Faculty Opinions recommendation of Redefining the role of ectoderm in somitogenesis: a player in the formation of the fibronectin matrix of presomitic mesoderm.

2007 ◽  
Author(s):  
Douglas DeSimone
Keyword(s):  
Presomitic Mesoderm ◽  
Fibronectin Matrix

scholarly journals Redefining the role of ectoderm in somitogenesis: a player in the formation of the fibronectin matrix of presomitic mesoderm

Development ◽  
2007 ◽  
Vol 134 (17) ◽  
pp. 3155-3165 ◽  
Author(s):  
P. Rifes ◽  
L. Carvalho ◽  
C. Lopes ◽  
R. P. Andrade ◽  
G. Rodrigues ◽  
...  
Keyword(s):  
Presomitic Mesoderm ◽  
Fibronectin Matrix

scholarly journals Role of the I-9 and III-1 modules of fibronectin in formation of an extracellular fibronectin matrix

1991 ◽  
Vol 266 (17) ◽  
pp. 10851-10858 ◽  
Author(s):  
M.A. Chernousov ◽  
F.J. Fogerty ◽  
V.E. Koteliansky ◽  
D.F. Mosher
Keyword(s):  
Fibronectin Matrix

scholarly journals Matrix Fibronectin Binds Gammaretrovirus and Assists in Entry: New Light on Viral Infections

2007 ◽  
Vol 81 (15) ◽  
pp. 8247-8257 ◽  
Author(s):  
Christiane Beer ◽  
Lene Pedersen
Keyword(s):  
Viral Infections ◽  
Leukemia Virus ◽  
Active Role ◽  
Infection Process ◽  
3T3 Fibroblasts ◽  
Viral Binding ◽  
Fibronectin Matrix ◽  
Viral Particles ◽  
Nih 3T3

ABSTRACT A major entry route for the gammaretrovirus amphotropic murine leukemia virus (A-MLV) into NIH 3T3 fibroblasts is via caveola-dependent endocytosis. However, during the infection time, few viral particles can be observed intracellularly. Analyzing the dynamics of the A-MLV infection process by using total internal reflection fluorescence microscopy, we show that the majority of viruses are extracellular and bound to the fibronectin matrix. Moreover, the amounts of bound virus and of fibronectin correlated. Using confocal microscopy, nanoparticles targeted to fibronectin by a III1C-fibronectin fragment or anti-fibronectin antibody were detected intracellularly in NIH 3T3 cells; unconjugated nanoparticles neither bound to cells nor were detectable intracellularly. Furthermore, A-MLV colocalized intracellularly with the fibronectin-targeted nanoparticles, suggesting that they were taken up by the same cellular pathway. Both A-MLV entry and fibronectin turnover depend on caveolar endocytosis, and we found that inhibiting viral binding to the extracellular NIH 3T3 fibronectin-matrix dramatically reduced A-MLV infection, indeed, showing an active role of fibronectin in infection. We suggest that binding to the cellular fibronectin matrix provides a new mechanism by which viruses can enter cells.

scholarly journals PAPC couples the Segmentation Clock to somite morphogenesis by regulating N-cadherin dependent adhesion

2016 ◽  
Author(s):  
Jerome Chal ◽  
Charlene Guillot ◽  
Olivier Pourquie
Keyword(s):  
Mouse Embryos ◽  
Loss Of Function ◽  
Presomitic Mesoderm ◽  
Segmentation Clock ◽  
Anterior Compartment ◽  
Chicken Embryos ◽  
Differential Adhesion ◽  
Complementary Pattern ◽  
The Future

Vertebrate segmentation is characterized by the periodic formation of epithelial somites from the mesenchymal presomitic mesoderm (PSM). How the rhythmic signaling pulse delivered by the Segmentation Clock is translated into the periodic morphogenesis of somites remains poorly understood. Here, we focused on the role of Paraxial protocadherin (PAPC/Pcdh8) in this process. We show that in chicken and mouse embryos, PAPC expression is tightly regulated by the Clock and Wavefront system in the posterior PSM. We observed that PAPC exhibits a striking complementary pattern to N-Cadherin (CDH2), marking the interface of the future somite boundary in the anterior PSM. Gain and loss of function of PAPC in chicken embryos disrupt somite segmentation by altering the CDH2-dependent epithelialization of PSM cells. Our data suggest that clathrin-mediated endocytosis is increased in PAPC expressing cells, subsequently affecting CDH2 internalization in the anterior compartment of the future somite. This in turn generates a differential adhesion interface, allowing formation of the acellular fissure that defines the somite boundary. Thus periodic expression of PAPC downstream of the Segmentation Clock triggers rhythmic endocytosis of CDH2, allowing for segmental de-adhesion and individualization of somites.

Role of the carboxyl-terminal Fib2 domain in fibronectin matrix assembly

1995 ◽  
Vol 108 (3) ◽  
pp. 907-915 ◽  
Author(s):  
K. Ichihara-Tanaka ◽  
K. Titani ◽  
K. Sekiguchi
Keyword(s):  
Residual Activity ◽  
Significant Activity ◽  
Matrix Assembly ◽  
En Bloc ◽  
Proteolytic Fragment ◽  
Cultured Fibroblasts ◽  
Fibronectin Matrix ◽  
The Matrix ◽  
Assembly Activity

