scholarly journals The polycystin-1 C-type lectin domain binds carbohydrate in a calcium-dependent manner, and interacts with extracellular matrix proteins in vitro

2001 ◽  
Vol 1536 (2-3) ◽  
pp. 161-176 ◽  
Author(s):  
Benjamin S Weston ◽  
Claire Bagnéris ◽  
Robert G Price ◽  
John L Stirling
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Dependent Manner ◽  
Lectin Domain ◽  
Calcium Dependent

scholarly journals Trypanosoma cruzi activates mouse cardiac fibroblasts in vitro leading to fibroblast-myofibroblast transition and increase in expression of extracellular matrix proteins

2018 ◽  
Vol 11 (1) ◽  
Author(s):  
Laura Lacerda Coelho ◽  
Isabela Resende Pereira ◽  
Mirian Claudia de Souza Pereira ◽  
Liliane Mesquita ◽  
Joseli Lannes-Vieira ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Trypanosoma Cruzi ◽  
Cardiac Fibroblasts ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins

scholarly journals Complete primary structure of a calcium-dependent serine proteinase capable of degrading extracellular matrix proteins

FEBS Letters ◽  
1989 ◽  
Vol 250 (2) ◽  
pp. 411-415 ◽  
Author(s):  
Hirohisa Kinoshita ◽  
Hisako Sakiyama ◽  
Kastuo Tokunaga ◽  
Shinobu Imajoh-Ohmi ◽  
Yoshio Hamada ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Primary Structure ◽  
Serine Proteinase ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Calcium Dependent ◽  
Complete Primary Structure

In vitro evaluation of antagonism, modulation of cytokines and extracellular matrix proteins by Bifidobacterium strains

2018 ◽  
Vol 67 (5) ◽  
pp. 497-505 ◽  
Author(s):  
A.K.S. Silva ◽  
T.R.N. Silva ◽  
J.R. Nicoli ◽  
L.M.C. Vasquez-Pinto ◽  
F.S. Martins
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
In Vitro Evaluation

Identification of a new C-type lectin, TES-70, secreted by infective larvae of Toxocara canis, which binds to host ligands

Parasitology ◽  
2000 ◽  
Vol 121 (5) ◽  
pp. 545-554 ◽  
Author(s):  
A. LOUKAS ◽  
A. DOEDENS ◽  
M. HINTZ ◽  
R. M. MAIZELS
Keyword(s):  
Immune Cell ◽  
Sequence Similarity ◽  
Mannose Receptor ◽  
Toxocara Canis ◽  
Dependent Manner ◽  
Expression Screening ◽  
Lectin Domain ◽  
Calcium Dependent ◽  
Infective Larvae

Infective larvae of the dog roundworm Toxocara canis survive in the tissues of their hosts for extended periods in a state of developmental arrest, successfully evading immune destruction. This survival strategy is thought to be mediated by T. canis excretory/secretory (TES) products which downregulate or divert the immune response. We purified one of the major TES products, TES-70 and gained amino acid sequence from 4 tryptic peptides. These peptides were matched to a predicted protein from a cDNA that was isolated by expression screening a T. canis cDNA library with mouse anti-TES serum. The predicted protein (Tc-CTL-4) is similar to, but larger than, Tc-CTL-1, a 32-kDa C-type lectin secreted by T. canis larvae. Tc-CTL-4 has a signal peptide, 2 Cys-rich domains and a C-terminal calcium-dependent C-type lectin domain that shares sequence similarity with host immune cell receptors such as macrophage mannose receptor and CD23. The lectin domain was expressed in bacteria and antiserum to the purified recombinant protein was used to confirm that Tc-ctl-4 did encode the native TES-70 glycoprotein. TES-70 selectively bound to ligands on the surface of Madin–Darby Canine Kidney cells in vitro in a calcium-dependent manner, inhibitable by mammalian serum, indicating that a host glycan is the native ligand for this new parasite lectin.

