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n3:pmcid
PMC0
bibo:doi
10.1083%2Fjcb.200704042
n5:contains
_:vb2997557 _:vb2997627 _:vb2997603 _:vb2997588
Subject Item
_:vb2997557
rdf:type
n5:Section
dc:title
introduction
n5:contains
_:vb2997558 _:vb2997559 _:vb2997560 _:vb2997561 _:vb2997562 _:vb2997563 _:vb2997564 _:vb2997565 _:vb2997566 _:vb2997567 _:vb2997584 _:vb2997585 _:vb2997586 _:vb2997587 _:vb2997568 _:vb2997569 _:vb2997570 _:vb2997571 _:vb2997572 _:vb2997573 _:vb2997574 _:vb2997575 _:vb2997576 _:vb2997577 _:vb2997578 _:vb2997579 _:vb2997580 _:vb2997581 _:vb2997582 _:vb2997583
Subject Item
_:vb2997558
rdf:type
n3:Context
rdf:value
The development of tension by myofibroblasts (Mfs) promotes physiological tissue repair for which the contracting granulation tissue of healing wounds is a paradigm (Hinz, >>2007<<). However, the excessive ECM-secreting and contractile activities of Mfs contribute to progressive fibrosis in many organs, such as the heart, lung, liver, kidney, and skin (Gabbiani, 2003; Hinz et al., 2007).
n3:mentions
n2:17299435
Subject Item
_:vb2997559
rdf:type
n3:Context
rdf:value
However, the excessive ECM-secreting and contractile activities of Mfs contribute to progressive fibrosis in many organs, such as the heart, lung, liver, kidney, and skin (Gabbiani, >>2003<<; Hinz et al., 2007).
n3:mentions
n2:12845617
Subject Item
_:vb2997560
rdf:type
n3:Context
rdf:value
However, the excessive ECM-secreting and contractile activities of Mfs contribute to progressive fibrosis in many organs, such as the heart, lung, liver, kidney, and skin (Gabbiani, 2003; Hinz et al., >>2007<<). The high contractile activity of Mfs is generated by α smooth muscle actin (α-SMA) in stress fibers, which are hallmarks of a differentiated Mf (Tomasek et al., 2002). Interfering with α-SMA action by adding a membrane-penetrating
n3:mentions
n2:17525249
Subject Item
_:vb2997561
rdf:type
n3:Context
rdf:value
The high contractile activity of Mfs is generated by α smooth muscle actin (α-SMA) in stress fibers, which are hallmarks of a differentiated Mf (Tomasek et al., >>2002<<). Interfering with α-SMA action by adding a membrane-penetrating fusion protein that contains the α-SMA–specific N-terminal sequence AcEEED (SMA-FP) significantly reduces tension generation by Mfs (Hinz et al., 2002).
n3:mentions
n2:11988769
Subject Item
_:vb2997562
rdf:type
n3:Context
rdf:value
Interfering with α-SMA action by adding a membrane-penetrating fusion protein that contains the α-SMA–specific N-terminal sequence AcEEED (SMA-FP) significantly reduces tension generation by Mfs (Hinz et al., >>2002<<).
n3:mentions
n2:11994316
Subject Item
_:vb2997563
rdf:type
n3:Context
rdf:value
Two factors, TGF-β1 and mechanical tension, are pivotal in promoting Mf differentiation from a variety of progenitors (Hinz et al., >>2007<<). TGF-β1 induces Mf differentiation on two-dimensional culture substrates with a stiffness that corresponds to that of contracting fibrotic and granulation tissue but not on substrates exhibiting the compliance of normal connective tissue
n3:mentions
n2:17525249
Subject Item
_:vb2997564
rdf:type
n3:Context
rdf:value
on two-dimensional culture substrates with a stiffness that corresponds to that of contracting fibrotic and granulation tissue but not on substrates exhibiting the compliance of normal connective tissue such as dermis (Goffin et al., >>2006<<). TGF-β1 also induces Mf differentiation in three-dimensional collagen when gels are mechanically restrained (Arora et al., 1999) but not when the gels are free-floating and relaxed (Tomasek et al., 2002).
n3:mentions
n2:16401722
Subject Item
_:vb2997565
rdf:type
n3:Context
rdf:value
TGF-β1 also induces Mf differentiation in three-dimensional collagen when gels are mechanically restrained (Arora et al., >>1999<<) but not when the gels are free-floating and relaxed (Tomasek et al., 2002).
n3:mentions
n2:10079265
Subject Item
_:vb2997566
rdf:type
n3:Context
rdf:value
TGF-β1 also induces Mf differentiation in three-dimensional collagen when gels are mechanically restrained (Arora et al., 1999) but not when the gels are free-floating and relaxed (Tomasek et al., >>2002<<). Conversely, mechanical stress alone fails to induce Mf differentiation in the absence of active TGF-β1, as demonstrated when TGF-β1 antagonists are either applied to cells cultured on rigid substrates (Arora et al., 1999; Hinz et al.,
n3:mentions
n2:11988769
Subject Item
_:vb2997567
rdf:type
n3:Context
rdf:value
Conversely, mechanical stress alone fails to induce Mf differentiation in the absence of active TGF-β1, as demonstrated when TGF-β1 antagonists are either applied to cells cultured on rigid substrates (Arora et al., >>1999<<; Hinz et al., 2001a) or injected into stressed granulation tissues (Hinz et al., 2001b).
n3:mentions
n2:10079265
Subject Item
_:vb2997568
rdf:type
n3:Context
rdf:value
mechanical stress alone fails to induce Mf differentiation in the absence of active TGF-β1, as demonstrated when TGF-β1 antagonists are either applied to cells cultured on rigid substrates (Arora et al., 1999; Hinz et al., 2001a) or injected into stressed granulation tissues (Hinz et al., 2001b).
n3:mentions
n2:11553712
Subject Item
_:vb2997569
rdf:type
n3:Context
rdf:value
in the absence of active TGF-β1, as demonstrated when TGF-β1 antagonists are either applied to cells cultured on rigid substrates (Arora et al., 1999; Hinz et al., 2001a) or injected into stressed granulation tissues (Hinz et al., 2001b). Although it is unclear whether and how mechanical stress and TGF-β1 signaling converge to promote increased α-SMA expression and Mf differentiation, it is possible that intracellular and extracellular tension directly regulate TGF-β1
n3:mentions
n2:11549593
Subject Item
_:vb2997570
rdf:type
n3:Context
rdf:value
LAP and TGF-β1 form the small latent complex (SLC; Miyazono et al., >>1991<<; Annes et al., 2003).
