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n3:pmcid
PMC0
bibo:doi
10.1038%2Fonc.2009.299
n5:contains
_:vb6199257 _:vb6199269 _:vb6199211 _:vb6199314
Subject Item
_:vb6199211
rdf:type
n5:Section
dc:title
introduction
n5:contains
_:vb6199240 _:vb6199241 _:vb6199242 _:vb6199243 _:vb6199244 _:vb6199245 _:vb6199246 _:vb6199247 _:vb6199232 _:vb6199233 _:vb6199234 _:vb6199235 _:vb6199236 _:vb6199237 _:vb6199238 _:vb6199239 _:vb6199256 _:vb6199248 _:vb6199249 _:vb6199250 _:vb6199251 _:vb6199252 _:vb6199253 _:vb6199254 _:vb6199255 _:vb6199212 _:vb6199213 _:vb6199214 _:vb6199215 _:vb6199224 _:vb6199225 _:vb6199226 _:vb6199227 _:vb6199228 _:vb6199229 _:vb6199230 _:vb6199231 _:vb6199216 _:vb6199217 _:vb6199218 _:vb6199219 _:vb6199220 _:vb6199221 _:vb6199222 _:vb6199223
Subject Item
_:vb6199212
rdf:type
n3:Context
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Mammographically dense breast tissue is correlated with a greater than four-fold increased risk for developing breast carcinoma (Boyd et al., >>1998<<; Boyd et al., 2001; McCormack & dos Santos Silva, 2006), making it one of the greatest independent risk factors for breast cancer (Boyd et al., 1998; McCormack & dos Santos Silva, 2006).
n3:mentions
n2:9865433
Subject Item
_:vb6199213
rdf:type
n3:Context
rdf:value
Mammographically dense breast tissue is correlated with a greater than four-fold increased risk for developing breast carcinoma (Boyd et al., 1998; Boyd et al., >>2001<<; McCormack & dos Santos Silva, 2006), making it one of the greatest independent risk factors for breast cancer (Boyd et al., 1998; McCormack & dos Santos Silva, 2006).
n3:mentions
n2:11389815
Subject Item
_:vb6199214
rdf:type
n3:Context
rdf:value
Mammographically dense breast tissue is correlated with a greater than four-fold increased risk for developing breast carcinoma (Boyd et al., 1998; Boyd et al., 2001; McCormack & dos Santos Silva, >>2006<<), making it one of the greatest independent risk factors for breast cancer (Boyd et al., 1998; McCormack & dos Santos Silva, 2006).
n3:mentions
n2:16775176
Subject Item
_:vb6199215
rdf:type
n3:Context
rdf:value
a greater than four-fold increased risk for developing breast carcinoma (Boyd et al., 1998; Boyd et al., 2001; McCormack & dos Santos Silva, 2006), making it one of the greatest independent risk factors for breast cancer (Boyd et al., >>1998<<; McCormack & dos Santos Silva, 2006). Ductal carcinoma in situ arises overwhelmingly in dense regions of the breast (Ursin et al., 2005), and high tissue density is associated with a greater risk for invasive breast carcinoma (Gill et al.
n3:mentions
n2:9865433
Subject Item
_:vb6199216
rdf:type
n3:Context
rdf:value
for developing breast carcinoma (Boyd et al., 1998; Boyd et al., 2001; McCormack & dos Santos Silva, 2006), making it one of the greatest independent risk factors for breast cancer (Boyd et al., 1998; McCormack & dos Santos Silva, >>2006<<). Ductal carcinoma in situ arises overwhelmingly in dense regions of the breast (Ursin et al., 2005), and high tissue density is associated with a greater risk for invasive breast carcinoma (Gill et al., 2006; Habel et al., 2004).
n3:mentions
n2:16775176
Subject Item
_:vb6199217
rdf:type
n3:Context
rdf:value
Ductal carcinoma in situ arises overwhelmingly in dense regions of the breast (Ursin et al., >>2005<<), and high tissue density is associated with a greater risk for invasive breast carcinoma (Gill et al., 2006; Habel et al., 2004).
n3:mentions
n2:16168104
Subject Item
_:vb6199218
rdf:type
n3:Context
rdf:value
Ductal carcinoma in situ arises overwhelmingly in dense regions of the breast (Ursin et al., 2005), and high tissue density is associated with a greater risk for invasive breast carcinoma (Gill et al., >>2006<<; Habel et al., 2004).
n3:mentions
n2:16796758
Subject Item
_:vb6199219
rdf:type
n3:Context
rdf:value
Ductal carcinoma in situ arises overwhelmingly in dense regions of the breast (Ursin et al., 2005), and high tissue density is associated with a greater risk for invasive breast carcinoma (Gill et al., 2006; Habel et al., >>2004<<). Importantly, areas of increased breast density are associated with significantly increased fibrillar collagen deposition (Alowami et al., 2003; Guo et al., 2001; Li et al., 2005). Yet, while there is considerable correlative data
n3:mentions
n2:15467036
Subject Item
_:vb6199220
rdf:type
n3:Context
rdf:value
Importantly, areas of increased breast density are associated with significantly increased fibrillar collagen deposition (Alowami et al., >>2003<<; Guo et al., 2001; Li et al., 2005).
n3:mentions
n2:12927043
Subject Item
_:vb6199221
rdf:type
n3:Context
rdf:value
Importantly, areas of increased breast density are associated with significantly increased fibrillar collagen deposition (Alowami et al., 2003; Guo et al., >>2001<<; Li et al., 2005).
n3:mentions
n2:11303594
Subject Item
_:vb6199222
rdf:type
n3:Context
rdf:value
Importantly, areas of increased breast density are associated with significantly increased fibrillar collagen deposition (Alowami et al., 2003; Guo et al., 2001; Li et al., >>2005<<). Yet, while there is considerable correlative data identifying breast density as a risk factor for developing carcinoma, and increased stromal collagen has been shown to promote mammary tumor formation in mice (Provenzano et al., 2008b),
n3:mentions
n2:15734956
Subject Item
_:vb6199223
rdf:type
n3:Context
rdf:value
Yet, while there is considerable correlative data identifying breast density as a risk factor for developing carcinoma, and increased stromal collagen has been shown to promote mammary tumor formation in mice (Provenzano et al., 2008b), the molecular mechanisms driving breast density-related tumor formation and progression remain largely unknown.
