaver, V M and Nickerson, J A and Larabell, C A and Bhaumik, A and Petersen, O W and Bissell, M J}
}
