Relevant bibliographies by topics / Fibulin-3

Academic literature on the topic 'Fibulin-3'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Fibulin-3"

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Hulleman, John D., Steven J. Brown, Hugh Rosen, and Jeffery W. Kelly. "A High-Throughput Cell-Based Gaussia Luciferase Reporter Assay for Identifying Modulators of Fibulin-3 Secretion." Journal of Biomolecular Screening 18, no. 6 (December 10, 2012): 647–58. http://dx.doi.org/10.1177/1087057112469405.

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An R345W mutation in fibulin-3 causes its inefficient secretion, increased intracellular steady-state levels, and the macular dystrophy, Malattia Leventinese (ML), a disease similar to age-related macular degeneration. It is unknown whether R345W causes ML through increased intracellular levels, by the secretion of a potentially aggregation-prone protein, or both. To identify small molecules that alter the secretion of fibulin-3, we developed ARPE19 retinal cell lines that inducibly express wild-type (WT) or R345W fibulin-3 fused to an enhanced Gaussia luciferase (eGLuc2). Screening of the Library of Pharmacologically Active Compounds demonstrated that these cell lines and the GLuc assay are suitable for high-throughput chemical screening. Two estrogen-related compounds enhanced fibulin-3 secretion, whereas a diverse series of small molecules reduced fibulin-3 secretion. A counterscreen identified compounds that did not substantially alter the secretion of unfused eGLuc2, demonstrating at least partial selectivity for fibulin-3. A secondary assay using untagged fibulin-3 confirmed that the top three inhibitory compounds reduced R345W fibulin-3 secretion. Interestingly, in untagged fibulin-3 studies, one compound, phorbol 12-myristate 13-acetate, reduced R345W fibulin-3 secretion while minimally enhancing WT fibulin-3 secretion, the desired activity and selectivity we sought for ML. The identified compounds could serve as tools for probing the etiology of fibulin-3–related diseases.
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Jiang, Zhaoqiang, Shibo Ying, Wei Shen, Xianglei He, Junqiang Chen, Hailing Xia, Min Yu, et al. "Plasma Fibulin-3 as a Potential Biomarker for Patients with Asbestos-Related Diseases in the Han Population." Disease Markers 2017 (2017): 1–8. http://dx.doi.org/10.1155/2017/1725354.

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Fibulin-3 has been reported as a potential biomarker for mesothelioma. However, little is known about the diagnostic efficacies of fibulin-3 for asbestos-related diseases (ARDs) in China. This study was to investigate the utility of fibulin-3 for asbestos exposure and ARDs. A total of 430 subjects were recruited from Southeast China, including healthy individuals, asbestos-exposed (AE) individuals, and patients with pleural plaques (PP), asbestosis, and malignant pleural mesothelioma (MPM). Plasma fibulin-3 was measured using the enzyme-linked immunosorbent assay. Linear regression analyses were applied to explore the influencing factors of fibulin-3. Receiver operating characteristic curves were used to determine the cutoff values. The median fibulin-3 level of subjects in the mesothelioma group was higher than that in other groups. Subjects in the asbestosis group had higher median fibulin-3 level than those in the control group. A higher fibulin-3 level was found in the group with ≥10 years of asbestos exposure as compared with control groups. The AUCs of fibulin-3 for distinguishing MPM subjects from control, AE, PP, and asbestosis subjects were 0.92, 0.88, 0.90, and 0.81, respectively. Our study provided evidence that fibulin-3 could be a potential biomarker for the early screening of MPM, but not of other nonmalignant ARDs in Chinese populations.
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Godyna, S., M. Diaz-Ricart, and WS Argraves. "Fibulin-1 mediates platelet adhesion via a bridge of fibrinogen." Blood 88, no. 7 (October 1, 1996): 2569–77. http://dx.doi.org/10.1182/blood.v88.7.2569.bloodjournal8872569.