n3:mentions
n2:18442412
Subject Item
_:vb6199224
rdf:type
n3:Context
rdf:value
Moreover, large deformations can be inflicted during mammographic examination and while undergoing certain medical procedures (see (Plewes et al., >>2000<<; Samani et al., 2001)), yet the effects of these mechanical loads on the ductal epithelium are unknown.
n3:mentions
n2:10870713
Subject Item
_:vb6199225
rdf:type
n3:Context
rdf:value
Moreover, large deformations can be inflicted during mammographic examination and while undergoing certain medical procedures (see (Plewes et al., 2000; Samani et al., >>2001<<)), yet the effects of these mechanical loads on the ductal epithelium are unknown.
n3:mentions
n2:11370894
Subject Item
_:vb6199226
rdf:type
n3:Context
rdf:value
Further complicating this issue is the fact that breast adenomas and carcinomas are stiffer than normal tissue (Sarvazyan et al., 1995; Sumi et al., >>2000<<); increasing the mechanical load environment for adjacent cells (Krouskop et al., 1998; Plewes et al., 2000).
n3:mentions
n2:10870707
Subject Item
_:vb6199227
rdf:type
n3:Context
rdf:value
complicating this issue is the fact that breast adenomas and carcinomas are stiffer than normal tissue (Sarvazyan et al., 1995; Sumi et al., 2000); increasing the mechanical load environment for adjacent cells (Krouskop et al., >>1998<<; Plewes et al., 2000).
n3:mentions
n2:10197347
Subject Item
_:vb6199228
rdf:type
n3:Context
rdf:value
issue is the fact that breast adenomas and carcinomas are stiffer than normal tissue (Sarvazyan et al., 1995; Sumi et al., 2000); increasing the mechanical load environment for adjacent cells (Krouskop et al., 1998; Plewes et al., >>2000<<). Hence, an understudied aspect of the epithelial-stromal interaction is the fact that epithelial cells exist in a dynamic mechanical microenvironment, where dense collagenous stroma may increase force transmission to breast cells during
n3:mentions
n2:10870713
Subject Item
_:vb6199229
rdf:type
n3:Context
rdf:value
Consistently, such mechanical signals arising from the rigidity of the microenvironment have been shown to play a role in the transformed phenotype of breast epithelial cells in vitro (Paszek et al., >>2005<<; Wozniak et al., 2003).
n3:mentions
n2:16169468
Subject Item
_:vb6199230
rdf:type
n3:Context
rdf:value
Consistently, such mechanical signals arising from the rigidity of the microenvironment have been shown to play a role in the transformed phenotype of breast epithelial cells in vitro (Paszek et al., 2005; Wozniak et al., >>2003<<).
n3:mentions
n2:14610060
Subject Item
_:vb6199231
rdf:type
n3:Context
rdf:value
Focal adhesions (FAs) are sites of integrin-clustering that link the actin cytoskeleton to the extracellular matrix (ECM; (Burridge et al., >>1988<<)). The primary functions of these complexes are to offer physical attachment to the ECM, transduce force between the cell and its microenvironment, and operate as a scaffolding node from which multiple signaling cascades emanate to
n3:mentions
n2:3058164
Subject Item
_:vb6199232
rdf:type
n3:Context
rdf:value
ECM, transduce force between the cell and its microenvironment, and operate as a scaffolding node from which multiple signaling cascades emanate to regulate cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, >>1996<<; Geiger et al., 2001; Mitra et al., 2005; Playford & Schaller, 2004). It has been demonstrated that application of external force to adhesions or exposure to a “stiff” two-dimensional substrate promotes FA size and strength (Choquet et al.
n3:mentions
n2:8970735
Subject Item
_:vb6199233
rdf:type
n3:Context
rdf:value
between the cell and its microenvironment, and operate as a scaffolding node from which multiple signaling cascades emanate to regulate cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, 1996; Geiger et al., >>2001<<; Mitra et al., 2005; Playford & Schaller, 2004).
n3:mentions
n2:11715046
Subject Item
_:vb6199234
rdf:type
n3:Context
rdf:value
its microenvironment, and operate as a scaffolding node from which multiple signaling cascades emanate to regulate cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, 1996; Geiger et al., 2001; Mitra et al., >>2005<<; Playford & Schaller, 2004).
n3:mentions
n2:15688067
Subject Item
_:vb6199235
rdf:type
n3:Context
rdf:value
operate as a scaffolding node from which multiple signaling cascades emanate to regulate cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, 1996; Geiger et al., 2001; Mitra et al., 2005; Playford & Schaller, >>2004<<). It has been demonstrated that application of external force to adhesions or exposure to a “stiff” two-dimensional substrate promotes FA size and strength (Choquet et al., 1997; Galbraith et al., 2002; Pelham & Wang, 1997; Sniadecki et
n3:mentions
n2:15489911
Subject Item
_:vb6199236
rdf:type
n3:Context
rdf:value
It has been demonstrated that application of external force to adhesions or exposure to a “stiff” two-dimensional substrate promotes FA size and strength (Choquet et al., >>1997<<; Galbraith et al., 2002; Pelham & Wang, 1997; Sniadecki et al., 2007); and that Rho-dependent contractile force through the actin cytoskeleton promotes FA assembly (Chrzanowska-Wodnicka & Burridge, 1996; Ridley & Hall, 1992).
n3:mentions
n2:9019403
Subject Item
_:vb6199237
rdf:type
n3:Context
rdf:value
It has been demonstrated that application of external force to adhesions or exposure to a “stiff” two-dimensional substrate promotes FA size and strength (Choquet et al., 1997; Galbraith et al., >>2002<<; Pelham & Wang, 1997; Sniadecki et al., 2007); and that Rho-dependent contractile force through the actin cytoskeleton promotes FA assembly (Chrzanowska-Wodnicka & Burridge, 1996; Ridley & Hall, 1992).
n3:mentions
n2:12446745
Subject Item
_:vb6199238
rdf:type
n3:Context
rdf:value
It has been demonstrated that application of external force to adhesions or exposure to a “stiff” two-dimensional substrate promotes FA size and strength (Choquet et al., 1997; Galbraith et al., 2002; Pelham & Wang, >>1997<<; Sniadecki et al., 2007); and that Rho-dependent contractile force through the actin cytoskeleton promotes FA assembly (Chrzanowska-Wodnicka & Burridge, 1996; Ridley & Hall, 1992).
n3:mentions
n2:9391082
Subject Item
_:vb6199239
rdf:type
n3:Context
rdf:value
been demonstrated that application of external force to adhesions or exposure to a “stiff” two-dimensional substrate promotes FA size and strength (Choquet et al., 1997; Galbraith et al., 2002; Pelham & Wang, 1997; Sniadecki et al., >>2007<<); and that Rho-dependent contractile force through the actin cytoskeleton promotes FA assembly (Chrzanowska-Wodnicka & Burridge, 1996; Ridley & Hall, 1992).