n3:mentions
n2:2022183
Subject Item
_:vb2997571
rdf:type
n3:Context
rdf:value
LAP and TGF-β1 form the small latent complex (SLC; Miyazono et al., 1991; Annes et al., >>2003<<). The LLC provides a reservoir of latent TGF-β1 in the ECM by binding to other ECM components like fibrillin-1 and fibronectin (FN; Unsold et al., 2001; Annes et al., 2003; Hyytiainen et al., 2004; Koli et al., 2005), of which ED-A FN is
n3:mentions
n2:12482908
Subject Item
_:vb2997572
rdf:type
n3:Context
rdf:value
The LLC provides a reservoir of latent TGF-β1 in the ECM by binding to other ECM components like fibrillin-1 and fibronectin (FN; Unsold et al., >>2001<<; Annes et al., 2003; Hyytiainen et al., 2004; Koli et al., 2005), of which ED-A FN is the major splice variant expressed by Mfs (Serini et al., 1998).
n3:mentions
n2:11112702
Subject Item
_:vb2997573
rdf:type
n3:Context
rdf:value
The LLC provides a reservoir of latent TGF-β1 in the ECM by binding to other ECM components like fibrillin-1 and fibronectin (FN; Unsold et al., 2001; Annes et al., >>2003<<; Hyytiainen et al., 2004; Koli et al., 2005), of which ED-A FN is the major splice variant expressed by Mfs (Serini et al., 1998).
n3:mentions
n2:12482908
Subject Item
_:vb2997574
rdf:type
n3:Context
rdf:value
The LLC provides a reservoir of latent TGF-β1 in the ECM by binding to other ECM components like fibrillin-1 and fibronectin (FN; Unsold et al., 2001; Annes et al., 2003; Hyytiainen et al., >>2004<<; Koli et al., 2005), of which ED-A FN is the major splice variant expressed by Mfs (Serini et al., 1998).
n3:mentions
n2:15307633
Subject Item
_:vb2997575
rdf:type
n3:Context
rdf:value
The LLC provides a reservoir of latent TGF-β1 in the ECM by binding to other ECM components like fibrillin-1 and fibronectin (FN; Unsold et al., 2001; Annes et al., 2003; Hyytiainen et al., 2004; Koli et al., >>2005<<), of which ED-A FN is the major splice variant expressed by Mfs (Serini et al., 1998).
n3:mentions
n2:16157329
Subject Item
_:vb2997576
rdf:type
n3:Context
rdf:value
binding to other ECM components like fibrillin-1 and fibronectin (FN; Unsold et al., 2001; Annes et al., 2003; Hyytiainen et al., 2004; Koli et al., 2005), of which ED-A FN is the major splice variant expressed by Mfs (Serini et al., >>1998<<). Several cellular mechanisms have been described that activate latent TGF-β1 by promoting its dissociation from LAP.
n3:mentions
n2:9700173
Subject Item
_:vb2997577
rdf:type
n3:Context
rdf:value
These activation processes include cleavage of LLC by proteases (Mu et al., >>2002<<; Ge and Greenspan, 2006) such as plasmin as well as interaction of LAP with thrombospondin (for review see Annes et al., 2003).
n3:mentions
n2:11970960
Subject Item
_:vb2997578
rdf:type
n3:Context
rdf:value
These activation processes include cleavage of LLC by proteases (Mu et al., 2002; Ge and Greenspan, >>2006<<) such as plasmin as well as interaction of LAP with thrombospondin (for review see Annes et al., 2003).
n3:mentions
n2:17015622
Subject Item
_:vb2997579
rdf:type
n3:Context
rdf:value
These activation processes include cleavage of LLC by proteases (Mu et al., 2002; Ge and Greenspan, 2006) such as plasmin as well as interaction of LAP with thrombospondin (for review see Annes et al., >>2003<<). Binding of active TGF-β1 to TGF-β receptor type II (TGF-β RII) leads to the phosphorylation and recruitment of TGF-β RI. This heteromeric receptor complex phosphorylates Smad2 and 3, which bind to Smad4 and translocate into the nucleus
n3:mentions
n2:12482908
Subject Item
_:vb2997580
rdf:type
n3:Context
rdf:value
receptor complex phosphorylates Smad2 and 3, which bind to Smad4 and translocate into the nucleus to enhance transcription of Mf-specific genes such as α-SMA by cooperating with DNA transcription factors (for review see Hinz, >>2007<<).
n3:mentions
n2:17299435
Subject Item
_:vb2997581
rdf:type
n3:Context
rdf:value
Recently, the epithelial integrin αvβ6 was demonstrated to activate latent TGF-β1 in vivo during development of lung fibrosis (Munger et al., >>1998<<; Jenkins et al., 2006) and in vitro (Annes et al., 2004).
n3:mentions
n2:9725916
Subject Item
_:vb2997582
rdf:type
n3:Context
rdf:value
Recently, the epithelial integrin αvβ6 was demonstrated to activate latent TGF-β1 in vivo during development of lung fibrosis (Munger et al., 1998; Jenkins et al., >>2006<<) and in vitro (Annes et al., 2004).
n3:mentions
n2:16710477
Subject Item
_:vb2997583
rdf:type
n3:Context
rdf:value
Recently, the epithelial integrin αvβ6 was demonstrated to activate latent TGF-β1 in vivo during development of lung fibrosis (Munger et al., 1998; Jenkins et al., 2006) and in vitro (Annes et al., >>2004<<). Because activation by αvβ6 depends on incorporation of the TGF-β1 LLC into the ECM via binding of the LTBP-1 hinge domain, cell traction mediated by αvβ6 integrin has been proposed as part of the mechanism of latent TGF-β1 activation
n3:mentions
n2:15184403
Subject Item
_:vb2997584
rdf:type
n3:Context
rdf:value
by αvβ6 depends on incorporation of the TGF-β1 LLC into the ECM via binding of the LTBP-1 hinge domain, cell traction mediated by αvβ6 integrin has been proposed as part of the mechanism of latent TGF-β1 activation (Annes et al., >>2004<<; Keski-Oja et al., 2004). However, no direct evidence has been provided that mechanical stress liberates TGF-β1 from the ECM-bound LLC.
n3:mentions
n2:15184403
Subject Item
_:vb2997585
rdf:type
n3:Context
rdf:value
incorporation of the TGF-β1 LLC into the ECM via binding of the LTBP-1 hinge domain, cell traction mediated by αvβ6 integrin has been proposed as part of the mechanism of latent TGF-β1 activation (Annes et al., 2004; Keski-Oja et al., >>2004<<). However, no direct evidence has been provided that mechanical stress liberates TGF-β1 from the ECM-bound LLC.
n3:mentions
n2:15564041
Subject Item
_:vb2997586
rdf:type
n3:Context
rdf:value
In addition, although latent TGF-β1 activation by αvβ6 integrin–mediated traction can be of physiological significance during initiation of lung and kidney fibrosis where epithelium is prominent (Jenkins et al., >>2006<<; Kim et al., 2006), this is unlikely to occur during progressive fibrosis of organs with less abundant epithelium.