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Fibulin-1 is a component of the extracellular matrix that surrounds vascular smooth muscle. This observation, along with the recent finding that fibulin-1 can bind fibrinogen (J Biol Chem 270:19458, 1995), prompted investigation into the potential role of fibulin-1 as a thrombogenic agent. In perfusion chamber assays, platelets in whole blood under flow conditions attached and spread on surfaces coated with fibulin-1. This adhesion was completely blocked by fibulin-1 antibodies. Platelets free of plasma did not attach to fibulin-1 coated surfaces; however, with the addition of fibrinogen, platelet adhesion to fibulin-1 took place. When detergent extracts of platelets were subjected to fibulin-1-Sepharose affinity chromatography, the integrin alpha IIb beta 3 was selected. Solid phase binding assays using purified components showed that integrin alpha IIb beta 3 could not bind directly to fibulin-1 but in the presence of fibrinogen the integrin bound to fibulin-1-coated surfaces. Monoclonal alpha IIb beta 3 antibodies capable of blocking its interaction with fibrinogen completely blocked platelet adhesion to fibulin-1 in both whole blood perfusion and static adhesion assays. The results show that fibulin-1 can support platelet attachment via a bridge of fibrinogen to the platelet integrin alpha IIb beta 3. When fibroblast monolayers containing extracellular matrix-incorporated fibulin-1 were used as adhesion substrates, platelet adhesion in the presence of fibrinogen could be inhibited by 30% using antibodies to fibulin-1. Following vascular injury, fibulin-1 present in the extracellular matrix of the vessel wall may therefore interact with plasma fibrinogen and promote platelet adhesion, leading to the formation of a platelet plug. Thus, fibulin-1 joins the list of matrix proteins including collagens I and IV and fibronectin that mediate platelet adhesion via a plasma protein bridge. This bridging phenomenon may represent a general mechanism by which platelets interact with exposed subendothelial matrices following vascular injury.
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Livingstone, Imogen, Vladimir N. Uversky, Dominic Furniss, and Akira Wiberg. "The Pathophysiological Significance of Fibulin-3." Biomolecules 10, no. 9 (September 8, 2020): 1294. http://dx.doi.org/10.3390/biom10091294.

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Fibulin-3 (also known as EGF-containing fibulin extracellular matrix protein 1 (EFEMP1)) is a secreted extracellular matrix glycoprotein, encoded by the EFEMP1 gene that belongs to the eight-membered fibulin protein family. It has emerged as a functionally unique member of this family, with a diverse array of pathophysiological associations predominantly centered on its role as a modulator of extracellular matrix (ECM) biology. Fibulin-3 is widely expressed in the human body, especially in elastic-fibre-rich tissues and ocular structures, and interacts with enzymatic ECM regulators, including tissue inhibitor of metalloproteinase-3 (TIMP-3). A point mutation in EFEMP1 causes an inherited early-onset form of macular degeneration called Malattia Leventinese/Doyne honeycomb retinal dystrophy (ML/DHRD). EFEMP1 genetic variants have also been associated in genome-wide association studies with numerous complex inherited phenotypes, both physiological (namely, developmental anthropometric traits) and pathological (many of which involve abnormalities of connective tissue function). Furthermore, EFEMP1 expression changes are implicated in the progression of numerous types of cancer, an area in which fibulin-3 has putative significance as a therapeutic target. Here we discuss the potential mechanistic roles of fibulin-3 in these pathologies and highlight how it may contribute to the development, structural integrity, and emergent functionality of the ECM and connective tissues across a range of anatomical locations. Its myriad of aetiological roles positions fibulin-3 as a molecule of interest across numerous research fields and may inform our future understanding and therapeutic approach to many human diseases in clinical settings.
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Mabotuwana, N., L. Murtha, S. Hardy, and A. Boyle. "Fibulin-3 in Cardiac Fibrosis." Heart, Lung and Circulation 26 (2017): S133. http://dx.doi.org/10.1016/j.hlc.2017.06.207.

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Kovac, Viljem, Metoda Dodic-Fikfak, Niko Arneric, Vita Dolzan, and Alenka Franko. "Fibulin-3 as a biomarker of response to treatment in malignant mesothelioma." Radiology and Oncology 49, no. 3 (September 1, 2015): 279–85. http://dx.doi.org/10.1515/raon-2015-0019.