n3:mentions
n2:17804810
Subject Item
_:vb6199240
rdf:type
n3:Context
rdf:value
and strength (Choquet et al., 1997; Galbraith et al., 2002; Pelham & Wang, 1997; Sniadecki et al., 2007); and that Rho-dependent contractile force through the actin cytoskeleton promotes FA assembly (Chrzanowska-Wodnicka & Burridge, >>1996<<; Ridley & Hall, 1992).
n3:mentions
n2:8682874
Subject Item
_:vb6199241
rdf:type
n3:Context
rdf:value
et al., 1997; Galbraith et al., 2002; Pelham & Wang, 1997; Sniadecki et al., 2007); and that Rho-dependent contractile force through the actin cytoskeleton promotes FA assembly (Chrzanowska-Wodnicka & Burridge, 1996; Ridley & Hall, >>1992<<). Furthermore, in fibroblasts, focal adhesion kinase (FAK), a key FA signaling molecule, is necessary for mechanosensing (Geiger et al., 2001; Mitra et al., 2005; Wang et al., 2001a) and becomes phosphorylated during cell deformation
n3:mentions
n2:1643657
Subject Item
_:vb6199242
rdf:type
n3:Context
rdf:value
Furthermore, in fibroblasts, focal adhesion kinase (FAK), a key FA signaling molecule, is necessary for mechanosensing (Geiger et al., >>2001<<; Mitra et al., 2005; Wang et al., 2001a) and becomes phosphorylated during cell deformation (Wang et al., 2001b).
n3:mentions
n2:11715046
Subject Item
_:vb6199243
rdf:type
n3:Context
rdf:value
Furthermore, in fibroblasts, focal adhesion kinase (FAK), a key FA signaling molecule, is necessary for mechanosensing (Geiger et al., 2001; Mitra et al., >>2005<<; Wang et al., 2001a) and becomes phosphorylated during cell deformation (Wang et al., 2001b).
n3:mentions
n2:15688067
Subject Item
_:vb6199244
rdf:type
n3:Context
rdf:value
Furthermore, in fibroblasts, focal adhesion kinase (FAK), a key FA signaling molecule, is necessary for mechanosensing (Geiger et al., 2001; Mitra et al., 2005; Wang et al., 2001a) and becomes phosphorylated during cell deformation (Wang et al., 2001b).
n3:mentions
n2:11572981
Subject Item
_:vb6199245
rdf:type
n3:Context
rdf:value
in fibroblasts, focal adhesion kinase (FAK), a key FA signaling molecule, is necessary for mechanosensing (Geiger et al., 2001; Mitra et al., 2005; Wang et al., 2001a) and becomes phosphorylated during cell deformation (Wang et al., 2001b). Fibroblast deformation promotes FAK activation through phosphorylation on Y397 and Y925, followed by FAK-dependent extracellular signal-regulated kinase (ERK) phosphorylation (Wang et al., 2001b) and proliferation (Wang et al., 2005).
n3:mentions
n2:11606050
Subject Item
_:vb6199246
rdf:type
n3:Context
rdf:value
Fibroblast deformation promotes FAK activation through phosphorylation on Y397 and Y925, followed by FAK-dependent extracellular signal-regulated kinase (ERK) phosphorylation (Wang et al., 2001b) and proliferation (Wang et al., 2005).
n3:mentions
n2:11606050
Subject Item
_:vb6199247
rdf:type
n3:Context
rdf:value
Fibroblast deformation promotes FAK activation through phosphorylation on Y397 and Y925, followed by FAK-dependent extracellular signal-regulated kinase (ERK) phosphorylation (Wang et al., 2001b) and proliferation (Wang et al., >>2005<<). FAK(Y397) phosphorylation creates a high-affinity site that is recognized by several Src-homology-2 (SH2) domain-containing proteins including Src and Shc (Schaller et al., 1994; Schlaepfer et al., 1998; Xing et al., 1994).
n3:mentions
n2:15808882
Subject Item
_:vb6199248
rdf:type
n3:Context
rdf:value
FAK(Y397) phosphorylation creates a high-affinity site that is recognized by several Src-homology-2 (SH2) domain-containing proteins including Src and Shc (Schaller et al., >>1994<<; Schlaepfer et al., 1998; Xing et al., 1994).
n3:mentions
n2:7509446
Subject Item
_:vb6199249
rdf:type
n3:Context
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FAK(Y397) phosphorylation creates a high-affinity site that is recognized by several Src-homology-2 (SH2) domain-containing proteins including Src and Shc (Schaller et al., 1994; Schlaepfer et al., >>1998<<; Xing et al., 1994).
n3:mentions
n2:9566877
Subject Item
_:vb6199250
rdf:type
n3:Context
rdf:value
FAK(Y397) phosphorylation creates a high-affinity site that is recognized by several Src-homology-2 (SH2) domain-containing proteins including Src and Shc (Schaller et al., 1994; Schlaepfer et al., 1998; Xing et al., >>1994<<). Moreover, FAK Y925 phosphorylation by Src promotes Grb2-FAK interactions which, along with Shc, link FAK to the Ras pathway (Schlaepfer & Hunter, 1996; Schlaepfer et al., 1998). Combined, these studies suggest that the force balance at
n3:mentions
n2:8054685
Subject Item
_:vb6199251
rdf:type
n3:Context
rdf:value
Moreover, FAK Y925 phosphorylation by Src promotes Grb2-FAK interactions which, along with Shc, link FAK to the Ras pathway (Schlaepfer & Hunter, >>1996<<; Schlaepfer et al., 1998).
n3:mentions
n2:8816475
Subject Item
_:vb6199252
rdf:type
n3:Context
rdf:value
Moreover, FAK Y925 phosphorylation by Src promotes Grb2-FAK interactions which, along with Shc, link FAK to the Ras pathway (Schlaepfer & Hunter, 1996; Schlaepfer et al., >>1998<<). Combined, these studies suggest that the force balance at the cell-matrix junction influences matrix adhesion structure and signaling, and that a functional linkage between FAK, Rho, and ERK exists.