n3:mentions
n2:16710477
Subject Item
_:vb2997587
rdf:type
n3:Context
rdf:value
In addition, although latent TGF-β1 activation by αvβ6 integrin–mediated traction can be of physiological significance during initiation of lung and kidney fibrosis where epithelium is prominent (Jenkins et al., 2006; Kim et al., >>2006<<), this is unlikely to occur during progressive fibrosis of organs with less abundant epithelium.
n3:mentions
n2:16924102
Subject Item
_:vb2997588
rdf:type
n5:Section
dc:title
materials and methods
n5:contains
_:vb2997600 _:vb2997601 _:vb2997602 _:vb2997589 _:vb2997590 _:vb2997591 _:vb2997596 _:vb2997597 _:vb2997598 _:vb2997599 _:vb2997592 _:vb2997593 _:vb2997594 _:vb2997595
Subject Item
_:vb2997589
rdf:type
n3:Context
rdf:value
Primary rat lung Mfs expressing constitutively high levels of α-SMA and low α-SMA–expressing subcutaneous fibroblasts were isolated and cultured as described previously (Hinz et al., 2001a). Subcutaneous Mf differentiation was induced with 5 ng/ml TGF-β1 (R&D Systems) for 5 d; to dedifferentiate lung Mfs, we applied 250 ng/ml of recombinant soluble TGF-β RII (provided by V.
n3:mentions
n2:11553712
Subject Item
_:vb2997590
rdf:type
n3:Context
rdf:value
Gabbiani, University of Geneva; Skalli et al., >>1986<<), LAP (goat, AF-246-NA; R&D Systems), LTBP-1 (rabbit, Ab39; provided by C.
n3:mentions
n2:3539945
Subject Item
_:vb2997591
rdf:type
n3:Context
rdf:value
Heldin, University of Uppsala, Uppsala, Sweden; Kanzaki et al., >>1990<<), ED-A FN (mouse IgG1, IST-9; provided by L.
n3:mentions
n2:2350783
Subject Item
_:vb2997592
rdf:type
n3:Context
rdf:value
Zardi, National Institute for Cancer Research, Genoa, Italy; Serini et al., >>1998<<), TGF-β RII (rabbit, L-21; Santa Cruz Biotechnology, Inc.
n3:mentions
n2:9700173
Subject Item
_:vb2997593
rdf:type
n3:Context
rdf:value
Kymographs were produced from image sequences as described previously (Hinz et al., >>1999<<) using MetaMorph and figures were assembled with Photoshop (Adobe).
n3:mentions
n2:10438589
Subject Item
_:vb2997594
rdf:type
n3:Context
rdf:value
Cells were stretched isoaxially by 3–10% in home-made culture devices with silicone membranes at the bottom (Goffin et al., >>2006<<). Compliant culture substrates were generated and calibrated as described previously (Goffin et al., 2006) with a Young's modulus of ∼47 and 5 kPa, respectively, as determined by atomic force microscopy (Nanowizard II; JPK Instruments;
n3:mentions
n2:16401722
Subject Item
_:vb2997595
rdf:type
n3:Context
rdf:value
Compliant culture substrates were generated and calibrated as described previously (Goffin et al., >>2006<<) with a Young's modulus of ∼47 and 5 kPa, respectively, as determined by atomic force microscopy (Nanowizard II; JPK Instruments; Goffin et al., 2006).
n3:mentions
n2:16401722
Subject Item
_:vb2997596
rdf:type
n3:Context
rdf:value
substrates were generated and calibrated as described previously (Goffin et al., 2006) with a Young's modulus of ∼47 and 5 kPa, respectively, as determined by atomic force microscopy (Nanowizard II; JPK Instruments; Goffin et al., >>2006<<). Wrinkling silicone substrates to visualize cell contraction were prepared as described previously (Hinz et al., 2001a).
n3:mentions
n2:16401722
Subject Item
_:vb2997597
rdf:type
n3:Context
rdf:value
Wrinkling silicone substrates to visualize cell contraction were prepared as described previously (Hinz et al., 2001a). All surfaces were activated for cell attachment by covalent linking of 10 μg/ml of collagen type I (Sigma-Aldrich; Goffin et al., 2006).
n3:mentions
n2:11553712
Subject Item
_:vb2997598
rdf:type
n3:Context
rdf:value
All surfaces were activated for cell attachment by covalent linking of 10 μg/ml of collagen type I (Sigma-Aldrich; Goffin et al., >>2006<<).
n3:mentions
n2:16401722
Subject Item
_:vb2997599
rdf:type
n3:Context
rdf:value
To prepare ECM, cultures were extracted two times for 5 min with 0.5% DOC in radio immunoprecipitation assay buffer (50 mM Tris, 150 mM NaCl, and 1% Nonidet P-40) under gentle shaking (Unsold et al., >>2001<<). Membrane- and cytosol-free cytoskeletons were produced by extracting cells two times for 15 min with TX-100–containing buffer (60 mM Pipes, 25 mM Hepes, 2 mM MgCl2, 1 mM sodium orthovanadate, 1 mM PMSF, and 0.5% TX-100, pH 6.9) under
n3:mentions
n2:11112702
Subject Item
_:vb2997600
rdf:type
n3:Context
rdf:value
were produced by extracting cells two times for 15 min with TX-100–containing buffer (60 mM Pipes, 25 mM Hepes, 2 mM MgCl2, 1 mM sodium orthovanadate, 1 mM PMSF, and 0.5% TX-100, pH 6.9) under gentle shaking (Dugina et al., >>2001<<); all steps were performed with ice-cold solutions at 4°C.
n3:mentions
n2:11591817
Subject Item
_:vb2997601
rdf:type
n3:Context
rdf:value
To quantify active TGF-β, we used TMLC to produce luciferase under control of the PAI-1 promoter in response to TGF-β (Abe et al., >>1994<<). TMLC (50,000 cells/cm2) were grown for 4 h before being exposed to TGF-β1 in 0.1% BSA in serum-free medium.
n3:mentions
n2:8179182
Subject Item
_:vb2997602
rdf:type
n3:Context
rdf:value
In selected experiments, the level of total TGF-β was assessed by heat-activating samples for 10 min at 80°C (Abe et al., >>1994<<). After exposure to TGF-β1, TMLC were incubated for further 14 h and lysed, and luciferase activity was assessed by light production from a luciferin substrate (Promega) using a luminometer (Centro LB; Berthold Technologies). If not
n3:mentions
n2:8179182
Subject Item
_:vb2997603
rdf:type
n5:Section
dc:title
results
n5:contains
_:vb2997608 _:vb2997609 _:vb2997610 _:vb2997611 _:vb2997612 _:vb2997613 _:vb2997614 _:vb2997615 _:vb2997604 _:vb2997605 _:vb2997606 _:vb2997607 _:vb2997624 _:vb2997625 _:vb2997626 _:vb2997616 _:vb2997617 _:vb2997618 _:vb2997619 _:vb2997620 _:vb2997621 _:vb2997622 _:vb2997623
Subject Item
_:vb2997604
rdf:type
n3:Context
rdf:value
Autocrine TGF-β1 formation has been suggested as the stimulus for constitutive α-SMA expression in cultured rat lung Mfs (Hinz et al., 2001a). To determine whether a portion of this TGF-β1 is stored in the ECM as the LLC, we first assessed ECM incorporation of the latent TGF-β1 scaffolding protein LTBP-1.