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AbstractBackground.Fibulin-3 is a new potential biomarker for malignant mesothelioma (MM). This study evaluated the potential applicability of fibulin-3 plasma levels as a biomarker of response to treatment and its prognostic value for progressive disease within 18 months. The potential applicability of fibulin-3 in comparison with or in addition to soluble mesothelin-related peptides (SMRP) was also assessed.Patients and methods.The study included 78 MM patients treated at the Institute of Oncology Ljubljana between 2007 and 2011. Fibulin-3 levels in plasma samples obtained before treatment and in various responses to treatment were measured with the enzyme-linked immunosorbent assay.Results.In patients evaluated before the treatment, fibulin-3 levels were not influenced by histopathological sub-types, tumour stages or the presence of metastatic disease. Significantly higher fibulin-3 levels were found in progressive disease as compared to the levels before treatment (Mann-Whitney [U] test = 472.50, p = 0.003), in complete response to treatment (U = 42.00, p = 0.010), and in stable disease (U = 542.00, p = 0.001). Patients with fibulin-3 levels exceeding 34.25 ng/ml before treatment had more than four times higher probability for developing progressive disease within 18 months (odds ratio [OR] = 4.35, 95% confidence interval [CI] 1.56–12.13). Additionally, patients with fibulin-3 levels above 34.25 ng/ml after treatment with complete response or stable disease had increased odds for progressive disease within 18 months (OR = 6.94, 95% CI 0.99–48.55 and OR = 4.39, 95% CI 1.63–11.81, respectively).Conclusions.Our findings suggest that in addition to SMRP fibulin-3 could also be helpful in detecting the progression of MM.
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Luong, Trang T. D., Nadeshda Schelski, Beate Boehme, Manousos Makridakis, Antonia Vlahou, Florian Lang, Burkert Pieske, Ioana Alesutan, and Jakob Voelkl. "Fibulin-3 Attenuates Phosphate-Induced Vascular Smooth Muscle Cell Calcification by Inhibition of Oxidative Stress." Cellular Physiology and Biochemistry 46, no. 4 (2018): 1305–16. http://dx.doi.org/10.1159/000489144.

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Background/Aims: Fibulin-3, an extracellular matrix glycoprotein, inhibits vascular oxidative stress and remodeling in hypertension. Oxidative stress is prevalent in chronic kidney disease (CKD) patients and is an important mediator of osteo-/chondrogenic transdifferentiation and calcification of vascular smooth muscle cells (VSMCs) during hyperphosphatemia. Therefore, the present study explored the effects of Fibulin-3 on phosphate-induced vascular calcification. Methods: Experiments were performed in primary human aortic smooth muscle cells (HAoSMCs) treated with control or with phosphate without or with additional treatment with recombinant human Fibulin-3 protein or with hydrogen peroxide as an exogenous source of oxidative stress. Results: Treatment with calcification medium significantly increased calcium deposition in HAoSMCs, an effect significantly blunted by additional treatment with Fibulin-3. Moreover, phosphate-induced alkaline phosphatase activity and mRNA expression of osteogenic and chondrogenic markers MSX2, CBFA1, SOX9 and ALPL were all significantly reduced by addition of Fibulin-3. These effects were paralleled by similar regulation of oxidative stress in HAoSMCs. Phosphate treatment significantly up-regulated mRNA expression of the oxidative stress markers NOX4 and CYBA, down-regulated total antioxidant capacity and increased the expression of downstream effectors of oxidative stress PAI-1, MMP2 and MMP9 as well as BAX/BLC2 ratio in HAoSMCs, all effects blocked by additional treatment with Fibulin-3. Furthermore, the protective effects of Fibulin-3 on phosphate-induced osteogenic and chondrogenic markers expression in HAoSMCs were reversed by additional treatment with hydrogen peroxide. Conclusions: Fibulin-3 attenuates phosphate-induced osteo-/ chondrogenic transdifferentiation and calcification of VSMCs, effects involving inhibition of oxidative stress. Up-regulation or supplementation of Fibulin-3 may be beneficial in reducing the progression of vascular calcification during hyperphosphatemic conditions such as CKD.
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Tian, Meiling, Jing Wang, Yuqin Wei, Qingle Lu, and Baohua Huang. "Serum and vitreous fibulin-1 concentrations in patients with diabetic retinopathy." Journal of Investigative Medicine 64, no. 7 (July 15, 2016): 1209–12. http://dx.doi.org/10.1136/jim-2016-000130.