n3:mentions
n2:9566877
Subject Item
_:vb6199253
rdf:type
n3:Context
rdf:value
Importantly, increased breast density is associated with increased epithelial cellularity (Guo et al., >>2001<<; Li et al., 2005) and one prevailing hypotheses for breast density-related carcinoma risk centers on increased epithelial growth that is susceptible to increased mutagenic damage (Martin & Boyd, 2008).
n3:mentions
n2:11303594
Subject Item
_:vb6199254
rdf:type
n3:Context
rdf:value
Importantly, increased breast density is associated with increased epithelial cellularity (Guo et al., 2001; Li et al., >>2005<<) and one prevailing hypotheses for breast density-related carcinoma risk centers on increased epithelial growth that is susceptible to increased mutagenic damage (Martin & Boyd, 2008).
n3:mentions
n2:15734956
Subject Item
_:vb6199255
rdf:type
n3:Context
rdf:value
cellularity (Guo et al., 2001; Li et al., 2005) and one prevailing hypotheses for breast density-related carcinoma risk centers on increased epithelial growth that is susceptible to increased mutagenic damage (Martin & Boyd, >>2008<<). As such, we set out to determine if increased collagen matrix density per se, in the absence of stromal cells, was sufficient to alter nontransformed breast cell growth and promote cellular proliferation and invasion.
n3:mentions
n2:18226174
Subject Item
_:vb6199256
rdf:type
n3:Context
rdf:value
While previous work by Paszek and co-workers (Paszek et al., >>2005<<) elegantly showed that changing substrate stiffness can regulate epithelial phenotype, the molecular mechanisms associated with collagen matrix density-induced mechanoregulation remain largely unknown.
n3:mentions
n2:16169468
Subject Item
_:vb6199257
rdf:type
n5:Section
dc:title
materials and methods
n5:contains
_:vb6199258 _:vb6199259 _:vb6199260 _:vb6199261 _:vb6199262 _:vb6199263 _:vb6199264 _:vb6199265 _:vb6199266 _:vb6199267 _:vb6199268
Subject Item
_:vb6199258
rdf:type
n3:Context
rdf:value
MCF10A T47D, MDA-MB-231, and NMuMG mammary epithelial cells (MECs) were maintained as described previously (Provenzano et al., 2008c; Wozniak et al., >>2003<<). Each cell type had an optimal collagen density for promoting tubulogenesis that was determined through preliminary experiments.
n3:mentions
n2:14610060
Subject Item
_:vb6199259
rdf:type
n3:Context
rdf:value
Polyacrylamide substrates were prepared as described by Pelham and Wang (Pelham & Wang, >>1997<<) and Yeung et al., (Yeung et al., 2005).
n3:mentions
n2:9391082
Subject Item
_:vb6199260
rdf:type
n3:Context
rdf:value
Polyacrylamide substrates were prepared as described by Pelham and Wang (Pelham & Wang, 1997) and Yeung et al., (Yeung et al., >>2005<<).
n3:mentions
n2:15573414
Subject Item
_:vb6199261
rdf:type
n3:Context
rdf:value
Multiphoton excitation and SHG imaging microscopy were performed as previously described (Provenzano et al., 2008b; Provenzano et al., 2008c).
n3:mentions
n2:18442412
Subject Item
_:vb6199262
rdf:type
n3:Context
rdf:value
Mechanical testing to generate stress-strain data for collagen matrices was performed as described previously (Provenzano et al., >>2003<<) using sample design similar to (Roeder et al., 2002).
n3:mentions
n2:12391134
Subject Item
_:vb6199263
rdf:type
n3:Context
rdf:value
Mechanical testing to generate stress-strain data for collagen matrices was performed as described previously (Provenzano et al., 2003) using sample design similar to (Roeder et al., >>2002<<).
n3:mentions
n2:12002131
Subject Item
_:vb6199264
rdf:type
n3:Context
rdf:value
Immunofluorescence microscopy of cells was performed as described previously (Provenzano et al., 2008b; Wozniak et al., 2003).
n3:mentions
n2:18442412
Subject Item
_:vb6199265
rdf:type
n3:Context
rdf:value
Immunofluorescence microscopy of cells was performed as described previously (Provenzano et al., 2008b; Wozniak et al., >>2003<<).
n3:mentions
n2:14610060
Subject Item
_:vb6199266
rdf:type
n3:Context
rdf:value
Western blotting was performed as described previously (Provenzano et al., 2008a).
n3:mentions
n2:18845837
Subject Item
_:vb6199267
rdf:type
n3:Context
rdf:value
Total RNA was isolated from mammary epithelial cells in 3D collagen matrices (LD, n=5; HD, n=5; HD+DMSO, n=5; HD+U0126, n=5) in a manner similar to a previous report (Provenzano et al., 2008a).
n3:mentions
n2:18845837
Subject Item
_:vb6199268
rdf:type
n3:Context
rdf:value
Analysis was performed as previously described (Provenzano et al., 2008a).
n3:mentions
n2:18845837
Subject Item
_:vb6199269
rdf:type
n5:Section
dc:title
results
n5:contains
_:vb6199280 _:vb6199281 _:vb6199282 _:vb6199283 _:vb6199284 _:vb6199285 _:vb6199286 _:vb6199287 _:vb6199288 _:vb6199289 _:vb6199290 _:vb6199291 _:vb6199292 _:vb6199293 _:vb6199294 _:vb6199295 _:vb6199270 _:vb6199271 _:vb6199272 _:vb6199273 _:vb6199274 _:vb6199275 _:vb6199276 _:vb6199277 _:vb6199278 _:vb6199279 _:vb6199312 _:vb6199313 _:vb6199296 _:vb6199297 _:vb6199298 _:vb6199299 _:vb6199300 _:vb6199301 _:vb6199302 _:vb6199303 _:vb6199304 _:vb6199305 _:vb6199306 _:vb6199307 _:vb6199308 _:vb6199309 _:vb6199310 _:vb6199311
Subject Item
_:vb6199270
rdf:type
n3:Context
rdf:value
Although it has been shown that increased collagen matrix density in three-dimensional (3D) culture disrupts tubulogenesis of T47D breast carcinoma cells (Wozniak et al., >>2003<<) and normal acini formation of MCF10A cells (Paszek et al., 2005), the effects of increased collagen density on tubule structures from nontransformed mammary epithelial cells (MECs) has not been examined.
n3:mentions
n2:14610060
Subject Item
_:vb6199271
rdf:type
n3:Context
rdf:value
it has been shown that increased collagen matrix density in three-dimensional (3D) culture disrupts tubulogenesis of T47D breast carcinoma cells (Wozniak et al., 2003) and normal acini formation of MCF10A cells (Paszek et al., >>2005<<), the effects of increased collagen density on tubule structures from nontransformed mammary epithelial cells (MECs) has not been examined.