n3:mentions
n2:11553712
Subject Item
_:vb2997605
rdf:type
n3:Context
rdf:value
Proteolytic processing was required to liberate LTBP-1 presumably because of covalent binding of LTBP-1 to other ECM proteins (Nunes et al., >>1997<<). In Mf cultures, LTBP-1 colocalized with the Mf-characteristic FN splice variant ED-A FN (Fig.
n3:mentions
n2:9060478
Subject Item
_:vb2997606
rdf:type
n3:Context
rdf:value
The heat-released TGF-β was then measured using transformed mink lung reporter cells (TMLC), which produce luciferase as a function of active TGF-β (Abe et al., >>1994<<). To distinguish between cellular and ECM-derived TGF-β, i.e., LLC, we first measured TGF-β in heated trypsinized cells, which represent the nonsecreted pool of TGF-β. This fraction of total TGF-β was increased as early as 3 d of culture
n3:mentions
n2:8179182
Subject Item
_:vb2997607
rdf:type
n3:Context
rdf:value
The ∼240-kD band corresponds to LTBP-1 bound to LAP–TGF-β1 and the ∼140-kD band represents unbound LTBP-1 (Koli et al., >>2005<<). Consistently, the anti-LAP antibody under nonreducing conditions revealed one band at ∼240 kD (unpublished data), confirming the presence of the LLC in the ECM. Significant levels of TGF-β were liberated by heating Mf-derived ECM to
n3:mentions
n2:16157329
Subject Item
_:vb2997608
rdf:type
n3:Context
rdf:value
The direct contact between the experimental and reporter cells was mandatory to detect cell-activated TGF-β1, confirming previous studies demonstrating that nonproteolytically activated TGF-β1 was poorly soluble (Munger et al., >>1999<<). To elucidate how much of the active TGF-β1 had been liberated from the ECM as opposed to secreted, we compared latent TGF-β1 activation from Mf-derived ECM to that from cells cultured for the same time on tissue culture dishes. On
n3:mentions
n2:10025398
Subject Item
_:vb2997609
rdf:type
n3:Context
rdf:value
1 H, right) correlated with their contractile activity (Hinz et al., 2001a). To study further whether contraction can promote release of TGF-β1 from the ECM, we assessed latent TGF-β1 activation after treating Mfs with drugs that modulate cell tension development (Fig.
n3:mentions
n2:11553712
Subject Item
_:vb2997610
rdf:type
n3:Context
rdf:value
Thrombin, the most potent latent TGF-β1–activating agonist in our experiments is also known to liberate active TGF-β1 from the LLC by proteolytic cleavage at 10-fold higher concentrations than used here (0.5 U/ml; Taipale et al., >>1992<<). At 0.5 U/ml, thrombin did not release active TGF-β1 from cell-free, Mf-derived ECM (Fig.
n3:mentions
n2:1281156
Subject Item
_:vb2997611
rdf:type
n3:Context
rdf:value
2 C; Taipale et al., >>1992<<). To further eliminate the role of proteolysis in our system, we stimulated Mf contraction in the presence of a protease inhibitor cocktail.
n3:mentions
n2:1281156
Subject Item
_:vb2997612
rdf:type
n3:Context
rdf:value
2 E) because thrombin induces Mf contraction through proteolytic cleavage of the protease-activated receptor 1 (Bogatkevich et al., >>2003<<). In contrast, when added to Mf/TMLC co-cultures, protease-independent contraction of Mfs by ET-1 and AT-II elevated the amounts of active TGF- β1 by 1.8–2.5-fold compared with the BSA control in the presence of protease inhibitors (Fig.
n3:mentions
n2:12665468
Subject Item
_:vb2997613
rdf:type
n3:Context
rdf:value
The fibroblast integrins that bind to the LLC and are potentially involved in protease-independent latent TGF-β1 activation are αvβ3, α8β1, and αvβ5 (Levine et al., >>2000<<; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, 2005; Araya et al., 2006).
n3:mentions
n2:10854216
Subject Item
_:vb2997614
rdf:type
n3:Context
rdf:value
The fibroblast integrins that bind to the LLC and are potentially involved in protease-independent latent TGF-β1 activation are αvβ3, α8β1, and αvβ5 (Levine et al., 2000; Lu et al., >>2002<<; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, 2005; Araya et al., 2006).
n3:mentions
n2:12415008
Subject Item
_:vb2997615
rdf:type
n3:Context
rdf:value
The fibroblast integrins that bind to the LLC and are potentially involved in protease-independent latent TGF-β1 activation are αvβ3, α8β1, and αvβ5 (Levine et al., 2000; Lu et al., 2002; Mu et al., >>2002<<; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, 2005; Araya et al., 2006).
n3:mentions
n2:11970960
Subject Item
_:vb2997616
rdf:type
n3:Context
rdf:value
The fibroblast integrins that bind to the LLC and are potentially involved in protease-independent latent TGF-β1 activation are αvβ3, α8β1, and αvβ5 (Levine et al., 2000; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., >>2003<<; Asano et al., 2005; Sheppard, 2005; Araya et al., 2006). As visualized by immunofluorescence, cultured lung Mfs do express β3 (Fig.
n3:mentions
n2:12358597
Subject Item
_:vb2997617
rdf:type
n3:Context
rdf:value
integrins that bind to the LLC and are potentially involved in protease-independent latent TGF-β1 activation are αvβ3, α8β1, and αvβ5 (Levine et al., 2000; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., >>2005<<; Sheppard, 2005; Araya et al., 2006). As visualized by immunofluorescence, cultured lung Mfs do express β3 (Fig.
n3:mentions
n2:16301681
Subject Item
_:vb2997618
rdf:type
n3:Context
rdf:value
that bind to the LLC and are potentially involved in protease-independent latent TGF-β1 activation are αvβ3, α8β1, and αvβ5 (Levine et al., 2000; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, >>2005<<; Araya et al., 2006). As visualized by immunofluorescence, cultured lung Mfs do express β3 (Fig.
n3:mentions
n2:16258727
Subject Item
_:vb2997619
rdf:type
n3:Context
rdf:value
and are potentially involved in protease-independent latent TGF-β1 activation are αvβ3, α8β1, and αvβ5 (Levine et al., 2000; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, 2005; Araya et al., >>2006<<). As visualized by immunofluorescence, cultured lung Mfs do express β3 (Fig. 3 A) and β1 (Fig.