A truncated form of fibronectin consisting of the N-terminal 70 kDa and C-terminal 37 kDa regions, designated r70F2, retained the ability to assemble into the extracellular matrix when expressed in cultured fibroblasts (Ichihara-Tanaka et al. (1992) FEBS Lett. 299, 155–158). To elucidate the role of the C-terminal 37 kDa region in fibronectin matrix assembly, we expressed a panel of mutant forms of r70F2 with various deletions and amino acid substitutions in mouse L cells. Although substitution of Ser for two Cys residues in the C-terminal dimerforming segment led to a marked reduction in the matrix assembly activity of r70F2, the resulting monomeric r70F2 still retained a low, but significant activity to assemble into the matrix. Neither the N-terminal 70 kDa nor the C-terminal 37 kDa regions, when expressed as monomeric forms, exhibited any residual activity, suggesting that the core domain of the 37 kDa region consisting of III15 and I10 through I12 modules, termed Fib2 domain, is actively involved in the matrix assembly of r70F2. In support of the role of Fib2 domain, the proteolytic fragment derived from the 37 kDa region inhibited the assembly of r70F2. Furthermore, en bloc deletion of the Fib2 domain or deletion of the I10 through I12 modules from r70F2 resulted in a marked decrease of the matrix assembly activity.(ABSTRACT TRUNCATED AT 250 WORDS)

The role of FGF-2/HGF and fibronectin matrix on pleomorphic adenoma myoepithelial cell morphology and immunophenotype: anin vitrostudy

2014 ◽  
Vol 33 (1) ◽  
pp. 50-56
Author(s):  
Carolina Amália Barcellos Silva ◽  
Laura Cristina Leite Nardello ◽  
Frederico Windlin Garcia ◽  
Ney Soares de Araújo ◽  
Victor Angelo Montalli ◽  
...  
Keyword(s):  
Pleomorphic Adenoma ◽  
Cell Morphology ◽  
Myoepithelial Cell ◽  
Fibronectin Matrix

scholarly journals Tumor cell-organized fibronectin is required to maintain a dormant breast cancer population

2019 ◽  
Author(s):  
Lauren E. Barney ◽  
Christopher L. Hall ◽  
Alyssa D. Schwartz ◽  
Akia N. Parks ◽  
Christopher Sparages ◽  
...  
Keyword(s):  
Serum Deprivation ◽  
Cell Populations ◽  
Drug Resistant ◽  
Cell Culture System ◽  
Proliferating Cells ◽  
Fibronectin Matrix ◽  
Fibronectin Deposition

AbstractTumors can undergo long periods of dormancy, with cancer cells entering a largely quiescent, non-proliferative state before reactivation and outgrowth. For a patient, these post-remission tumors are often drug resistant and highly aggressive, resulting in poor prognosis. To understand the role of the extracellular matrix (ECM) in regulating tumor dormancy, we created anin vitrocell culture system that combines carefully controlled ECM substrates with nutrient deprivation to observe entranceintoand exitfromdormancy with live imaging. We saw that cell populations capable of surviving entrance into long-term dormancy were heterogeneous, containing quiescent, cell cycle arrested, and actively proliferating cells. Cell populations that endured extended periods of serum-deprivation-induced dormancy formed an organized, fibrillar fibronectin matrix via αvβ3and α5β1integrin adhesion, ROCK-generated tension, and TGFβ2 stimulation. We surmised that the fibronectin matrix was primarily a mediator of cell survival, not proliferation, during the serum-deprivation stress, bacause cancer cell outgrowth after dormancy required MMP-2-mediated fibronectin degradation. Given the difficulty of animal models in observing entrance and exit from dormancy in real-time, we propose this approach as a new,in vitromethod to study factors important in regulating dormancy, and we used it here to elucidate a role for fibronectin deposition and MMP activation.

scholarly journals The zebrafish presomitic mesoderm elongates through compression-extension

2021 ◽  
Author(s):  
Lewis Thomson ◽  
Leila Muresan ◽  
Benjamin Steventon
Keyword(s):  
Morphometric Analysis ◽  
Cell Tracking ◽  
Paraxial Mesoderm ◽  
Presomitic Mesoderm ◽  
Volume Increase ◽  
Extension Mechanism ◽  
Adopted Model ◽  
Vertebrate Embryos ◽  
Anterior Posterior

AbstractIn vertebrate embryos the presomitic mesoderm become progressively segmented into somites at the anterior end while extending along the anterior-posterior axis. A commonly adopted model to explain how this tissue elongates is that of posterior growth, driven in part by the addition of new cells from uncommitted progenitor populations in the tailbud. However, in zebrafish, much of somitogenesis is associated with an absence of overall volume increase and posterior progenitors do not contribute new cells until the final stages of somitogenesis. Here, we perform a comprehensive 3D morphometric analysis of the paraxial mesoderm and reveal that extension is linked to a volumetric decrease, compression in both dorsal-ventral and medio-lateral axes, and an increase in cell density. We also find that individual cells decrease in their cell volume over successive somite stages. Live cell tracking confirms that much of this tissue deformation occurs within the presomitic mesoderm progenitor zone and is associated with non-directional rearrangement. Furthermore, unlike the trunk somites that are laid down during gastrulation, tail somites develop from a tissue that can continue to elongate in the absence of functional PCP signalling. Taken together, we propose a compression-extension mechanism of tissue elongation that highlights the need to better understand the role of tissue intrinsic and extrinsic forces play in regulating morphogenesis.

The Role of Proteases in Fibronectin Matrix Remodeling in Thyroid Epithelial Cell Monolayer Cultures

2002 ◽  
Vol 383 (1) ◽  
Author(s):  
Luigi Nezi ◽  
Dario Greco ◽  
Lucio Nitsch ◽  
Corrado Garbi
Keyword(s):  
Epithelial Cell ◽  
Cell Monolayer ◽  
Matrix Remodeling ◽  
Monolayer Cultures ◽  
Fibronectin Matrix ◽  
Thyroid Epithelial Cell
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