scholarly journals Fibronectin Deposition Participates in Extracellular Matrix Assembly and Vascular Morphogenesis

PLoS ONE ◽  
2016 ◽  
Vol 11 (1) ◽  
pp. e0147600 ◽  
Author(s):  
Abigail Hielscher ◽  
Kim Ellis ◽  
Connie Qiu ◽  
Josh Porterfield ◽  
Sharon Gerecht
Keyword(s):  
Extracellular Matrix ◽  
Matrix Assembly ◽  
Vascular Morphogenesis ◽  
Fibronectin Deposition

scholarly journals pVHL Function Is Essential for Endothelial Extracellular Matrix Deposition

2006 ◽  
Vol 26 (7) ◽  
pp. 2519-2530 ◽  
Author(s):  
Nan Tang ◽  
Fiona Mack ◽  
Volker H. Haase ◽  
M. Celeste Simon ◽  
Randall S. Johnson
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Critical Role ◽  
Matrix Assembly ◽  
Developmental Defects ◽  
Vhl Gene ◽  
Matrix Deposition ◽  
Fibronectin Deposition

ABSTRACT The tumor suppressor von Hippel-Lindau protein (pVHL) is critical for cellular molecular oxygen sensing, acting to target degradation of the hypoxia-inducible factor alpha transcription factor subunits under normoxic conditions. We have found that independent of its function in regulating hypoxic response, the VHL gene plays a critical role in embryonic endothelium development through regulation of vascular extracellular matrix assembly. We created mice lacking the VHL gene in endothelial cells; these conditional null mice died at the same stage as homozygous VHL-null mice, with similar vascular developmental defects. These included defective vasculogenesis in the placental labyrinth, a collapsed endocardium, and impaired vessel network patterning. The defects in embryonic vascularization were correlated with a diminished vascular fibronectin deposition in vivo and defective endothelial extracellular fibronectin assembly in vitro. We found that the impaired migration and adhesion of VHL-null endothelial cells can be partially rescued by the addition of back exogenous fibronectin, which indicates that pVHL regulation of fibronectin deposition plays an important functional role in vascular patterning and maintenance of vascular integrity.

A novel role for alpha 3 beta 1 integrins in extracellular matrix assembly

1995 ◽  
Vol 108 (6) ◽  
pp. 2511-2523 ◽  
Author(s):  
C. Wu ◽  
A.E. Chung ◽  
J.A. McDonald
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Binding Activity ◽  
Integrin Subunit ◽  
Pericellular Matrix ◽  
Matrix Assembly ◽  
Amino Terminal ◽  
Beta 1 Integrin ◽  
Fibronectin Deposition

To study the biological role of alpha 3 beta 1 integrins in cell adhesion, migration, and in the deposition of extracellular matrix, we stably expressed the human alpha 3 integrin subunit in the alpha 4, alpha 5 integrin deficient CHO cell line B2. The expression of alpha 3 beta 1 integrins enhanced cell adhesion on entactin (also known as nidogen), but not on fibronectin. Using recombinant GST-fusion proteins that span the entire length of the entactin molecule, we located cell adhesive activity to the G2 domain of entactin. These results suggest that the alpha 3 beta 1 integrin functions as an adhesion receptor interacting with the G2 domain of entactin. On the other hand, the expression of alpha 3 beta 1 integrins did not confer the ability to migrate on entactin. Strikingly, the expression of alpha 3 beta 1 dramatically increased the deposition of entactin and fibronectin into the pericellular matrix. This was accompanied by increased binding activity of the 29 kDa amino-terminal domain of fibronectin. Thus, similar to alpha 5 beta 1 integrins, alpha 3 beta 1 integrins can play an important role in modulating the assembly of pericellular matrices. However, unlike fibronectin deposition supported by alpha 5 beta 1, alpha 3 beta 1 supported fibronectin deposition into pericellular matrix was not inhibited by antibodies binding to the RGD containing cell adhesion domain of fibronectin, demonstrating that the two processes are mechanistically distinct. The role of alpha 3 beta 1 in pericellular matrix assembly potentially implicates this receptor in the assembly and/or recognition of entactin-containing pericellular matrices, an observation consistent with its apparent role in the renal glomerulus of the mammalian kidney.

Hyaluronic acid drives mesenchymal stromal cell-derived extracellular matrix assembly by promoting fibronectin fibrillogenesis

2021 ◽  
Author(s):  
Marisa Assunção ◽  
Chi Him Kendrick Yiu ◽  
Ho-Ying Wan ◽  
Dan Wang ◽  
Dai Fei Elmer Ker ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Hyaluronic Acid ◽  
Mesenchymal Stromal Cell ◽  
Stromal Cell ◽  
Matrix Assembly ◽  
Fibronectin Deposition

Hyaluronic acid (HA) is present at sites of ongoing fibronectin fibrillogenesis (fibrillar adhesions) and necessary for efficient fibronectin fibrillogenesis. As a result, fibronectin deposition can be enhanced by exogenous HA.

scholarly journals EPB41L5 controls podocyte extracellular matrix assembly by adhesome-dependent force transmission

Cell Reports ◽  
2021 ◽  
Vol 34 (12) ◽  
pp. 108883
Author(s):  
Jasmin I. Maier ◽  
Manuel Rogg ◽  
Martin Helmstädter ◽  
Alena Sammarco ◽  
Oliver Schilling ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Force Transmission ◽  
Matrix Assembly

Construction of 3-D Cellular Multi-Layers with Extracellular Matrix Assembly Using Magnetic Nanoparticles

2016 ◽  
Vol 12 (10) ◽  
pp. 1916-1928 ◽  
Author(s):  
Yu Bin Lee ◽  
Joong-Yup Lee ◽  
Taufiq Ahmad ◽  
Seongwoo Bak ◽  
Jinkyu Lee ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Magnetic Nanoparticles ◽  
Matrix Assembly

The localized assembly of extracellular matrix integrin ligands requires cell-cell contact

2000 ◽  
Vol 113 (21) ◽  
pp. 3715-3723 ◽  
Author(s):  
M.D. Martin-Bermudo ◽  
N.H. Brown
Keyword(s):  
Extracellular Matrix ◽  
Drosophila Embryo ◽  
Cell Contact ◽  
Primary Role ◽  
Dependent Manner ◽  
Muscle Attachment ◽  
Matrix Assembly ◽  
Attachment Sites ◽  
Genetically Manipulated ◽  
Cell Cell

The assembly of an organism requires the interaction between different layers of cells, in many cases via an extracellular matrix. In the developing Drosophila larva, muscles attach in an integrin-dependent manner to the epidermis, via a specialized extracellular matrix called tendon matrix. Tiggrin, a tendon matrix integrin ligand, is primarily synthesized by cells distant to the muscle attachment sites, yet it accumulates specifically at these sites. Previous work has shown that the PS integrins are not required for tiggrin localization, suggesting that there is redundancy among tiggrin receptors. We have examined this by testing whether the PS2 integrin can recruit tiggrin to ectopic locations within the Drosophila embryo. We found that neither the wild type nor modified forms of the PS2 integrin, which have higher affinity for tiggrin, can recruit tiggrin to new cellular contexts. Next, we genetically manipulated the fate of the muscles and the epidermal muscle attachment cells, which demonstrated that muscles have the primary role in recruiting tiggrin to the tendon matrix and that cell-cell contact is necessary for this recruitment. Thus we propose that the inherent polarity of the muscle cells leads to a molecular specialization of their ends, and interactions between the ends produces an integrin-independent tiggrin receptor. Thus, interaction between cells generates an extracellular environment capable of nucleating extracellular matrix assembly.

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