n3:mentions
n2:16877343
Subject Item
_:vb2997620
rdf:type
n3:Context
rdf:value
1 E), and focal adhesion integrity (Hinz et al., >>2003<<). Cytosol and membranes were completely removed as shown by the loss of the membrane marker Na+/K+-ATPase (Fig.
n3:mentions
n2:12808047
Subject Item
_:vb2997621
rdf:type
n3:Context
rdf:value
5, E–G), which indicates that TGF-β1 binds to its receptor (Heldin et al., >>1997<<). This was confirmed by Western blotting, demonstrating increased Smad2/3 phosphorylation at unchanged levels of total Smad2/3 (Fig. 5, H and I).
n3:mentions
n2:9393997
Subject Item
_:vb2997622
rdf:type
n3:Context
rdf:value
Mf differentiation and function depend on a threshold of ECM stiffness (Arora et al., >>1999<<; Goffin et al., 2006).
n3:mentions
n2:10079265
Subject Item
_:vb2997623
rdf:type
n3:Context
rdf:value
Mf differentiation and function depend on a threshold of ECM stiffness (Arora et al., 1999; Goffin et al., >>2006<<). To investigate whether the mechanical properties of the ECM modulate the level of contraction-activated latent TGF-β1, we assessed latent TGF-β1 activation by Mfs grown on silicone culture substrates with tunable Young's modulus (5–47
n3:mentions
n2:16401722
Subject Item
_:vb2997624
rdf:type
n3:Context
rdf:value
increased by ∼1.5-fold between 5-kPa soft substrates that mimic the compliance of a normal dermis and substrates exhibiting a stiffness corresponding to that of fibrotic and late wound granulation tissue (47 kPa; Goffin et al., >>2006<<). Induction of Mf contraction with thrombin enhanced latent TGF-β1 activation on 9–47-kPa substrates by approximately twofold but had no effect on 5-kPa soft substrates (Fig.
n3:mentions
n2:16401722
Subject Item
_:vb2997625
rdf:type
n3:Context
rdf:value
However, we have previously shown that incorporation of α-SMA into contractile stress fibers of rat embryonic fibroblasts is impaired by prolonged growth on soft substrates (Goffin et al., >>2006<<), which is also observed for lung Mfs (Fig.
n3:mentions
n2:16401722
Subject Item
_:vb2997626
rdf:type
n3:Context
rdf:value
Expression of α-SMA was induced earlier and stronger by 6 d and enhanced after 9 d after wounding, when wounds were subjected to mechanical stress by splinting the edges with a plastic frame as described previously (Hinz et al., 2001b). Relaxation of prestressed wounds by removing the splint after 8 d for 2 d significantly reduced α-SMA expression levels compared with 10-d stressed wounds (Fig.
n3:mentions
n2:11549593
Subject Item
_:vb2997627
rdf:type
n5:Section
dc:title
discussion
n5:contains
_:vb2997628 _:vb2997629 _:vb2997630 _:vb2997631 _:vb2997640 _:vb2997641 _:vb2997642 _:vb2997643 _:vb2997644 _:vb2997645 _:vb2997646 _:vb2997647 _:vb2997632 _:vb2997633 _:vb2997634 _:vb2997635 _:vb2997636 _:vb2997637 _:vb2997638 _:vb2997639 _:vb2997656 _:vb2997657 _:vb2997658 _:vb2997659 _:vb2997660 _:vb2997661 _:vb2997662 _:vb2997663 _:vb2997648 _:vb2997649 _:vb2997650 _:vb2997651 _:vb2997652 _:vb2997653 _:vb2997654 _:vb2997655 _:vb2997672 _:vb2997673 _:vb2997664 _:vb2997665 _:vb2997666 _:vb2997667 _:vb2997668 _:vb2997669 _:vb2997670 _:vb2997671
Subject Item
_:vb2997628
rdf:type
n3:Context
rdf:value
Mechanical tension in conjunction with the presence of active TGF-β1 is a prerequisite for the development of α-SMA–positive fibrogenic Mfs (Arora et al., >>1999<<; Hinz et al., 2001b). However, a direct link between both factors has not been established.
n3:mentions
n2:10079265
Subject Item
_:vb2997629
rdf:type
n3:Context
rdf:value
Mechanical tension in conjunction with the presence of active TGF-β1 is a prerequisite for the development of α-SMA–positive fibrogenic Mfs (Arora et al., 1999; Hinz et al., 2001b). However, a direct link between both factors has not been established. Here, we provide evidence that Mfs activate TGF-β1 from self-generated and predeposited ECM stores by a contraction-mediated mechanism.
n3:mentions
n2:11549593
Subject Item
_:vb2997630
rdf:type
n3:Context
rdf:value
We propose that tension-mediated activation of TGF-β1 plays an important role in maintaining Mf differentiation in mechanically challenged environments, e.g., in the stiff ECM of fibrotic lesions (Hinz, >>2007<<), during the contraction phase of wound healing (Goffin et al., 2006) and in the stiff stroma that surrounds epithelial tumors (Paszek and Weaver, 2004; Amatangelo et al., 2005).
n3:mentions
n2:17299435
Subject Item
_:vb2997631
rdf:type
n3:Context
rdf:value
of TGF-β1 plays an important role in maintaining Mf differentiation in mechanically challenged environments, e.g., in the stiff ECM of fibrotic lesions (Hinz, 2007), during the contraction phase of wound healing (Goffin et al., >>2006<<) and in the stiff stroma that surrounds epithelial tumors (Paszek and Weaver, 2004; Amatangelo et al., 2005).
n3:mentions
n2:16401722
Subject Item
_:vb2997632
rdf:type
n3:Context
rdf:value
challenged environments, e.g., in the stiff ECM of fibrotic lesions (Hinz, 2007), during the contraction phase of wound healing (Goffin et al., 2006) and in the stiff stroma that surrounds epithelial tumors (Paszek and Weaver, >>2004<<; Amatangelo et al., 2005).
n3:mentions
n2:15838603
Subject Item
_:vb2997633
rdf:type
n3:Context
rdf:value
e.g., in the stiff ECM of fibrotic lesions (Hinz, 2007), during the contraction phase of wound healing (Goffin et al., 2006) and in the stiff stroma that surrounds epithelial tumors (Paszek and Weaver, 2004; Amatangelo et al., >>2005<<).
