scholarly journals Stabilization of the third fibronectin type III domain of human tenascin-C through minimal mutation and rational design

2014 ◽  
Vol 27 (10) ◽  
pp. 411-418 ◽  
Author(s):  
R. N. Gilbreth ◽  
B. M. Chacko ◽  
L. Grinberg ◽  
J. S. Swers ◽  
M. Baca
Keyword(s):  
Rational Design ◽  
Tenascin C ◽  
Type Iii ◽  
The Third ◽  
Fibronectin Type Iii ◽  
Fibronectin Type Iii Domain ◽  
Fibronectin Type

The glia-derived extracellular matrix glycoprotein tenascin-C promotes embryonic and postnatal retina axon outgrowth via the alternatively spliced fibronectin type III domain TNfnD

2008 ◽  
Vol 4 (4) ◽  
pp. 271-283 ◽  
Author(s):  
Sonia Siddiqui ◽  
Andrea Horvat-Bröcker ◽  
Andreas Faissner
Keyword(s):  
Extracellular Matrix ◽  
Neurite Outgrowth ◽  
Ganglion Cells ◽  
Axon Growth ◽  
Fc Fragment ◽  
Tenascin C ◽  
Type Iii ◽  
Fibronectin Type Iii ◽  
Fibronectin Type Iii Domain ◽  
Fibronectin Type

Tenascin-C (Tnc) is an astrocytic multifunctional extracellular matrix (ECM) glycoprotein that potentially promotes or inhibits neurite outgrowth. To investigate its possible functions for retinal development, explants from embryonic day 18 (E18) rat retinas were cultivated on culture substrates composed of poly-d-lysine (PDL), or PDL additionally coated with Tnc or laminin (LN)-1, which significantly increased fiber length. When combined with LN, Tnc induced axon fasciculation that reduced the apparent number of outgrowing fibers. In order to circumscribe the stimulatory region, Tnc-derived fibronectin type III (TNfn) domains fused to the human Ig-Fc-fragment TNfnD6-Fc, TNfnBD-Fc, TNFnA1A2-Fc and TNfnA1D-Fc were studied. The fusion proteins TNfnBD-Fc and to a lesser degree TNfnA1D-Fc were stimulatory when compared with the Ig-Fc-fragment protein without insert. In contrast, the combination TNfnA1A2-Fc reduced fiber outgrowth beneath the values obtained for the Ig-Fc domain, indicating potential inhibitory properties. The monoclonal J1/tn2 antibody (clone 578) that is specific for domain TNfnD blocked the stimulatory properties of the TNfn-Fc fusions. When postnatal day 7 retinal ganglion cells were used rather that explants, Tnc and Tnc-derived proteins proved permissive for neurite outgrowth. The present study highlights a strong retinal axon growth-promoting activity of the Tnc domain TNfnD, which is modulated by neighboring domains.

scholarly journals Tenascin-C Binds Heparin by Its Fibronectin Type III Domain Five

1995 ◽  
Vol 270 (9) ◽  
pp. 4619-4623 ◽  
Author(s):  
Peter Weber ◽  
Dieter R. Zimmermann ◽  
Kaspar H. Winterhalter ◽  
Lloyd Vaughan
Keyword(s):  
Tenascin C ◽  
Type Iii ◽  
Fibronectin Type Iii ◽  
Fibronectin Type Iii Domain ◽  
Fibronectin Type

scholarly journals Identification of the Ligand Binding Site for the Integrin α9β1in the Third Fibronectin Type III Repeat of Tenascin-C

1998 ◽  
Vol 273 (19) ◽  
pp. 11423-11428 ◽  
Author(s):  
Yasuyuki Yokosaki ◽  
Nariaki Matsuura ◽  
Shigeki Higashiyama ◽  
Isao Murakami ◽  
Masanobu Obara ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Ligand Binding Site ◽  
Tenascin C ◽  
Type Iii ◽  
The Third ◽  
Fibronectin Type Iii ◽  
Fibronectin Type

scholarly journals A targeted adenovirus vector displaying a human fibronectin type III domain-based monobody in a fiber protein

Biomaterials ◽  
2013 ◽  
Vol 34 (16) ◽  
pp. 4191-4201 ◽  
Author(s):  
Hayato Matsui ◽  
Fuminori Sakurai ◽  
Kazufumi Katayama ◽  
Yasuhiro Abe ◽  
Mitsuhiro Machitani ◽  
...  
Keyword(s):  
Adenovirus Vector ◽  
Type Iii ◽  
Fiber Protein ◽  
Fibronectin Type Iii ◽  
Human Fibronectin ◽  
Fibronectin Type Iii Domain ◽  
Fibronectin Type

scholarly journals Structural Studies of an Immunoglobulin-Fibronectin Type III Domain Tandem from Titin