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Fibulin-1, an extracellular matrix glycoprotein, is closely correlated with angiogenesis. The purpose of this investigation is to determine serum and vitreous fibulin-1 concentrations in diabetic retinopathy (DR). This cross-sectional investigation was carried out in a population of 154 diabetic patients (54 without DR, 42 with non-proliferative diabetic retinopathy (NPDR) and 58 with proliferative diabetic retinopathy (PDR)) and 49 control subjects. The diabetic group showed higher serum and vitreous fibulin-1 concentrations than the controls. Serum and vitreous fibulin-1 concentrations in PDR patients were significantly elevated compared with those in the other 3 groups. NPDR patients showed elevated levels of serum and vitreous fibulin-1 concentrations compared with patients without DR. Logistic regression analysis revealed that serum and vitreous fibulin-1 were risk factors for developing DR. Pearson correlation analysis showed that serum fibulin-1 was correlated with systolic blood pressure (SBP), diastolic blood pressure (DBP), fasting plasma glucose and vitreous fibulin-1. Furthermore, Pearson correlation analysis showed that vitreous fibulin-1 was correlated with SBP, DBP, high-density lipoprotein cholesterol and serum fibulin-1. Serum and vitreous fibulin-1 concentrations are elevated under DR condition.
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Zhang, Youwen, and Lihua Y. Marmorstein. "Focus on molecules: Fibulin-3 (EFEMP1)." Experimental Eye Research 90, no. 3 (March 2010): 374–75. http://dx.doi.org/10.1016/j.exer.2009.09.018.

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Wakabayashi, Toru, Akihiko Matsumine, Shigeto Nakazora, Masahiro Hasegawa, Takahiro Iino, Hideki Ota, Hikaru Sonoda, Akihiro Sudo, and Atsumasa Uchida. "Fibulin-3 negatively regulates chondrocyte differentiation." Biochemical and Biophysical Research Communications 391, no. 1 (January 2010): 1116–21. http://dx.doi.org/10.1016/j.bbrc.2009.12.034.

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Dissertations / Theses on the topic "Fibulin-3"

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Djokic, Jelena. "Molecular properties of fibulin-3, -4 and-5." Thesis, McGill University, 2013. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=114359.

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The fibulin family comprises eight extracellular matrix proteins associated with elastic fibers and basement membranes. Elastic fibers provide necessary tissue recoil to organs, including large arteries, lung, and skin, and elastogenesis requires the coordinated effort of many proteins. Knockout mouse studies have implicated fibulin-3, -4, and -5 (collectively referred to as the short fibulins), in elastic fiber assembly, stabilization, and function.Recombinant human full-length short fibulins were expressed in human embryonic kidney cells, and purified by immobilized metal ion affinity chromatography. All three members consistently appear as multiple bands on protein gels. N-terminal protein sequencing revealed that all three proteins are readily cleaved within the atypical N-terminal linker region of the first calcium-binding epidermal growth factor domain. This multiple band pattern is also in part caused by the N-glycosylation and multimerization of the short fibulins. A similar band pattern was produced by incubation of the short fibulins with select matrix metalloproteinases. Fibulin-3 proteolysis was almost completely inhibited in cell culture with doxycycline (a broad-spectrum matrix metalloproteinase inhibitor) supplementation.Human skin fibroblasts adhered strongly to the short fibulins, as measured by crystal violet attachment assays. Human lung fibroblasts and human umbilical vein and artery smooth muscle cells adhered slightly less. Calcium-dependent binding of the short fibulins to immobilized heparin in solid phase binding assays suggests that these fibulins may bind cell-surface heparan sulfate.
La famille de protéines fibuline est composée de huit membres, se situant dans la matrice extracellulaire, associée aux fibres élastiques et aux membranes basales. Les fibres élastiques confèrent l'élasticité requise aux organes, tels que les artères majeures, les poumons et la peau. La formation des fibres élastiques requiert la coordination de nombreuses protéines. Les souris knockout ont impliqué les fibulines courtes (fibuline-3, -4, et -5) dans la formation, la stabilisation, et le fonctionnement des fibres élastiques.Les fibulines courtes recombinantes ont été exprimées par les cellules HEK293 et purifiées par chromatographie d'affinité métallique. Les trois protéines migrent en plusieurs bandes sur les gels de SDS-PAGE. Le séquençage de l'extrémité N-terminale de ces bandes a démontré que les trois protéines sont coupées dans le linker du premier domaine de facteur de croissance épidermique lié au calcium. Cet effet de plusieurs bandes est en partie causé pas la N-glycosylation et la multimérisation des fibulines courtes. Un effet similaire se produit après l'incubation des fibulines courtes avec certaines métalloprotéinases matricielles. La protéolyse de fibuline-3 est presque complètement inhibée par l'addition de doxycycline (un inhibiteur de tous les métalloprotéinases matricielles) aux cellules HEK293.Les fibroblastes dermiques humains adhèrent fortement aux fibulines courtes, ce qui a été mesuré avec la coloration des cellules au cristal violet. Les fibroblastes pulmonaires humains et les cellules musculaires lisses de veine ombilicale et d'artère ombilicale adhèrent un peu moins fort. Les fibulines courtes interagissent aussi avec l'héparine immobilisée, en la présence de calcium. Ceci suggère que les fibulines courtes peuvent adhérer au sulfate d'héparane à la surface des cellules.
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Zayas-Santiago, Astrid, Samuel D. Cross, James B. Stanton, Alan D. Marmorstein, and Lihua Y. Marmorstein. "Mutant Fibulin-3 Causes Proteoglycan Accumulation and Impaired Diffusion Across Bruch's Membrane." ASSOC RESEARCH VISION OPHTHALMOLOGY INC, 2017. http://hdl.handle.net/10150/624956.

