scholarly journals Extracellular Matrix Assembly in Diatoms (Bacillariophyceae) (II. 2,6-Dichlorobenzonitrile Inhibition of Motility and Stalk Production in the Marine Diatom Achnanthes longipes)

1997 ◽  
Vol 113 (4) ◽  
pp. 1071-1080 ◽  
Author(s):  
Y. Wang ◽  
J. Lu ◽  
J. C. Mollet ◽  
M. R. Gretz ◽  
K. D. Hoagland
Keyword(s):  
Extracellular Matrix ◽  
Marine Diatom ◽  
Matrix Assembly ◽  
Achnanthes Longipes

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.

Control of extracellular matrix assembly by syndecan-2 proteoglycan

2000 ◽  
Vol 113 (3) ◽  
pp. 493-506 ◽  
Author(s):  
C.M. Klass ◽  
J.R. Couchman ◽  
A. Woods
Keyword(s):  
Extracellular Matrix ◽  
Chinese Hamster ◽  
Surface Expression ◽  
Metabolic Labeling ◽  
Sulfate Proteoglycan ◽  
S2 Cells ◽  
Matrix Assembly ◽  
The Matrix ◽  
Beta1 Integrin ◽  
Assembly Defect

Extracellular matrix (ECM) deposition and organization is maintained by transmembrane signaling and integrins play major roles. We now show that a second transmembrane component, syndecan-2 heparan sulfate proteoglycan, is pivotal in matrix assembly. Chinese Hamster Ovary (CHO) cells were stably transfected with full length (S2) or truncated syndecan-2 lacking the C-terminal 14 amino acids of the cytoplasmic domain (S2deltaS). No differences in the amount of matrix assembly were noted with S2 cells, but those expressing S2deltaS could not assemble laminin or fibronectin into a fibrillar matrix. The loss of matrix formation was not caused by a failure to synthesize or externalize ECM components as determined by metabolic labeling or due to differences in surface expression of alpha5 or beta1 integrin. The matrix assembly defect was at the cell surface, since S2deltaS cells also lost the ability to rearrange laminin or fibronectin substrates into fibrils and to bind exogenous fibronectin. Transfection of activated alphaIIbalphaLdeltabeta3 integrin into alpha(5)-deficient CHO B2 cells resulted in reestablishment of the previously lost fibronectin matrix. However, cotransfection of this cell line with S2deltaS could override the presence of activated integrins. These results suggest a regulatory role for syndecan-2 in matrix assembly, along with previously suggested roles for activated integrins.

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 Challenges in Fabrication of Tissue-Engineered Cartilage with Correct Cellular Colonization and Extracellular Matrix Assembly

2018 ◽  
Vol 19 (9) ◽  
pp. 2700 ◽  
Author(s):  
Mikko Lammi ◽  
Juha Piltti ◽  
Juha Prittinen ◽  
Chengjuan Qu
Keyword(s):  
Extracellular Matrix ◽  
Articular Cartilage ◽  
Pore Size ◽  
Cartilage Tissue ◽  
Cellular Interactions ◽  
Matrix Assembly ◽  
Small Pore ◽  
Culture Models ◽  
Open Question ◽  
Engineered Cartilage

A correct articular cartilage ultrastructure regarding its structural components and cellularity is important for appropriate performance of tissue-engineered articular cartilage. Various scaffold-based, as well as scaffold-free, culture models have been under development to manufacture functional cartilage tissue. Even decellularized tissues have been considered as a potential choice for cellular seeding and tissue fabrication. Pore size, interconnectivity, and functionalization of the scaffold architecture can be varied. Increased mechanical function requires a dense scaffold, which also easily restricts cellular access within the scaffold at seeding. High pore size enhances nutrient transport, while small pore size improves cellular interactions and scaffold resorption. In scaffold-free cultures, the cells assemble the tissue completely by themselves; in optimized cultures, they should be able to fabricate native-like tissue. Decellularized cartilage has a native ultrastructure, although it is a challenge to obtain proper cellular colonization during cell seeding. Bioprinting can, in principle, provide the tissue with correct cellularity and extracellular matrix content, although it is still an open question as to how the correct molecular interaction and structure of extracellular matrix could be achieved. These are challenges facing the ongoing efforts to manufacture optimal articular cartilage.

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