2011 ◽  
Vol 100 (3) ◽  
pp. 604a
Author(s):  
Andras Czajlik ◽  
Gary Thompson ◽  
Ghulam N. Khan ◽  
Arnout Kalverde ◽  
Steve W. Homans ◽  
...  
Keyword(s):  
Structural Studies ◽  
Type Iii ◽  
Fibronectin Type Iii ◽  
Fibronectin Type Iii Domain ◽  
Fibronectin Type

scholarly journals Interaction of CREB and PGC-1α Induces Fibronectin Type III Domain-Containing Protein 5 Expression in C2C12 Myotubes

2018 ◽  
Vol 50 (4) ◽  
pp. 1574-1584 ◽  
Author(s):  
Xiu-ying Yang ◽  
Margaret C.L. Tse ◽  
Xiang Hu ◽  
Wei-hua Jia ◽  
Guan-hua Du ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Molecular Mechanisms ◽  
Metabolic Effects ◽  
Hek293 Cells ◽  
Metabolic Phenotype ◽  
C2c12 Myotubes ◽  
Type Iii ◽  
Fibronectin Type Iii ◽  
Fibronectin Type Iii Domain ◽  
Fibronectin Type

Background/Aims: Fibronectin type III domain-containing protein 5 (FNDC5), also known as irisin, is a myokine secreted from muscle in response to exercise. However, the molecular mechanisms that regulate FNDC5 expression and the functional significance of irisn in skeletal muscle remain unknown. In this study, we explored the potential pathways that induce FNDC5 expression and delineated the metabolic effects of irisin on skeletal muscle. Methods: C2C12 myotubes were treated with drugs at various concentrations and durations. The expression and activation of genes were measured by real-time polymerase chain reaction (qRT-PCR) and Western blotting. Oxidative phosphorylation was quantified by measuring the oxygen consumption rate (OCR). Results: We found that the exercise-mimicking treatment (cAMP, forskolin and isoproterenol) increased Fndc5 expression in C2C12 myotubes. CREB over-expressed C2C12 myotubes displayed higher Fndc5 expression. CREB over-expression also promoted peroxisome proliferator-activated receptor gamma coactivator 1α (PGC-1α) expression. PGC-1α-induced Fndc5 expression was blocked when the dominant negative form of CREB (S133A) was present. PGC-1α mutation (S570A) also decreased Fndc5 expression. Immunoprecipitation showed that overexpressed PGC-1α complexed with CREB in HEK293 cells. C2C12 myotubes treated with forskolin also increased endogenous CREB and PGC-1α binding. Functionally, irisin treatment increased mitochondrial respiration, enhanced ATP production, promoted fatty acid oxidation but decreased glycolysis in myotubes. Conclusion: Our observation indicates that cAMP-mediated PGC-1α/CREB interaction triggers Fndc5 expression, which acts as an autocrine/paracrine to shape the metabolic phenotype of myotubes.

scholarly journals Mertk Interacts with Tim-4 to Enhance Tim-4-Mediated Efferocytosis

Cells ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 1625 ◽  
Author(s):  
Byeongjin Moon ◽  
Juyeon Lee ◽  
Sang-Ah Lee ◽  
Chanhyuk Min ◽  
Hyunji Moon ◽  
...  
Keyword(s):  
Cell Surface ◽  
Molecular Mechanism ◽  
Soluble Form ◽  
Physical Interaction ◽  
Apoptotic Cells ◽  
Type Iii ◽  
Biochemical Interaction ◽  
Fibronectin Type Iii ◽  
Fibronectin Type Iii Domain ◽  
Fibronectin Type

Apoptotic cells expressing phosphatidylserine (PS) on their cell surface are directly or indirectly recognized by phagocytes through PS-binding proteins. The PS-binding protein Tim-4 secures apoptotic cells to phagocytes to facilitate the engulfment of apoptotic cells. However, the molecular mechanism by which Tim-4 transduces signals to phagocytes during Tim-4-mediated efferocytosis is incompletely understood. Here, we report that Tim-4 collaborates with Mertk during efferocytosis through a biochemical interaction with Mertk. Proximal localization between the two proteins in phagocytes was observed by immunofluorescence and proximal ligation assays. Physical association between Tim-4 and Mertk, which was mediated by an interaction between the IgV domain of Tim-4 and the fibronectin type-III domain of Mertk, was also detected with immunoprecipitation. Furthermore, the effect of Mertk on Tim-4-mediated efferocytosis was abolished by GST-MertkFnIII, a soluble form of the fibronectin type-III domain of Mertk that disrupts the interaction between Tim-4 and Mertk. Taken together, the results from our study suggest that a physical interaction between Tim-4 and Mertk is necessary for Mertk to enhance efferocytosis mediated by Tim-4.

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