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PURPOSE. The mutation R345W in EFEMP1 (fibulin-3) causes macular degeneration. This study sought to determine whether proteoglycan content and diffusion across Bruch's membrane are altered in Efemp1(ki/ki) mice carrying this mutation or in Efemp1(-/-) mice. METHODS. Proteoglycans in mouse Bruch's membranes were stained with Cupromeronic Blue (CB). Heparan sulfated proteoglycan (HSPG) and chondroitin/dermatan sulfate proteoglycan (C/DSPG) distributions were visualized following treatments with chondroitinase ABC (C-ABC) or nitrous acid. Total sulfated glycosaminoglycans (sGAGs) in Bruch's membrane/choroid (BrM/Ch) were measured with dimethylmethylene blue (DMMB). Matrix metalloprotease (MMP)-2, MMP-9, and tissue inhibitor of metalloproteinase (TIMP)-3 were examined by immunofluorescence and quantified using Image J. Molecules with different Stokes radius (R-s) were allowed simultaneously to diffuse through mouse BrM/Ch mounted in a modified Ussing chamber. Samples were quantified using gel exclusion chromatography. RESULTS. HSPGs and C/DSPGs were markedly increased in Efemp1(ki/ki) Bruch's membrane, and MMP-2 and MMP-9 were decreased, but TIMP-3 was increased. Diffusion across Efemp1(ki/ki) Bruch's membrane was impaired. In contrast, the proteoglycan amount in Efemp1(-/-) Bruch's membrane was not significantly different, but the size of proteoglycans was much larger. MMP-2, MMP-3, and TIMP-3 levels were similar to that of Efemp1(+/+) mice, but they were localized diffusely in retinal pigment epithelium (RPE) cells instead of Bruch's membrane. Diffusion across Efemp1(-/-) Bruch's membrane was enhanced. CONCLUSIONS. Mutant fibulin-3 causes proteoglycan accumulation, reduction of MMP-2 and MMP-9, but increase of TIMP-3, and impairs diffusion across Bruch's membrane. Fibulin-3 ablation results in altered sizes of proteoglycans, altered distributions of MMP-2, MMP-9, and TIMP-3, and enhances diffusion across Bruch's membrane.
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Papon, Marie-Amélie. "Régulation des sous-types d’hétérodimères du récepteur GABAB dans la moelle épinière en conditions de douleurs neuropathiques : rôle des protéines partenaires." Thesis, Bordeaux 2, 2009. http://www.theses.fr/2009BOR21671/document.