n3:mentions
n2:16169468
Subject Item
_:vb6199272
rdf:type
n3:Context
rdf:value
Using 3D culture models, it has been shown that integrin-containing adhesions play a significant role in regulating epithelial phenotype (Keely et al., >>1995<<; Weaver et al., 1997). Moreover, FAK is overexpressed in human breast cancer (Cance et al., 2000) and is necessary for mammary tumor growth and progression (Lahlou et al., 2007; Provenzano et al., 2008a).
n3:mentions
n2:7769004
Subject Item
_:vb6199273
rdf:type
n3:Context
rdf:value
Using 3D culture models, it has been shown that integrin-containing adhesions play a significant role in regulating epithelial phenotype (Keely et al., 1995; Weaver et al., >>1997<<). Moreover, FAK is overexpressed in human breast cancer (Cance et al., 2000) and is necessary for mammary tumor growth and progression (Lahlou et al., 2007; Provenzano et al., 2008a).
n3:mentions
n2:9105051
Subject Item
_:vb6199274
rdf:type
n3:Context
rdf:value
Moreover, FAK is overexpressed in human breast cancer (Cance et al., >>2000<<) and is necessary for mammary tumor growth and progression (Lahlou et al., 2007; Provenzano et al., 2008a).
n3:mentions
n2:10873094
Subject Item
_:vb6199275
rdf:type
n3:Context
rdf:value
Moreover, FAK is overexpressed in human breast cancer (Cance et al., 2000) and is necessary for mammary tumor growth and progression (Lahlou et al., >>2007<<; Provenzano et al., 2008a).
n3:mentions
n2:18056629
Subject Item
_:vb6199276
rdf:type
n3:Context
rdf:value
Moreover, FAK is overexpressed in human breast cancer (Cance et al., 2000) and is necessary for mammary tumor growth and progression (Lahlou et al., 2007; Provenzano et al., 2008a). Since FAK is also required for mechanosensing and influences cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, 1996; Geiger et al., 2001; Mitra et al., 2005; Playford & Schaller, 2004), we examined the state
n3:mentions
n2:18845837
Subject Item
_:vb6199277
rdf:type
n3:Context
rdf:value
Since FAK is also required for mechanosensing and influences cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, >>1996<<; Geiger et al., 2001; Mitra et al., 2005; Playford & Schaller, 2004), we examined the state of FAK as a function of tissue stiffness.
n3:mentions
n2:8970735
Subject Item
_:vb6199278
rdf:type
n3:Context
rdf:value
Since FAK is also required for mechanosensing and influences cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, 1996; Geiger et al., >>2001<<; Mitra et al., 2005; Playford & Schaller, 2004), we examined the state of FAK as a function of tissue stiffness.
n3:mentions
n2:11715046
Subject Item
_:vb6199279
rdf:type
n3:Context
rdf:value
Since FAK is also required for mechanosensing and influences cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, 1996; Geiger et al., 2001; Mitra et al., >>2005<<; Playford & Schaller, 2004), we examined the state of FAK as a function of tissue stiffness.
n3:mentions
n2:15688067
Subject Item
_:vb6199280
rdf:type
n3:Context
rdf:value
Since FAK is also required for mechanosensing and influences cell proliferation, survival, and migration (Burridge & Chrzanowska-Wodnicka, 1996; Geiger et al., 2001; Mitra et al., 2005; Playford & Schaller, >>2004<<), we examined the state of FAK as a function of tissue stiffness.
n3:mentions
n2:15489911
Subject Item
_:vb6199281
rdf:type
n3:Context
rdf:value
FA signaling can lead to Rho activation that promotes myosin light chain (MLC)-mediated intracellular contractile force, which further promotes focal adhesion clustering and maturation (Choquet et al., >>1997<<; Chrzanowska-Wodnicka & Burridge, 1996; Galbraith et al., 2002; Riveline et al., 2001).
n3:mentions
n2:9019403
Subject Item
_:vb6199282
rdf:type
n3:Context
rdf:value
can lead to Rho activation that promotes myosin light chain (MLC)-mediated intracellular contractile force, which further promotes focal adhesion clustering and maturation (Choquet et al., 1997; Chrzanowska-Wodnicka & Burridge, >>1996<<; Galbraith et al., 2002; Riveline et al., 2001). Herein, the presence of actin stress fibers in Figure 2, suggests increased Rho activity in response to mechanical signals.
n3:mentions
n2:8682874
Subject Item
_:vb6199283
rdf:type
n3:Context
rdf:value
that promotes myosin light chain (MLC)-mediated intracellular contractile force, which further promotes focal adhesion clustering and maturation (Choquet et al., 1997; Chrzanowska-Wodnicka & Burridge, 1996; Galbraith et al., >>2002<<; Riveline et al., 2001). Herein, the presence of actin stress fibers in Figure 2, suggests increased Rho activity in response to mechanical signals.
n3:mentions
n2:12446745
Subject Item
_:vb6199284
rdf:type
n3:Context
rdf:value
myosin light chain (MLC)-mediated intracellular contractile force, which further promotes focal adhesion clustering and maturation (Choquet et al., 1997; Chrzanowska-Wodnicka & Burridge, 1996; Galbraith et al., 2002; Riveline et al., >>2001<<). Herein, the presence of actin stress fibers in Figure 2, suggests increased Rho activity in response to mechanical signals.
n3:mentions
n2:11402062
Subject Item
_:vb6199285
rdf:type
n3:Context
rdf:value
in 3D matrices, previous studies have utilized cells either stably expressing Rho/ROCK mutants or under continuous pharmacological inhibition of the Rho-ROCK pathway to study morphogenesis of epithelial tubules (Wozniak et al., >>2003<<) or acini (Paszek et al., 2005).
n3:mentions
n2:14610060
Subject Item
_:vb6199286
rdf:type
n3:Context
rdf:value
studies have utilized cells either stably expressing Rho/ROCK mutants or under continuous pharmacological inhibition of the Rho-ROCK pathway to study morphogenesis of epithelial tubules (Wozniak et al., 2003) or acini (Paszek et al., >>2005<<). Herein, we set out to test whether Rho-mediated contractility was necessary to maintain the invasive phenotype associated with elevated isometric tension, by allowing the invasive phenotype to form and then selectively inhibiting the
n3:mentions
n2:16169468
Subject Item
_:vb6199287
rdf:type
n3:Context
rdf:value
High breast tissue density in human patients is associated with increased epithelial content (Guo et al., >>2001<<; Li et al., 2005) suggesting that high density promotes epithelial growth and/or survival.