n3:mentions
n2:16049333
Subject Item
_:vb2997634
rdf:type
n3:Context
rdf:value
Thrombin was recently shown to enhance TGF-β1 activation by epithelial cells in an αvβ6 integrin–dependent manner, presumably via the receptor protease-activated receptor 1 and downstream activation of RhoA ( Jenkins et al., >>2006<<). Moreover, adenoviral infection with a constitutively active form of RhoA, which is known to enhance actin reorganization, leads to increased TGF-β activation in β6 integrin–transfected fibroblasts (Jenkins et al., 2006). It has been
n3:mentions
n2:16710477
Subject Item
_:vb2997635
rdf:type
n3:Context
rdf:value
Moreover, adenoviral infection with a constitutively active form of RhoA, which is known to enhance actin reorganization, leads to increased TGF-β activation in β6 integrin–transfected fibroblasts (Jenkins et al., >>2006<<). It has been suggested that subsequent cytoskeletal changes enhance cell traction without further evaluating this point (Jenkins et al., 2006). We reduced the activation of latent TGF-β1 by inhibiting Mf contractile activity generated in
n3:mentions
n2:16710477
Subject Item
_:vb2997636
rdf:type
n3:Context
rdf:value
It has been suggested that subsequent cytoskeletal changes enhance cell traction without further evaluating this point (Jenkins et al., >>2006<<). We reduced the activation of latent TGF-β1 by inhibiting Mf contractile activity generated in α-SMA–positive stress fibers. Low contractile fibroblasts were consistently less efficient in liberating active TGF-β1 from Mf-derived ECM
n3:mentions
n2:16710477
Subject Item
_:vb2997637
rdf:type
n3:Context
rdf:value
8), which is similar to a recent model proposed for epithelial cells (Annes et al., >>2003<<). Whereas compliant substrates appear to absorb the large deformations generated by Mf contraction and thus protect the LLC against conformational changes (Fig. 7 A), individual fibers become stretched on stiff substrates. In our
n3:mentions
n2:12482908
Subject Item
_:vb2997638
rdf:type
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rdf:value
ECM by 3–10% liberates active TGF-β1 from the LLC in the presence of the mechanically resistant Mf cytoskeleton; this stretch is in the same range as what has been described to reveal cryptic self-assembly sites in FN (Zhong et al., >>1998<<) and to mediate mechanotransduction by various extracellular and cytoplasmic proteins (Giannone and Sheetz, 2006; Vogel, 2006).
n3:mentions
n2:9548730
Subject Item
_:vb2997639
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this stretch is in the same range as what has been described to reveal cryptic self-assembly sites in FN (Zhong et al., 1998) and to mediate mechanotransduction by various extracellular and cytoplasmic proteins (Giannone and Sheetz, >>2006<<; Vogel, 2006). To allow deformation by cell traction, the LLC must be connected to an element that provides resistance to mechanical strain (Annes et al., 2004; Keski-Oja et al., 2004).
n3:mentions
n2:16529933
Subject Item
_:vb2997640
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rdf:value
is in the same range as what has been described to reveal cryptic self-assembly sites in FN (Zhong et al., 1998) and to mediate mechanotransduction by various extracellular and cytoplasmic proteins (Giannone and Sheetz, 2006; Vogel, >>2006<<). To allow deformation by cell traction, the LLC must be connected to an element that provides resistance to mechanical strain (Annes et al., 2004; Keski-Oja et al., 2004).
n3:mentions
n2:16689645
Subject Item
_:vb2997641
rdf:type
n3:Context
rdf:value
To allow deformation by cell traction, the LLC must be connected to an element that provides resistance to mechanical strain (Annes et al., >>2004<<; Keski-Oja et al., 2004).
n3:mentions
n2:15184403
Subject Item
_:vb2997642
rdf:type
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rdf:value
To allow deformation by cell traction, the LLC must be connected to an element that provides resistance to mechanical strain (Annes et al., 2004; Keski-Oja et al., >>2004<<). Consistent with this idea, transformed fibroblasts overexpressing SLC (LAP–TGF-β1) do not induce Mf formation when implanted into mouse dermis (Campaner et al., 2006), presumably because of the lack of ECM fixation in the absence of
n3:mentions
n2:15564041
Subject Item
_:vb2997643
rdf:type
n3:Context
rdf:value
Consistent with this idea, transformed fibroblasts overexpressing SLC (LAP–TGF-β1) do not induce Mf formation when implanted into mouse dermis (Campaner et al., >>2006<<), presumably because of the lack of ECM fixation in the absence of LTBP-1.
n3:mentions
n2:16498396
Subject Item
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Normal dermis contains significant levels of LTBP-1 that potentially acts as a repository for the TGF-β1 LLC (Karonen et al., >>1997<<; Raghunath et al., 1998), and the levels of total TGF-β1 are elevated during all stages of wound healing (Brunner and Blakytny, 2004).
n3:mentions
n2:9274625
Subject Item
_:vb2997645
rdf:type
n3:Context
rdf:value
Normal dermis contains significant levels of LTBP-1 that potentially acts as a repository for the TGF-β1 LLC (Karonen et al., 1997; Raghunath et al., >>1998<<), and the levels of total TGF-β1 are elevated during all stages of wound healing (Brunner and Blakytny, 2004).
n3:mentions
n2:9764833
Subject Item
_:vb2997646
rdf:type
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rdf:value
levels of LTBP-1 that potentially acts as a repository for the TGF-β1 LLC (Karonen et al., 1997; Raghunath et al., 1998), and the levels of total TGF-β1 are elevated during all stages of wound healing (Brunner and Blakytny, >>2004<<). In contrast, active TGF-β1 is generally low and peaks during early inflammation as well as during the phase of wound contraction by Mfs (Yang et al., 1999).
n3:mentions
n2:15269820
Subject Item
_:vb2997647
rdf:type
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rdf:value
In contrast, active TGF-β1 is generally low and peaks during early inflammation as well as during the phase of wound contraction by Mfs (Yang et al., >>1999<<). The question arises why α-SMA–negative fibroblasts, which are abundant during early wound remodeling, are not capable of activating existing latent TGF-β1 deposits from the ECM. Our in vivo data suggest that ECM stress makes the
n3:mentions
n2:9916924
Subject Item
_:vb2997648
rdf:type
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rdf:value
The fact that αvβ6-mediated latent TGF-β1 activation in an animal model of early lung fibrosis is augmented by high-tidal-volume ventilation, i.e., stress (Jenkins et al., >>2006<<), seems to support the requirement for a mechanically loaded ECM in this system.
n3:mentions
n2:16710477
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_:vb2997649
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rdf:value
stiff ECM only liberated active TGF-β1 in the presence of the Mf cytoskeleton in our experiments, and depolymerization of the actin cytoskeleton completely blocked activation of latent TGF-β1 by epithelial cells (Munger et al., >>1999<<). These results indicate that the proposed LLC conformation change requires a second, cellular anchor point.
n3:mentions
n2:10025398
Subject Item
_:vb2997650
rdf:type
n3:Context
rdf:value
Integrins αvβ5, β3, β1, and β8 are expressed in fibroblastic cells and bind to RGD in LAP (Levine et al., >>2000<<; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, 2005; Araya et al., 2006).
n3:mentions
n2:10854216
Subject Item
_:vb2997651
rdf:type
n3:Context
rdf:value
Integrins αvβ5, β3, β1, and β8 are expressed in fibroblastic cells and bind to RGD in LAP (Levine et al., 2000; Lu et al., >>2002<<; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, 2005; Araya et al., 2006).