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Dans le système nerveux central, le récepteur inhibiteur GABAB est un archétype des RCPGs hétérodimériques. Il est composé en effet de deux sous-unités, la sous-unité GABAB1 (B1a ou B1b) qui lie l’agoniste et la sous-unité GABAB2 couplée aux protéines G. L’activation de ce récepteur a un effet antinociceptif bien établi concernant les douleurs aiguës mais son effet reste cependant très limité en cas de douleurs neuropathiques. Notre hypothèse est que son activation et sa signalisation peuvent être altérées par des protéines partenaires, aboutissant à des processus de désinhibition dans la moelle épinière en conditions de neuropathie. Nos résultats mettent en évidence le rôle de deux protéines partenaires qui sont surexprimées en conditions douloureuses et qui diminuent l’activation du récepteur GABAB via deux mécanismes différents. D’un part, la protéine cytosolique 14-3-3? induit la dissociation de l’hétérodimère B1b/B2. Cette action a lieu principalement dans les compartiments post-synaptiques. D’autre part, la fibuline-2, protéine de la matrice extracellulaire diminue l’activation de l’hétérodimère B1a/B2. Il s’agit cette fois préférentiellement d’une action dans les compartiments pré-synaptiques. Des stratégies anti-sens (siRNA anti-14-3-3? ou anti-fibuline-2) ou des peptides de compétition sélectifs de l’interaction B1b/14-3-3? permettent de potentialiser les effets antinociceptifs d’un agoniste du récepteur sur un modèle animal de neuropathie. L’ensemble de ces résultats suggèrent que l’état d’oligomérisation des RCPGs peut être modulé in vivo par des protéines partenaires endogènes impliquées dans le développement ou le maintien d’états pathologiques de sensibilisation à la douleur
In the central nervous system, the inhibitory GABAB receptor is an obligate heterodimeric GPCR that requires the association between GABAB1 (B1a or B1b) and GABAB2 subunits. The heterodimeric GABAB receptor activation has a well-known antinociceptive action in acute pain but its effect appears limited in pathological states. Our hypothesis is that the GABAB activation and signaling could be altered by partner proteins, thus resulting in desinhibition processes in the spinal cord. In the present study, we investigated the role of two partner proteins overexpressed in neuropathic states which decrease GABAB activation through two different mechanisms. On the one hand, the cytosolic 14-3-3? protein induces the dissociation of the heterodimer B1b/B2. This effect occurs in post-synaptic compartments. On the other hand, fibulin-2, an extracellular matrix protein, which decreases the activation of the heterodimer B1a/B2 localized preferentially in presynaptic compartments. Anti-sens strategies (anti-14-3-3? or anti-fibulin-2 siRNA) or competing peptides specific of 14-3-3?/B1b interaction, potentiate the antinociceptive effects of GABAB agonist in an animal model of neuropathic pain. Taken together, our data suggest that GPCR oligomeric state can be modulated in vivo by endogenous partners proteins that are involved in the development and the maintenance of pain sensitization
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Vukovic, Jana. "An in vitro and in vitro study on the role of the glycoprotein fibulin-3 in olfactory nerve growth and repair." University of Western Australia. School of Anatomy and Human Biology, 2008. http://theses.library.uwa.edu.au/adt-WU2008.0182.

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The primary olfactory pathway in adult mammals has retained a remarkable potential for self-repair. Olfactory ensheathing cells (OECs), specialized glial cells within the olfactory nerve, are thought to play an important role in the ongoing growth and replenishment of sensory connections in this system. To gain insight into novel molecules that could mediate OEC-supported growth of axons within the olfactory nerve, gene expression profiling experiments revealed very high expression of the fibulin-3 glycoprotein in OECs. To date, research on fibulin-3 has been limited and mainly focused on its involvement in Doyne honeycomb retinal dystrophy, vasculogenesis and tumor formation. As the extracellular matrix associated with OECs is thought to be an important contributor to a growth-permissive environment, the main aim of this thesis was to define a putative role for fibulin-3 during olfactory receptor neuron replacement and regeneration. This hypothesis was investigated in a series of in vitro and in vivo experiments that involved lentiviral vectors to manipulate fibulin-3 gene expression in OECs as well as the use of knock-out mice. Using genetically-modified OECs, experimental data showed that increased levels of fibulin-3 induced morphological changes in OECs and also impeded their migration. Lentiviral vector-mediated expression of fibulin-3 in OECs also had an inhibitory effect on neurite outgrowth from dorsal root ganglion explants. On the other hand, knock-down of fibulin-3 levels via siRNA technology resulted in reduced proliferation. Comparative lesioning experiments in fibulin-3 knock-out and wild-type mice allowed for further assessment of a role for fibulin-3 in olfactory nerve repair in vivo. Two experimental injury models, i.e. epithelial (Triton-X) lesioning and olfactory bulbectomy, were employed. The results obtained were in line with in vitro observations. A lack of fibulin-3 in knock-out mice resulted in a seemingly augmented regeneration of the olfactory epithelium at 10 days post-injury. However, at the latest recovery time point of 42 days post-injury, an impaired recovery of the olfactory epithelium from the experimental insults was observed. Although the precise mechanism for the latter phenomenon is not yet fully understood, our data point towards several factors which include vascular abnormalities and altered cell proliferation within the olfactory epithelium. Additionally, the precise protein distribution of another wide-spread family of extracellular matrix molecules, the laminins, was investigated in this thesis. It was of interest to investigate the spatiotemporal expression of laminin isoforms during iii olfactory nerve development and regeneration as these molecules may have distinct roles in promoting olfactory sensory neuron growth and patterning. In situ hybridization and immunohistochemical studies concluded that laminin-211 and laminin-411 were the most likely candidates to play such a role. In summary, this thesis provides new insights into the role of the extracellular matrix, fibulin-3 in particular, in regulating cell migration, division and axonal growth in the primary olfactory pathway. Such knowledge also gives a greater understanding of the molecular mechanisms by which OEC transplants may enhance axonal regeneration elsewhere in the CNS.
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Schubert, Andrea [Verfasser], Nicolai [Akademischer Betreuer] Miosge, Anette [Akademischer Betreuer] Wiegand, and Martin [Akademischer Betreuer] Oppermann. "Vergleichende histologische Untersuchungen oraler Gewebe der Wildtyp- und der DDR1-Knockout-Maus hinsichtlich ihrer Struktur und der Expression von Fibulin-3, -4 und -5 / Andrea Schubert. Gutachter: Anette Wiegand ; Martin Oppermann. Betreuer: Nicolai Miosge." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2014. http://d-nb.info/1064404022/34.