n3:mentions
n2:11303594
Subject Item
_:vb6199288
rdf:type
n3:Context
rdf:value
High breast tissue density in human patients is associated with increased epithelial content (Guo et al., 2001; Li et al., >>2005<<) suggesting that high density promotes epithelial growth and/or survival. Herein, we observed that epithelial colonies were larger and more cell-dense in HD matrices, suggesting a more proliferative phenotype (Supp.
n3:mentions
n2:15734956
Subject Item
_:vb6199289
rdf:type
n3:Context
rdf:value
with statistical gene ontology enrichment analysis, produced two clusters associated with proliferation (Fig 5C and D), with each cluster containing genes known to be important for breast carcinoma proliferation (Whitfield et al., >>2006<<). In fact, the full set of genes previously identified as the human breast carcinoma-associated “proliferation signature” (Whitfield et al., 2006), which predicts survival and metastasis-free outcome in human patients (Fig.
n3:mentions
n2:16491069
Subject Item
_:vb6199290
rdf:type
n3:Context
rdf:value
In fact, the full set of genes previously identified as the human breast carcinoma-associated “proliferation signature” (Whitfield et al., >>2006<<), which predicts survival and metastasis-free outcome in human patients (Fig.
n3:mentions
n2:16491069
Subject Item
_:vb6199291
rdf:type
n3:Context
rdf:value
This finding is consistent with previous data showing increased tumor formation in transgenic mice possessing increased stromal collagen (Provenzano et al., 2008b), and confirms that increased collagen density promotes proliferation in both nontransformed and transformed MECs.
n3:mentions
n2:18442412
Subject Item
_:vb6199292
rdf:type
n3:Context
rdf:value
The ERK/mitogen-activated protein kinase (MAPK) pathway has been implicated in multiple cellular processes such as proliferation, migration and apoptosis (Dhillon et al., >>2007<<; Turjanski et al., 2007; Yoon & Seger, 2006).
n3:mentions
n2:17496922
Subject Item
_:vb6199293
rdf:type
n3:Context
rdf:value
The ERK/mitogen-activated protein kinase (MAPK) pathway has been implicated in multiple cellular processes such as proliferation, migration and apoptosis (Dhillon et al., 2007; Turjanski et al., >>2007<<; Yoon & Seger, 2006).
n3:mentions
n2:17496919
Subject Item
_:vb6199294
rdf:type
n3:Context
rdf:value
The ERK/mitogen-activated protein kinase (MAPK) pathway has been implicated in multiple cellular processes such as proliferation, migration and apoptosis (Dhillon et al., 2007; Turjanski et al., 2007; Yoon & Seger, >>2006<<). Activation of ERK1/2 is sufficient to transform NIH 3T3 cells (Mansour et al., 1994) and pro-growth signals in many human cancers result from hyper-activation of the ERK pathway due to mutation/overexpression of ERK pathway-regulating
n3:mentions
n2:16393692
Subject Item
_:vb6199295
rdf:type
n3:Context
rdf:value
Activation of ERK1/2 is sufficient to transform NIH 3T3 cells (Mansour et al., >>1994<<) and pro-growth signals in many human cancers result from hyper-activation of the ERK pathway due to mutation/overexpression of ERK pathway-regulating molecules, such as Ras, receptor tyrosine kinases, or integrins (Dhillon et al., 2007;
n3:mentions
n2:8052857
Subject Item
_:vb6199296
rdf:type
n3:Context
rdf:value
and pro-growth signals in many human cancers result from hyper-activation of the ERK pathway due to mutation/overexpression of ERK pathway-regulating molecules, such as Ras, receptor tyrosine kinases, or integrins (Dhillon et al., >>2007<<; Giancotti & Ruoslahti, 1999; Turjanski et al., 2007).
n3:mentions
n2:17496922
Subject Item
_:vb6199297
rdf:type
n3:Context
rdf:value
many human cancers result from hyper-activation of the ERK pathway due to mutation/overexpression of ERK pathway-regulating molecules, such as Ras, receptor tyrosine kinases, or integrins (Dhillon et al., 2007; Giancotti & Ruoslahti, >>1999<<; Turjanski et al., 2007).
n3:mentions
n2:10446041
Subject Item
_:vb6199298
rdf:type
n3:Context
rdf:value
from hyper-activation of the ERK pathway due to mutation/overexpression of ERK pathway-regulating molecules, such as Ras, receptor tyrosine kinases, or integrins (Dhillon et al., 2007; Giancotti & Ruoslahti, 1999; Turjanski et al., >>2007<<). Furthermore, while work by Paszek et al., (Paszek et al., 2005) showed that in MECs on stiffer basement membrane-coated polyacryamide gels have higher ERK-2 activity in response to EGF stimulation, it is currently not known if changes
n3:mentions
n2:17496919
Subject Item
_:vb6199299
rdf:type
n3:Context
rdf:value
Furthermore, while work by Paszek et al., (Paszek et al., >>2005<<) showed that in MECs on stiffer basement membrane-coated polyacryamide gels have higher ERK-2 activity in response to EGF stimulation, it is currently not known if changes in the mechanical 3D-microenvironment influence proliferation by
n3:mentions
n2:16169468
Subject Item
_:vb6199300
rdf:type
n3:Context
rdf:value
This effect of MEK/ERK inhibition was possibly through ERK’s regulation of MLC phosphorylation by MLC kinase (Klemke et al., >>1997<<), as this result is consistent with the phenotypic reversion observed following treatment with blebbistatin (Fig 4F).
n3:mentions
n2:9128257
Subject Item
_:vb6199301
rdf:type
n3:Context
rdf:value
Activated ERK translocates to the nucleus where ERK can regulate the activity of transcription factors to alter gene expression (Dhillon et al., >>2007<<; Turjanski et al., 2007; Yoon & Seger, 2006). Of particular relevance to the malignant phenotype, sustained ERK activation promotes entry into, and progression through, the cell cycle (Chambard et al., 2007; Dhillon et al., 2007).
n3:mentions
n2:17496922
Subject Item
_:vb6199302
rdf:type
n3:Context
rdf:value
Activated ERK translocates to the nucleus where ERK can regulate the activity of transcription factors to alter gene expression (Dhillon et al., 2007; Turjanski et al., >>2007<<; Yoon & Seger, 2006). Of particular relevance to the malignant phenotype, sustained ERK activation promotes entry into, and progression through, the cell cycle (Chambard et al., 2007; Dhillon et al., 2007).
