WARP: A Unique Extracellular Matrix Component of Cartilage, Muscle, and Endothelial Cell Basement Membranes

2019 ◽  
Vol 303 (6) ◽  
pp. 1619-1623 ◽  
Author(s):  
Jamie Fitzgerald
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cell ◽  
Basement Membranes ◽  
Extracellular Matrix Component ◽  
Matrix Component

scholarly journals Evidence of Swim secretion and association with extracellular matrix in the Drosophila embryo

2021 ◽  
Author(s):  
Valeria Kaltezioti ◽  
Katerina M. Vakaloglou ◽  
Aristidis S. Charonis ◽  
Christos G. Zervas
Keyword(s):  
Extracellular Matrix ◽  
Expression System ◽  
Ectopic Expression ◽  
Basement Membranes ◽  
Confocal Imaging ◽  
Drosophila Embryo ◽  
Dependent Manner ◽  
Extracellular Matrix Component ◽  
Matrix Component

Secreted wingless-interacting protein (Swim) is the Drosophila ortholog gene of the mammalian Tubulointerstitial Nephritis Antigen Like 1 (TINAGL1), known also as lipocalin-7 (LCN7), or adrenocortical zonation factor 1 (AZ-1). Swim and TINAGL1 proteins share a significant homology, including the somatomedin B and the predictive inactive C1 cysteine peptidase domains. In mammals, both TINAGL1 and its closely related homolog TINAG have been identified in basement membranes, where they may function as modulators of integrin-mediated adhesion. In Drosophila, Swim was initially identified in the eggshell matrix and subsequently was detected in the culture medium of S2 cells. Further biochemical analysis indicated that Swim binds to wingless (wg) in a lipid-dependent manner. This observation together with RNAiknockdown studies suggested that Swim is an essential cofactor of wg-signalling. However, recent elegant genetic studies ruled out the possibility that Swim is required alone to facilitate wgsignalling in Drosophila, because flies without Swim are viable and fertile. Here, we use the UAS/Gal4 expression system together with confocal imaging to analyze the in vivo localization of a chimeric Swim-GFP in the developing Drosophila embryo. Our data fully support the notion that Swim is an extracellular matrix component that upon ectopic expression is secreted and preferentially associates with the basement membranes of various organs and with the specialized tendon matrix at the muscle attachment sites (MAS). Interestingly, the accumulation of Swim at the MAS does not require integrins. In conclusion, Swim is an extracellular matrix component, and it is possible that Swim exhibits overlapping functions in concert with other undefined components.

scholarly journals Unique distribution of the extracellular matrix component thrombospondin in the developing mouse embryo.

1988 ◽  
Vol 107 (6) ◽  
pp. 2737-2748 ◽  
Author(s):  
K S O'Shea ◽  
V M Dixit
Keyword(s):  
Extracellular Matrix ◽  
Peripheral Nerve ◽  
Mouse Embryo ◽  
Basement Membranes ◽  
Extracellular Matrices ◽  
Immunocytochemical Localization ◽  
Extracellular Matrix Component ◽  
Cortical Layers ◽  
Matrix Component ◽  
Unique Distribution

Immunocytochemical localization of thrombospondin (TSP), a trimeric glycoprotein constituent of extracellular matrices, produced striking regional and temporal patterns of distribution in the developing mouse embryo. TSP was present in many basement membranes, surrounded epithelial cells, and was associated with peripheral nerve outgrowth. During organogenesis, TSP was also found on the surface of myoblasts and chondroblasts, and TSP was differentially deposited in cortical layers. With differentiation of chondrocytes and myotubes immunoreactivity was decreased, and differential cortical staining was lost. Presence of TSP was associated with morphogenetic processes of proliferation, migration, and intercellular adhesion.

scholarly journals Hyperglycaemia and aberrated insulin signalling stimulate tumour progression via induction of the extracellular matrix component hyaluronan

2017 ◽  
Vol 141 (4) ◽  
pp. 791-804 ◽  
Author(s):  
Sören Twarock ◽  
Christina Reichert ◽  
Ulrike Peters ◽  
Daniel J. Gorski ◽  
Katharina Röck ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Insulin Signalling ◽  
Tumour Progression ◽  
Extracellular Matrix Component ◽  
Matrix Component

The impact of age on cardiac function and extracellular matrix component expression in adverse post-infarction remodeling in mice

2019 ◽  
Vol 119 ◽  
pp. 193-202 ◽  
Author(s):  
Felix Nagel ◽  
David Santer ◽  
Stefan Stojkovic ◽  
Christoph Kaun ◽  
Anne-Kristin Schaefer ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cardiac Function ◽  
Extracellular Matrix Component ◽  
Matrix Component ◽  
The Impact

scholarly journals Fibrinogen induces endothelial cell adhesion and spreading via the release of endogenous matrix proteins and the recruitment of more than one integrin receptor

Blood ◽  
1990 ◽  
Vol 75 (7) ◽  
pp. 1509-1517 ◽  
Author(s):  
E Dejana ◽  
MG Lampugnani ◽  
M Giorgi ◽  
M Gaboli ◽  
PC Marchisio
Keyword(s):  
Endothelial Cell ◽  
Matrix Protein ◽  
Matrix Proteins ◽  
Extracellular Matrix Component ◽  
Integrin Receptor ◽  
Complex Type ◽  
Matrix Component ◽  
Cytoskeletal Organization ◽  
Subendothelial Matrix ◽  
Alpha V Beta 3

Abstract We have previously shown that fibrinogen (fg) acts as a subendothelial matrix protein in promoting human endothelial cell (EC) adhesion and cytoskeletal organization. In this study we report that EC spreading on fg, at variance with other matrix proteins, requires endogenous matrix protein synthesis and secretion. ECs, upon seeding on fg, promptly released and organized a fibronectin (fn) matrix. Fg was more effective than vitronectin (vn) in promoting the deposition of this protein. ECs treated with monensin to block matrix protein secretion still adhered to fg but did not properly organize their cytoskeleton and adhesion structures. In contrast, monensin did not affect EC spreading either on vn or on fn. Using antibodies to the alpha and beta chains of fn (alpha 5 beta 1) and vn (alpha v beta 3) receptors, it was found that ECs adherent to fg show clustering and organization in adhesion structures of both type of receptors. A faint staining of adhesion structures with alpha 2 but not alpha 3 and alpha 6 antibodies was also observed. Antibodies either to vn or fn receptors were able to disrupt the EC monolayer and to induce EC retraction and detachment, thus indicating that both receptors are important in maintaining a sustained EC adhesion to fg. However, when ECs were treated with monensin only the vn receptor was organized in adhesion structures while the fn receptor was diffusely distributed. This suggests that clustering of the fn receptor is mediated by the release of endogenous matrix proteins induced by the exposure to fg. In conclusion, fg has a peculiar and complex type of interaction with ECs since it requires endogenous matrix protein release and the recruitment of more than one adhesive receptor. This suggests a specific way of response of ECs to each extracellular matrix component.

scholarly journals Cartilage link protein 1 (Crtl1), an extracellular matrix component playing an important role in heart development

2007 ◽  
Vol 310 (2) ◽  
pp. 291-303 ◽  
Author(s):  
Elaine E. Wirrig ◽  
Brian S. Snarr ◽  
Mastan R. Chintalapudi ◽  
Jessica L. O'Neal ◽  
Aimee L. Phelps ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Heart Development ◽  
Extracellular Matrix Component ◽  
Matrix Component ◽  
Link Protein
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