n3:mentions
n2:12415008
Subject Item
_:vb2997652
rdf:type
n3:Context
rdf:value
Integrins αvβ5, β3, β1, and β8 are expressed in fibroblastic cells and bind to RGD in LAP (Levine et al., 2000; Lu et al., 2002; Mu et al., >>2002<<; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, 2005; Araya et al., 2006).
n3:mentions
n2:11970960
Subject Item
_:vb2997653
rdf:type
n3:Context
rdf:value
Integrins αvβ5, β3, β1, and β8 are expressed in fibroblastic cells and bind to RGD in LAP (Levine et al., 2000; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., >>2003<<; Asano et al., 2005; Sheppard, 2005; Araya et al., 2006).
n3:mentions
n2:12358597
Subject Item
_:vb2997654
rdf:type
n3:Context
rdf:value
Integrins αvβ5, β3, β1, and β8 are expressed in fibroblastic cells and bind to RGD in LAP (Levine et al., 2000; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., >>2005<<; Sheppard, 2005; Araya et al., 2006).
n3:mentions
n2:16301681
Subject Item
_:vb2997655
rdf:type
n3:Context
rdf:value
Integrins αvβ5, β3, β1, and β8 are expressed in fibroblastic cells and bind to RGD in LAP (Levine et al., 2000; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, >>2005<<; Araya et al., 2006).
n3:mentions
n2:16258727
Subject Item
_:vb2997656
rdf:type
n3:Context
rdf:value
Integrins αvβ5, β3, β1, and β8 are expressed in fibroblastic cells and bind to RGD in LAP (Levine et al., 2000; Lu et al., 2002; Mu et al., 2002; Ludbrook et al., 2003; Asano et al., 2005; Sheppard, 2005; Araya et al., >>2006<<). Activation of latent TGF-β1 by binding of αvβ8 integrin to SLC involves proteolytic action of MT1–matrix metalloproteinase and does not require incorporation of LLC into the ECM (Mu et al., 2002). The generally low levels of active
n3:mentions
n2:16877343
Subject Item
_:vb2997657
rdf:type
n3:Context
rdf:value
Activation of latent TGF-β1 by binding of αvβ8 integrin to SLC involves proteolytic action of MT1–matrix metalloproteinase and does not require incorporation of LLC into the ECM (Mu et al., >>2002<<). The generally low levels of active TGF-β1 in the culture supernatant and the activation of latent TGF-β1 by purified cytoskeletons all rule out αvβ8 integrin–assisted proteolytic release in our conditions.
n3:mentions
n2:11970960
Subject Item
_:vb2997658
rdf:type
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rdf:value
candidates for latent TGF-β1 stress activation because they are involved in TGF-β1 activation by systemic sclerosis fibroblasts and their inhibition reverses the myofibroblastic phenotype by a yet undefined mechanism (Scaffidi et al., >>2004<<; Asano et al., 2005, 2006). Function blocking of the β3 integrin in our hands moderately reduces latent TGF-β1 activation by Mf contraction.
n3:mentions
n2:15187087
Subject Item
_:vb2997659
rdf:type
n3:Context
rdf:value
TGF-β1 stress activation because they are involved in TGF-β1 activation by systemic sclerosis fibroblasts and their inhibition reverses the myofibroblastic phenotype by a yet undefined mechanism (Scaffidi et al., 2004; Asano et al., >>2005<<, 2006). Function blocking of the β3 integrin in our hands moderately reduces latent TGF-β1 activation by Mf contraction.
n3:mentions
n2:16301681
Subject Item
_:vb2997660
rdf:type
n3:Context
rdf:value
stress activation because they are involved in TGF-β1 activation by systemic sclerosis fibroblasts and their inhibition reverses the myofibroblastic phenotype by a yet undefined mechanism (Scaffidi et al., 2004; Asano et al., 2005, >>2006<<). Function blocking of the β3 integrin in our hands moderately reduces latent TGF-β1 activation by Mf contraction.
n3:mentions
n2:16436664
Subject Item
_:vb2997661
rdf:type
n3:Context
rdf:value
Integrin α8β1 was previously shown to strongly interact with LAP–TGF-β1 (Lu et al., >>2002<<) and is up-regulated in conjunction with Mf differentiation during heart (Bouzeghrane et al., 2004), pulmonary, and hepatic fibrosis (Levine et al., 2000).
n3:mentions
n2:12415008
Subject Item
_:vb2997662
rdf:type
n3:Context
rdf:value
Integrin α8β1 was previously shown to strongly interact with LAP–TGF-β1 (Lu et al., 2002) and is up-regulated in conjunction with Mf differentiation during heart (Bouzeghrane et al., >>2004<<), pulmonary, and hepatic fibrosis (Levine et al., 2000).
n3:mentions
n2:15010273
Subject Item
_:vb2997663
rdf:type
n3:Context
rdf:value
α8β1 was previously shown to strongly interact with LAP–TGF-β1 (Lu et al., 2002) and is up-regulated in conjunction with Mf differentiation during heart (Bouzeghrane et al., 2004), pulmonary, and hepatic fibrosis (Levine et al., >>2000<<). However, overexpression of α8β1 integrin in nonfibroblastic cells does not enhance levels of active TGF-β1 (Lu et al., 2002).
n3:mentions
n2:10854216
Subject Item
_:vb2997664
rdf:type
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However, overexpression of α8β1 integrin in nonfibroblastic cells does not enhance levels of active TGF-β1 (Lu et al., >>2002<<). This apparent discrepancy with our results can be explained by the low contractile potential of the transfected cells or by the involvement of another β1 integrin heterodimer that has not yet been shown to bind to LAP. Further studies
n3:mentions
n2:12415008
Subject Item
_:vb2997665
rdf:type
n3:Context
rdf:value
Until now, activation of latent TGF-β1 by cell traction has been suggested exclusively for the epithelial integrin αvβ6 (Annes et al., >>2004<<; Yang et al., 2007), which is involved in the initiation of lung fibrosis (Jenkins et al., 2006; Munger et al., 1999).
n3:mentions
n2:15184403
Subject Item
_:vb2997666
rdf:type
n3:Context
rdf:value
Until now, activation of latent TGF-β1 by cell traction has been suggested exclusively for the epithelial integrin αvβ6 (Annes et al., 2004; Yang et al., >>2007<<), which is involved in the initiation of lung fibrosis (Jenkins et al., 2006; Munger et al., 1999).
n3:mentions
n2:17353357
Subject Item
_:vb2997667
rdf:type
n3:Context
rdf:value
Until now, activation of latent TGF-β1 by cell traction has been suggested exclusively for the epithelial integrin αvβ6 (Annes et al., 2004; Yang et al., 2007), which is involved in the initiation of lung fibrosis (Jenkins et al., >>2006<<; Munger et al., 1999).