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Schubert, Andrea. "Vergleichende histologische Untersuchungen oraler Gewebe der Wildtyp- und der DDR1-Knockout-Maus hinsichtlich ihrer Struktur und der Expression von Fibulin-3, -4 und -5." Doctoral thesis, 2014. http://hdl.handle.net/11858/00-1735-0000-0023-9952-4.

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Book chapters on the topic "Fibulin-3"

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Topalovski, Mary, and Rolf A. Brekken. "The Extracellular Matrix of Tumors: A Focus on Fibronectin and Fibulin-5." In Extracellular Matrix in Tumor Biology, 1–15. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-60907-2_1.

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Amano, Satoshi. "Fibulin-5 Deposition in Human Skin: Decrease with Aging and UVB Exposure and Increase in Solar Elastosis." In Textbook of Aging Skin, 641–49. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-47398-6_32.

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Amano, Satoshi. "Fibulin-5 Deposition in Human Skin: Decrease with Aging and UVB Exposure and Increase in Solar Elastosis." In Textbook of Aging Skin, 333–39. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-540-89656-2_32.

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Amano, Satoshi. "Fibulin-5 Deposition in Human Skin: Decrease with Aging and UVB Exposure and Increase in Solar Elastosis." In Textbook of Aging Skin, 1–9. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-642-27814-3_32-2.

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Jeronimo Rafael, Rodríguez-Cid, and Flores-Mariñelarena Rodrigo Rafael. "Predictive and Prognosis Factors of Clinical Utility in Mesothelioma." In Mesothelioma. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.91769.

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The constant research in therapeutics for mesothelioma has been improving their tumor response and overall survival, generating the need to propose markers that guide the doctor’s therapeutic approach in a more precise way. Recently, different predictive factors have been proposed, such as mesothelin-related peptides, fibulin-3, and osteopontin associated with an image giving information about the probability of tumor response to a therapeutic agent or a combination of agents. As is well known, the importance of prognostic markers of utility lies in providing prospective information on the evolution of the patient and thus their ability to guide therapeutic decisions. Although the clinical stage and histology are currently the most described prognostic factors, recent studies have shown interest in the expression of estrogen receptor beta and calretinin, among other promising factors. Given the heterogeneity of this broad field of research in mesothelioma, it is necessary to objectively present the prognostic and predictive factors of greater clinical utility.
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Conference papers on the topic "Fibulin-3"

1

Pinelli, Valentina, Donatella Fini, Enrico Battolla, Paola Ferro, Maria Cristiana Franceschini, Vincenzo Fontana, Maria Pia Pistillo, Silvio Roncella, and Pier Aldo Canessa. "Comparison between mesothelin and fibulin-3 detection in pleural malignant mesothelioma (MPM) patients." In ERS International Congress 2016 abstracts. European Respiratory Society, 2016. http://dx.doi.org/10.1183/13993003.congress-2016.pa5075.

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2

Espinosa, Gabriela, Lisa Bennett, William Gardner, and Jessica Wagenseil. "The Effects of Extracellular Matrix Protein Insufficiency and Treatment on the Stiffness of Arterial Smooth Muscle Cells." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14131.

