scholarly journals Morphologies of Fibronectin Fibrils Formed under Shear Conditions and Their Cellular Adhesiveness Properties

2020 ◽  
Vol 17 (3) ◽  
pp. 113-118
Author(s):  
Phuong Thao Nguyen Thi ◽  
Quoc Phong Le ◽  
Volker R. Stoldt ◽  
Ngoc Quyen Tran ◽  
Anh Tho Le ◽  
...  
Keyword(s):  
Fibronectin Fibrils

Clathrin-mediated endocytosis and recycling of autocrine motility factor receptor to fibronectin fibrils is a limiting factor for NIH-3T3 cell motility

2000 ◽  
Vol 113 (18) ◽  
pp. 3227-3240 ◽  
Author(s):  
P.U. Le ◽  
N. Benlimame ◽  
A. Lagana ◽  
A. Raz ◽  
I.R. Nabi
Keyword(s):  
Cell Surface ◽  
Cell Motility ◽  
Endocytic Pathway ◽  
Limiting Factor ◽  
Autocrine Motility Factor ◽  
Endocytic Compartment ◽  
Motility Factor ◽  
Microtubule Disruption ◽  
Nih 3T3 ◽  
Fibronectin Fibrils

Autocrine motility factor receptor (AMF-R) is internalized via a clathrin-independent pathway to smooth endoplasmic reticulum tubules. This endocytic pathway is shown here to be inhibited by methyl-(beta)-cyclodextrin (m(beta)CD) implicating caveolae or caveolae-like structures in AMF internalization to smooth ER. AMF-R is also internalized via a clathrin-dependent pathway to a transferrin receptor-negative, LAMP-1/lgpA-negative endocytic compartment identified by electron microscopy as a multivesicular body (MVB). Endocytosed AMF recycles to cell surface fibrillar structures which colocalize with fibronectin; AMF-R recycling is inhibited at 20 degrees C, which blocks endocytosis past the early endosome, but not by m(beta)CD demonstrating that AMF-R recycling to fibronectin fibrils is mediated by clathrin-dependent endocytosis to MVBs. Microtubule disruption with nocodazole did not affect delivery of bAMF to cell surface fibrils indicating that recycling bAMF traverses the MVB but not a later endocytic compartment. Plating NIH-3T3 cells on an AMF coated substrate did not specifically affect cell adhesion but prevented bAMF delivery to cell surface fibronectin fibrils and reduced cell motility. AMF-R internalization and recycling via the clathrin-mediated pathway are therefore rate-limiting for cell motility. This recycling pathway to the site of deposition of fibronectin may be implicated in the de novo formation of cellular attachments or the remodeling of the extracellular matrix during cell movement.

Degradation of Fibronectin Fibrils by Matrilysin and Characterization of the Degradation Products

1995 ◽  
Vol 221 (1) ◽  
pp. 83-91 ◽  
Author(s):  
D.C. von Bredow ◽  
R.B. Nagle ◽  
G.T. Bowden ◽  
A.E. Cress
Keyword(s):  
Degradation Products ◽  
Fibronectin Fibrils

Establishment of substratum polarity in the blastocoel roof of the Xenopus embryo

Development ◽  
1999 ◽  
Vol 126 (9) ◽  
pp. 1975-1984 ◽  
Author(s):  
M. Nagel ◽  
R. Winklbauer
Keyword(s):  
Extracellular Matrix ◽  
Cell Migration ◽  
Signaling Pathways ◽  
Fibril Formation ◽  
Fgf Signaling ◽  
Matrix Assembly ◽  
Mesoderm Cell ◽  
Guidance Cues ◽  
Mesoderm Formation ◽  
Fibronectin Fibrils

The fibronectin fibril matrix on the blastocoel roof of the Xenopus gastrula contains guidance cues that determine the direction of mesoderm cell migration. The underlying guidance-related polarity of the blastocoel roof is established in the late blastula under the influence of an instructive signal from the vegetal half of the embryo, in particular from the mesoderm. Formation of an oriented substratum depends on functional activin and FGF signaling pathways in the blastocoel roof. Besides being involved in tissue polarization, activin and FGF also affect fibronectin matrix assembly. Activin treatment of the blastocoel roof inhibits fibril formation, whereas FGF modulates the structure of the fibril network. The presence of intact fibronectin fibrils is permissive for directional mesoderm migration on the blastocoel roof extracellular matrix.

scholarly journals Role of Fibronectin in Primary Open Angle Glaucoma

Cells ◽  
2019 ◽  
Vol 8 (12) ◽  
pp. 1518 ◽  
Author(s):  
Jennifer A. Faralli ◽  
Mark S. Filla ◽  
Donna M. Peters
Keyword(s):  
United States ◽  
Trabecular Meshwork ◽  
Vision Loss ◽  
Primary Open Angle Glaucoma ◽  
Open Angle Glaucoma ◽  
The United States ◽  
Open Angle ◽  
Cell Matrix ◽  
Fibronectin Fibrils