n3:mentions
n2:17496919
Subject Item
_:vb6199303
rdf:type
n3:Context
rdf:value
Activated ERK translocates to the nucleus where ERK can regulate the activity of transcription factors to alter gene expression (Dhillon et al., 2007; Turjanski et al., 2007; Yoon & Seger, >>2006<<). Of particular relevance to the malignant phenotype, sustained ERK activation promotes entry into, and progression through, the cell cycle (Chambard et al., 2007; Dhillon et al., 2007).
n3:mentions
n2:16393692
Subject Item
_:vb6199304
rdf:type
n3:Context
rdf:value
Of particular relevance to the malignant phenotype, sustained ERK activation promotes entry into, and progression through, the cell cycle (Chambard et al., >>2007<<; Dhillon et al., 2007).
n3:mentions
n2:17188374
Subject Item
_:vb6199305
rdf:type
n3:Context
rdf:value
Of particular relevance to the malignant phenotype, sustained ERK activation promotes entry into, and progression through, the cell cycle (Chambard et al., 2007; Dhillon et al., >>2007<<). Since ERK inhibition repressed both proliferation and the invasive phenotype of MECs in stiff matrices, we speculated that loss of ERK activity would have a profound effect on the transcriptome, particularly genes associated with
n3:mentions
n2:17496922
Subject Item
_:vb6199306
rdf:type
n3:Context
rdf:value
ERK regulated transcription factors (Sp1, HNF4, p53, Spz1, Zic1-3, Pax4, Stat6, and AP4) were previously identified as part of a conserved set of TFs in FAK-regulated mammary carcinoma proliferation and metastasis (Provenzano et al., 2008a). In particular, we previously found that expression of genes associated with the G2-G2/M phases of the cell cycle were regulated by FAK through predicted TFBS for Sp1, p53, p300/CBP, AP4, HNF4, Lmo2-complex, Spz1, Zic1-3, AP2α, Stat6,
n3:mentions
n2:18845837
Subject Item
_:vb6199307
rdf:type
n3:Context
rdf:value
In addition, ERK is predicted to regulate TFs associated with earlier phases of the cell cycle (such as E2F, c-Myb, Elk-1; (Chambard et al., >>2007<<; Oh & Reddy, 1999)), consistent with our finding that ERK inhibition resulted in reduced expression of genes associated with each phase of the cell cycle (Table 1).
n3:mentions
n2:17188374
Subject Item
_:vb6199308
rdf:type
n3:Context
rdf:value
In addition, ERK is predicted to regulate TFs associated with earlier phases of the cell cycle (such as E2F, c-Myb, Elk-1; (Chambard et al., 2007; Oh & Reddy, >>1999<<)), consistent with our finding that ERK inhibition resulted in reduced expression of genes associated with each phase of the cell cycle (Table 1).
n3:mentions
n2:10378697
Subject Item
_:vb6199309
rdf:type
n3:Context
rdf:value
FAK phosphorylation at Y397 creates a high-affinity site recognized by SH2 domain-containing proteins Src and Shc (Schaller et al., >>1994<<; Schlaepfer et al., 1998; Xing et al., 1994). Subsequent phosphorylation at Y925 by Src promotes Grb2-FAK interactions which, along with Shc, link FAK to the Ras pathway in fibroblasts (Schlaepfer & Hunter, 1996; Schlaepfer et al., 1998).
n3:mentions
n2:7509446
Subject Item
_:vb6199310
rdf:type
n3:Context
rdf:value
FAK phosphorylation at Y397 creates a high-affinity site recognized by SH2 domain-containing proteins Src and Shc (Schaller et al., 1994; Schlaepfer et al., >>1998<<; Xing et al., 1994). Subsequent phosphorylation at Y925 by Src promotes Grb2-FAK interactions which, along with Shc, link FAK to the Ras pathway in fibroblasts (Schlaepfer & Hunter, 1996; Schlaepfer et al., 1998).
n3:mentions
n2:9566877
Subject Item
_:vb6199311
rdf:type
n3:Context
rdf:value
FAK phosphorylation at Y397 creates a high-affinity site recognized by SH2 domain-containing proteins Src and Shc (Schaller et al., 1994; Schlaepfer et al., 1998; Xing et al., >>1994<<). Subsequent phosphorylation at Y925 by Src promotes Grb2-FAK interactions which, along with Shc, link FAK to the Ras pathway in fibroblasts (Schlaepfer & Hunter, 1996; Schlaepfer et al., 1998).
n3:mentions
n2:8054685
Subject Item
_:vb6199312
rdf:type
n3:Context
rdf:value
Subsequent phosphorylation at Y925 by Src promotes Grb2-FAK interactions which, along with Shc, link FAK to the Ras pathway in fibroblasts (Schlaepfer & Hunter, >>1996<<; Schlaepfer et al., 1998).
n3:mentions
n2:8816475
Subject Item
_:vb6199313
rdf:type
n3:Context
rdf:value
Subsequent phosphorylation at Y925 by Src promotes Grb2-FAK interactions which, along with Shc, link FAK to the Ras pathway in fibroblasts (Schlaepfer & Hunter, 1996; Schlaepfer et al., >>1998<<). To determine if ERK is regulated by FAK in MECs, we manipulated FAK activity by expressing FRNK, a dominant-negative C-terminal region of FAK. FRNK expression (confirmed with antibodies specific for the C-terminal region of FAK)
n3:mentions
n2:9566877
Subject Item
_:vb6199314
rdf:type
n5:Section
dc:title
discussion
n5:contains
_:vb6199336 _:vb6199332 _:vb6199333 _:vb6199334 _:vb6199335 _:vb6199328 _:vb6199329 _:vb6199330 _:vb6199331 _:vb6199324 _:vb6199325 _:vb6199326 _:vb6199327 _:vb6199320 _:vb6199321 _:vb6199322 _:vb6199323 _:vb6199316 _:vb6199317 _:vb6199318 _:vb6199319 _:vb6199315
Subject Item
_:vb6199315
rdf:type
n3:Context
rdf:value
High breast tissue density may account for up to 30% of breast cancers (Boyd et al., >>1998<<; Boyd et al., 2001; McCormack & dos Santos Silva, 2006), yet the molecular mechanisms driving this increased risk are not known.