Von Willebrand Factor Binds to the Endothelial Growth Factor Angiopoietin-2 Both within Endothelial Cells and Upon Release From Weibel Palade Bodies

Blood ◽  
2011 ◽  
Vol 118 (21) ◽  
pp. 698-698 ◽  
Author(s):  
Thomas A J Mckinnon ◽  
Richard D Starke ◽  
Kushani Ediriwickrema ◽  
Anna Maria Randi ◽  
Michael Laffan
Keyword(s):  
Extracellular Matrix ◽  
Endothelial Cells ◽  
Von Willebrand Factor ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Dependent Manner ◽  
Platelet Receptor ◽  
Angiopoietin 2 ◽  
Von Willebrand ◽  
Willebrand Factor

Abstract Abstract 698 Von Willebrand Factor (VWF) is a large multimeric plasma glycoprotein essential for homeostasis, also involved in inflammation and angiogenesis. The majority of VWF is synthesised by endothelial cells (EC) and is either constitutively secreted or stored in Weibel-Palade bodies (WPB), ready to be released in response to endothelial stimulation. Several studies have shown that formation of WPB is dependent on the presence of VWF, and deletion of VWF in human umbilical vein EC (HUVEC) results in loss of WPB. Amongst the other proteins shown to co-localise to WPB is angiopoietin-2 (Ang2), a ligand of the receptor tyrosine kinase Tie-2. Ang2 regulates endothelial cell survival, vascular stability and maturation, by destabilizing quiescent endothelium and facilitating the response to inflammatory and angiogenic stimuli. VWF is required for storage of Ang2, and release of Ang-2 from EC is increased in VWF-deficient HUVEC. Recently, we have shown that VWF itself regulates angiogenesis, raising the hypothesis that some of the angiogenic activity of VWF may be mediated by Ang-2. In the present study we investigated the interaction between Ang2 and VWF. Binding analysis demonstrated that recombinant human Ang2 bound to purified plasma-derived VWF in a pH and calcium dependent manner, with optimal binding occurring at pH 6.5 and 10mM calcium, indicative of binding within the Golgi body. Generation of binding isotherms established that Ang2 bound to VWF with high affinity (KD∼3nM); furthermore binding affinity was not dependent on VWF conformation. Using an array of VWF constructs we determined that Ang2 bound predominantly to the VWF A1 domain, which also contains binding sites to the platelet receptor GPIb and extracellular matrix proteins. Co-immunoprecipitation experiments performed on TNFα- and ionomycin-stimulated HUVECs, to induce WPB exocytosis, confirmed that a portion of Ang2 remained bound to secreted VWF. Moreover, immunofluorescence staining of histamine-stimulated HUVECs to induce VWF release demonstrated the presence of Ang2 on VWF strings secreted from ECs. Finally we demonstrated that Ang2 bound to VWF was still able to interact with Tie-2. These data demonstrate that binding of Ang2 to VWF occurs within the cell; we propose that this is the mechanism mediating storage of Ang2 in WPB. Moreover, the finding that the Ang2-VWF interaction is preserved following secretion raises the intriguing possibility VWF may affect Ang2 function, possibly by localising Ang2 to the Tie 2 receptor under the shear forces experienced in flowing blood. Similarly, Ang-2 binding to VWF may modulate its interaction with receptors and extracellular matrix proteins, and ultimately influence the role of VWF in the angiogenic processes. Disclosures: No relevant conflicts of interest to declare.

Effect of extracellular matrix proteins on in vitro testosterone production by rat Leydig cells

2002 ◽  
Vol 61 (4) ◽  
pp. 493-503 ◽  
Author(s):  
Emilce S. Diaz ◽  
Eliana Pellizzari ◽  
Silvina Meroni ◽  
Selva Cigorraga ◽  
Livia Lustig ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Leydig Cells ◽  
Extracellular Matrix Proteins ◽  
Matrix Proteins ◽  
Testosterone Production
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