Primary open angle glaucoma (POAG) is the most common form of glaucoma and the 2nd most common cause of irreversible vision loss in the United States. Nearly 67 million people have the disease worldwide including >3 million in the United States. A major risk factor for POAG is an elevation in intraocular pressure (IOP). The increase in IOP is believed to be caused by an increase in the deposition of extracellular matrix proteins, in particular fibronectin, in a region of the eye known as the trabecular meshwork (TM). How fibronectin contributes to the increase in IOP is not well understood. The increased density of fibronectin fibrils is thought to increase IOP by altering the compliance of the trabecular meshwork. Recent studies, however, also suggest that the composition and organization of fibronectin fibrils would affect IOP by changing the cell-matrix signaling events that control the functional properties of the cells in the trabecular meshwork. In this article, we will discuss how changes in the properties of fibronectin and fibronectin fibrils could contribute to the regulation of IOP.

scholarly journals Fibrillin Assembly Requires Fibronectin

2009 ◽  
Vol 20 (3) ◽  
pp. 846-858 ◽  
Author(s):  
Laetitia Sabatier ◽  
Daliang Chen ◽  
Christine Fagotto-Kaufmann ◽  
Dirk Hubmacher ◽  
Marc D. McKee ◽  
...  
Keyword(s):  
Dermal Fibroblasts ◽  
Terminal Region ◽  
Electron Microscopic Level ◽  
Binding Assays ◽  
Electron Microscopic ◽  
Binding Interaction ◽  
Fibrillin 1 ◽  
And Function ◽  
Sirna Knockdown ◽  
Fibronectin Fibrils

Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and nonelastic extracellular matrices. Proper assembly mechanisms are central to the formation and function of these microfibrils, and their properties are often compromised in pathological circumstances such as in Marfan syndrome and in other fibrillinopathies. Here, we have used human dermal fibroblasts to analyze the assembly of fibrillin-1 in dependence of other matrix-forming proteins. siRNA knockdown experiments demonstrated that the assembly of fibrillin-1 is strictly dependent on the presence of extracellular fibronectin fibrils. Immunolabeling performed at the light and electron microscopic level showed colocalization of fibrillin-1 with fibronectin fibrils at the early stages of the assembly process. Protein-binding assays demonstrated interactions of fibronectin with a C-terminal region of fibrillin-1, -2, and -3 and with an N-terminal region of fibrillin-1. The C-terminal half of fibrillin-2 and -3 had propensities to multimerize, as has been previously shown for fibrillin-1. The C-terminal of all three fibrillins interacted strongly with fibronectin as multimers, but not as monomers. Mapping studies revealed that the major binding interaction between fibrillins and fibronectin involves the collagen/gelatin-binding region between domains FNI6 and FNI9.

scholarly journals Fibronectin fibrils regulate TGF-β1-induced Epithelial-Mesenchymal Transition

2017 ◽  
Vol 60-61 ◽  
pp. 157-175 ◽  
Author(s):  
Lauren A. Griggs ◽  
Nadiah T. Hassan ◽  
Roshni S. Malik ◽  
Brian P. Griffin ◽  
Brittany A. Martinez ◽  
...  
Keyword(s):  
Epithelial Mesenchymal Transition ◽  
Mesenchymal Transition ◽  
Fibronectin Fibrils ◽  
Tgf Β1

scholarly journals Molecular architecture of native fibronectin fibrils

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Susanna Maria Früh ◽  
Ingmar Schoen ◽  
Jonas Ries ◽  
Viola Vogel
Keyword(s):  
Molecular Architecture ◽  
Fibronectin Fibrils

Assembly of fibronectin fibrils by fibroblasts cultured within an attached collagen lattice

1991 ◽  
Vol 49 ◽  
pp. 180-181
Author(s):  
J. J. Tomasek
Keyword(s):  
Potential Role ◽  
Model System ◽  
Palmar Fascia ◽  
Cellular Mechanisms ◽  
Tension Development ◽  
Collagen Lattice ◽  
Tissue Contraction ◽  
Fibronectin Fibrils ◽  
Develop Tension ◽  
Collagen Lattices

Dupuytren's disease is characterized by a contraction of the palmar fascia resulting in irreversible flexion of the affected digits. Collagen lattices provide a model system for studying the cellular mechanisms of tissue contraction. Fibroblasts cultured within an attached collagen lattice resemble the myofibroblasts present in the diseased tissue. They form bundles of actin microfilaments, assemble fibronectin fibrils and form a specialized transmembrane association (fibronexus) linking the two filament systems. In addition, fibroblasts cultured in an attached collagen lattice will develop tension which results in rapid lattice retraction upon mechanical release from the underlying substratum. In this study we examined fibronectin fibril assembly in an attached collagen lattice and the potential role these fibrils play in tension development.

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