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Increased arterial stiffness is directly correlated with hypertension and cardiovascular disease. Stiffness of the conducting arteries is largely determined by the extracellular matrix (ECM) proteins in the wall, such as collagen and elastin, produced by the smooth muscle cells (SMCs) found in the medial layer. Elastin is deposited as soluble tropoelastin and is later crosslinked into elastin fibers. Newborn mice lacking the elastin protein ( Eln−/−) have increased arterial wall stiffness and SMCs with altered proliferation, migration and morphology [1]. Vessel elasticity is also mediated by other ECM proteins, such as fibulin-4. Elastic tissue, such as lung, skin, and arteries, from fibulin-4 deficient ( Fbln4−/−) mice show no decrease in elastin content, but have reduced elasticity due to disrupted elastin fibers [2]. Arteries from both elastin and fibulin-4 deficient mice have been previously studied, but the mechanical properties of their SMCs have not been investigated. Recent experiments comparing arterial SMCs from old and young animals suggest that mechanical properties of the SMCs themselves may contribute to changes in wall stiffness [3]. Hence, we investigated the stiffness of isolated arterial SMCs from elastin and fibulin-4 deficient mice using atomic force microscopy (AFM). In addition, we studied the effects of two elastin treatments on the mechanical properties of SMCs from Eln+/+ and Eln−/− mice. Differences between the treatments may elucidate the importance of soluble versus crosslinked elastin on single cell stiffness.
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3

Nandhu, Mohan Sobhana, Prajna Behera, Vivek Bhaskaran, Ennio Antonio Chiocca, and Mariano S. Viapiano. "Abstract 3797: Validation of a novel antibody against fibulin-3 for targeted therapy of glioblastoma." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3797.

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4

Koba, T., Y. Takeda, R. Narumi, M. Ito, H. Yoshimura, Y. Nojima, J. Adachi, and A. Kumanogoh. "Proteomics of Serum Extracellular Vesicles Identifies a Novel COPD Biomarker, Fibulin-3 from Elastic Fibres." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a4346.

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Nandhu, Mohan Sobhana, Chandra Goparaju, Sharon L. Longo, Harvey I. Pass, and Mariano S. Viapiano. "Abstract 2769: Targeting malignant mesothelioma with an antibody against the tumor extracellular matrix protein fibulin-3." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-2769.

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6

Longo, Sharon L., Prajna Behera, Mariano S. Viapiano, and Mohan Sobhana Nandhu. "Abstract 1706: Inhibition of fibulin-3 reverses macrophage polarization in glioblastoma and increases anti-tumor inflammatory responses." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-1706.

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7

Roshini, Arivazhagan, Chandra Goparaju, Mohan S. Nandhu, Sharon L. Longo, John A. Longo, Joan Chou, Frank A. Middleton, Harvey I. Pass, and Mariano S. Viapiano. "Abstract 3954: Validation of the extracellular matrix protein fibulin-3 as a molecular target in malignant pleural mesothelioma." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-3954.

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8

Wan, William, and Rudolph L. Gleason. "Collagen Fiber Angle Quantification of Carotid Arteries From Fibulin-5 Null Mice." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53685.

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Recent studies have revealed that carotid arteries from fibulin-5 (fbln5) null mice exhibit altered biomechanical and microstructural properties [1–2]. While the previous studies outline quantitative differences in mechanical properties of arteries from fbln5 null and wildtype mice, physical microstructural differences have yet to be quantified. Measurement of microstructural parameters will provide a crucial link between previously quantified mechanical properties and biological effects of knocking out the fbln5 gene. Characterizing microstructural properties will also provide experimental data to validate structurally-motivated constitutive relations and growth and remodeling models [3–4]. In this study, we quantified collagen fiber orientation in carotid arteries from fbln5 null and wildtype mice; collagen in mouse carotid arteries were imaged using multiphoton microscopy and analyzed using a fast Fourier transform algorithm.
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Pesatori, AC, L. Angelici, C. Favero, L. Dioni, C. Mensi, C. Bareggi, A. Palleschi, et al. "1769d Combination of mirnas, mesothelin and fibulin-3 as potential biomarkers in malignant pleural mesothelioma and asbestos-exposed subjects." In 32nd Triennial Congress of the International Commission on Occupational Health (ICOH), Dublin, Ireland, 29th April to 4th May 2018. BMJ Publishing Group Ltd, 2018. http://dx.doi.org/10.1136/oemed-2018-icohabstracts.438.

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Hu, Bin, Paula A. Agudelo, Joshua C. Saldivar, Hosung Sim, Claire E. Dolan, Maria E. Mora, Gerard J. Nuovo, Susan E. Cole, and Mariano S. Viapiano. "Abstract 2353: Fibulin-3, an extracellular matrix protein, regulates Notch signaling and promotes brain tumor cell invasion and survival." In Proceedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL. American Association for Cancer Research, 2011. http://dx.doi.org/10.1158/1538-7445.am2011-2353.

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