n3:mentions
n2:16710477
Subject Item
_:vb2997668
rdf:type
n3:Context
rdf:value
of latent TGF-β1 by cell traction has been suggested exclusively for the epithelial integrin αvβ6 (Annes et al., 2004; Yang et al., 2007), which is involved in the initiation of lung fibrosis (Jenkins et al., 2006; Munger et al., >>1999<<). During fibrosis of epithelialized tissues, such as kidney and lung, Mfs are partly recruited through mesenchymal transition of epithelial cells (Hinz et al., 2007) involving αvβ6 integrin–mediated latent TGF-β1 activation (Kim et al.,
n3:mentions
n2:10025398
Subject Item
_:vb2997669
rdf:type
n3:Context
rdf:value
During fibrosis of epithelialized tissues, such as kidney and lung, Mfs are partly recruited through mesenchymal transition of epithelial cells (Hinz et al., >>2007<<) involving αvβ6 integrin–mediated latent TGF-β1 activation (Kim et al., 2006).
n3:mentions
n2:17525249
Subject Item
_:vb2997670
rdf:type
n3:Context
rdf:value
During fibrosis of epithelialized tissues, such as kidney and lung, Mfs are partly recruited through mesenchymal transition of epithelial cells (Hinz et al., 2007) involving αvβ6 integrin–mediated latent TGF-β1 activation (Kim et al., >>2006<<). However, the evolution of pulmonary fibrosis toward end-stage fibrotic lung disease depends on the persistence of αvβ6-negative Mfs to express and activate latent TGF-β1 (Phan, 2002; Thannickal et al., 2004).
n3:mentions
n2:16924102
Subject Item
_:vb2997671
rdf:type
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rdf:value
However, the evolution of pulmonary fibrosis toward end-stage fibrotic lung disease depends on the persistence of αvβ6-negative Mfs to express and activate latent TGF-β1 (Phan, >>2002<<; Thannickal et al., 2004).
n3:mentions
n2:12475801
Subject Item
_:vb2997672
rdf:type
n3:Context
rdf:value
However, the evolution of pulmonary fibrosis toward end-stage fibrotic lung disease depends on the persistence of αvβ6-negative Mfs to express and activate latent TGF-β1 (Phan, 2002; Thannickal et al., >>2004<<). Furthermore, Mfs drive fibrosis in a variety of other organs that neither exhibit a pronounced epithelium nor posses cells expressing αvβ6 integrin (Hinz et al., 2007). Our data strongly suggest that in these conditions, Mfs liberate
n3:mentions
n2:14746528
Subject Item
_:vb2997673
rdf:type
n3:Context
rdf:value
Furthermore, Mfs drive fibrosis in a variety of other organs that neither exhibit a pronounced epithelium nor posses cells expressing αvβ6 integrin (Hinz et al., >>2007<<). Our data strongly suggest that in these conditions, Mfs liberate and activate TGF-β1 from preexisting and self-generated deposits in the ECM by transmitting their high contractile force to the LLC through αvβ5 integrin and yet
n3:mentions
n2:17525249
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n3:RelevantBibliographicResource
n3:RelevantScore
42
n3:hasRelevantPaperId
n2:10025398
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n3:RelevantBibliographicResource
n3:RelevantScore
35
n3:hasRelevantPaperId
n2:11988769
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n3:RelevantBibliographicResource
n3:RelevantScore
28
n3:hasRelevantPaperId
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
25
n3:hasRelevantPaperId
n2:12482908
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
24
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n3:RelevantBibliographicResource
n3:RelevantScore
24
n3:hasRelevantPaperId
n2:17525249
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
23
n3:hasRelevantPaperId
n2:16169468
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
23
n3:hasRelevantPaperId
n2:11970960
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
21
n3:hasRelevantPaperId
n2:24216753
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
18
n3:hasRelevantPaperId
n2:19296884
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n3:RelevantBibliographicResource
n3:RelevantScore
18
n3:hasRelevantPaperId
n2:17299435
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
17
n3:hasRelevantPaperId
n2:20733059
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
17
n3:hasRelevantPaperId
n2:21677751
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
17
n3:hasRelevantPaperId
n2:19931152
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
17
n3:hasRelevantPaperId
n2:22387320
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
16
n3:hasRelevantPaperId
n2:11553712
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
16
n3:hasRelevantPaperId
n2:12297042
Subject Item
_:vb367200922
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
16
n3:hasRelevantPaperId
n2:19800625
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
15
n3:hasRelevantPaperId
n2:21654799
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
14
n3:hasRelevantPaperId
n2:25960420
Subject Item
_:vb367200925
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
14
n3:hasRelevantPaperId
n2:16401722
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
14
n3:hasRelevantPaperId
n2:15117886
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
14
n3:hasRelevantPaperId
n2:9700173
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
13
n3:hasRelevantPaperId
n2:18161745
Subject Item
_:vb367200929
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
13
n3:hasRelevantPaperId
n2:20075988
Subject Item
_:vb367200930
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
13
n3:hasRelevantPaperId
n2:16436664
Subject Item
_:vb367200931
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
13
n3:hasRelevantPaperId
n2:17916809
Subject Item
_:vb367200932
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
12
n3:hasRelevantPaperId
n2:9259574
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
12
n3:hasRelevantPaperId
n2:22936357
Subject Item
_:vb367200934
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n3:RelevantBibliographicResource
n3:RelevantScore
12
n3:hasRelevantPaperId
n2:22169532
Subject Item
_:vb367200935
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
12
n3:hasRelevantPaperId
n2:16924102
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
11
n3:hasRelevantPaperId
n2:22461426
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
11
n3:hasRelevantPaperId
n2:16923388
Subject Item
_:vb367200938
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
11
n3:hasRelevantPaperId
n2:23434591
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:25332161
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:14534577
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:24639195
Subject Item
_:vb367200942
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:17625791
Subject Item
_:vb367200943
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:12809600
Subject Item
_:vb367200944
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:19965464
Subject Item
_:vb367200945
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:15573414
Subject Item
_:vb367200946
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:16293750
Subject Item
_:vb367200947
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:19114990
Subject Item
_:vb367200948
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:17932231
Subject Item
_:vb367200949
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:7856739
Subject Item
_:vb367200950
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:19165226
Subject Item
_:vb367200951
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:19487818
Subject Item
_:vb367200952
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:20818376
Subject Item
_:vb367200953
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:22996908
Subject Item
_:vb367200954
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:20463011
Subject Item
_:vb367200955
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
10
n3:hasRelevantPaperId
n2:23000686
Subject Item
_:vb367200956
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:27108839
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:18662538
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:22772564
Subject Item
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rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:17660828
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
9
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n2:19104148
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:12845617
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:21471066
Subject Item
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n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:12531888
Subject Item
_:vb367200964
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:19701206
Subject Item
_:vb367200965
rdf:type
n3:RelevantBibliographicResource
n3:RelevantScore
9
n3:hasRelevantPaperId
n2:21900405
Subject Item
_:vb367200966
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