n3:mentions
n2:9865433
Subject Item
_:vb6199316
rdf:type
n3:Context
rdf:value
High breast tissue density may account for up to 30% of breast cancers (Boyd et al., 1998; Boyd et al., >>2001<<; McCormack & dos Santos Silva, 2006), yet the molecular mechanisms driving this increased risk are not known.
n3:mentions
n2:11389815
Subject Item
_:vb6199317
rdf:type
n3:Context
rdf:value
High breast tissue density may account for up to 30% of breast cancers (Boyd et al., 1998; Boyd et al., 2001; McCormack & dos Santos Silva, >>2006<<), yet the molecular mechanisms driving this increased risk are not known.
n3:mentions
n2:16775176
Subject Item
_:vb6199318
rdf:type
n3:Context
rdf:value
Importantly, increased breast density is not only associated with increased epithelial and stromal cellularity but also significantly increased collagen deposition (Alowami et al., >>2003<<; Guo et al., 2001; Li et al., 2005).
n3:mentions
n2:12927043
Subject Item
_:vb6199319
rdf:type
n3:Context
rdf:value
Importantly, increased breast density is not only associated with increased epithelial and stromal cellularity but also significantly increased collagen deposition (Alowami et al., 2003; Guo et al., >>2001<<; Li et al., 2005).
n3:mentions
n2:11303594
Subject Item
_:vb6199320
rdf:type
n3:Context
rdf:value
Importantly, increased breast density is not only associated with increased epithelial and stromal cellularity but also significantly increased collagen deposition (Alowami et al., 2003; Guo et al., 2001; Li et al., >>2005<<). Therefore, although stromal cell populations (fibroblasts, macrophages, etc.) likely contribute to carcinoma formation and progression in dense breast tissue, the focus of the current study was to examine the influence of stromal
n3:mentions
n2:15734956
Subject Item
_:vb6199321
rdf:type
n3:Context
rdf:value
Of direct relevance to our findings are recent reports showing that increased resistance to cell contraction promotes a malignant phenotype (Paszek et al., >>2005<<; Wozniak et al., 2003).
n3:mentions
n2:16169468
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Of direct relevance to our findings are recent reports showing that increased resistance to cell contraction promotes a malignant phenotype (Paszek et al., 2005; Wozniak et al., >>2003<<). Supportive of results shown herein, Paszek and co-workers (Paszek et al., 2005) showed that increasing substrate stiffness promotes integrin clustering and FA signaling, and that inhibition of ERK reverts aberrant phenotype due to
n3:mentions
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Supportive of results shown herein, Paszek and co-workers (Paszek et al., >>2005<<) showed that increasing substrate stiffness promotes integrin clustering and FA signaling, and that inhibition of ERK reverts aberrant phenotype due to constitutive-activation of Rho in soft basement membrane gels.
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Additionally, using unconfined compression testing to determine ECM material properties, the authors (Paszek et al., >>2005<<) showed that increasing collagen concentration (in mixed collagen/basement membrane gels) increased matrix stiffness, which is consistent with results presented herein and data from Roeder and co-workers (Roeder et al., 2002) using
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et al., 2005) showed that increasing collagen concentration (in mixed collagen/basement membrane gels) increased matrix stiffness, which is consistent with results presented herein and data from Roeder and co-workers (Roeder et al., >>2002<<) using tensile testing to determine the elastic modulus.
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in the tensile direction since it is well established that collagen is predominantly a tensile load bearing protein, with groups of organized fibrils mounting minimal resistance to compression or free bending ((Provenzano & Vanderby, >>2006<<) and references therein). Moreover, when cells contract inside the matrix they face resistance from collagen deformed in the tensile direction (Provenzano et al., 2008c).
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Hence, it is clear that the data shown here, and in previous studies (Paszek et al., >>2005<<; Wozniak et al., 2003), provide compelling evidence that mechanical signals have a profound influence on epithelial behavior and can promote a malignant phenotype.
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Hence, it is clear that the data shown here, and in previous studies (Paszek et al., 2005; Wozniak et al., >>2003<<), provide compelling evidence that mechanical signals have a profound influence on epithelial behavior and can promote a malignant phenotype.
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Data suggest that MECs respond to stiff matrices with a phenotype and gene expression program consistent with malignant transformation and the in vivo phenotype associated with human breast tissue density (Boyd et al., >>1998<<; Boyd et al., 2001; Gill et al., 2006; Habel et al., 2004; McCormack & dos Santos Silva, 2006).
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suggest that MECs respond to stiff matrices with a phenotype and gene expression program consistent with malignant transformation and the in vivo phenotype associated with human breast tissue density (Boyd et al., 1998; Boyd et al., >>2001<<; Gill et al., 2006; Habel et al., 2004; McCormack & dos Santos Silva, 2006).
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respond to stiff matrices with a phenotype and gene expression program consistent with malignant transformation and the in vivo phenotype associated with human breast tissue density (Boyd et al., 1998; Boyd et al., 2001; Gill et al., >>2006<<; Habel et al., 2004; McCormack & dos Santos Silva, 2006).
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with a phenotype and gene expression program consistent with malignant transformation and the in vivo phenotype associated with human breast tissue density (Boyd et al., 1998; Boyd et al., 2001; Gill et al., 2006; Habel et al., >>2004<<; McCormack & dos Santos Silva, 2006).
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program consistent with malignant transformation and the in vivo phenotype associated with human breast tissue density (Boyd et al., 1998; Boyd et al., 2001; Gill et al., 2006; Habel et al., 2004; McCormack & dos Santos Silva, >>2006<<). While the in vivo condition is likely more complex, with stromal fibroblasts also stimulated to proliferate by dense matrices and contributing in a feed-forward manner to matrix density and aberrant epithelial behavior, we propose that
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In this capacity, ERK serves as a linkage between cell surface receptors and distinctly regulated intracellular targets (Dhillon et al., >>2007<<; Yoon & Seger, 2006).
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In this capacity, ERK serves as a linkage between cell surface receptors and distinctly regulated intracellular targets (Dhillon et al., 2007; Yoon & Seger, >>2006<<). Therefore, in order to carry out the task of regulating a complex variety of intracellular functions, ERK directly interacts with more than 160 known substrates (Yoon & Seger, 2006). Moreover, the MAPK cascade, in total, influences an
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Therefore, in order to carry out the task of regulating a complex variety of intracellular functions, ERK directly interacts with more than 160 known substrates (Yoon & Seger, >>2006<<). Moreover, the MAPK cascade, in total, influences an even greater number of molecules and pathways. In the current work, we demonstrate that ERK functions as a central regulator of transcriptional response to mechanical signals. By
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