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Journal articles on the topic 'Fibulin-3'

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Published: 4 June 2021

Last updated: 1 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Klingen, Tor A., Ying Chen, Hans Aas, Elisabeth Wik, and Lars A. Akslen. "Fibulin-2 expression associates with vascular invasion and patient survival in breast cancer." PLOS ONE 16, no. 4 (April 9, 2021): e0249767. http://dx.doi.org/10.1371/journal.pone.0249767.

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Stromal elastosis is related to good prognosis in breast cancer and fibulin-2 helps to stabilize elastic fibers in basement membranes. Here, we examined the level of perivascular fibulin-2 expression in relation to elastosis content, vascular invasion, molecular subtypes, tumour detection mode, and patient prognosis in breast cancer. We performed a population based retrospective study of invasive breast cancers from the Norwegian Breast Screening Program (Vestfold County, 2004–2009) including 200 screen-detected and 82 interval cancers. Perivascular fibulin-2 staining was semi-quantitatively graded based on immunohistochemistry (1–3) and dichotomized as high expression (grade 2–3) and low expression (grade 1). Elastosis content was graded on a 4-tiered scale and dichotomized as high (score 3) and low (score 0–2) expression, whereas lymphatic (LVI) and blood vessel invasion (BVI) were recorded as absent or present by immunohistochemistry. High perivascular fibulin-2 expression was strongly related to stromal elastosis (p<0.001), and inversely associated with BVI and LVI (p<0.001 for both). High fibulin-2 was associated with luminal breast cancer subgroups (p<0.001) and inversely with interval cancers compared with screen-detected tumours (p<0.001). By univariate analysis, low perivascular fibulin-2 was associated with reduced recurrence-free survival (p = 0.002) and disease specific survival (p = 0.019). Low perivascular fibulin-2 expression was strongly related to vascular invasion, low stromal elastosis, non-luminal breast cancer subtypes, interval presentation, and adverse prognosis.

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12

Gillezeau, Christina N., Maaike van Gerwen, Julio Ramos, Bian Liu, Raja Flores, and Emanuela Taioli. "Biomarkers for malignant pleural mesothelioma: a meta-analysis." Carcinogenesis 40, no. 11 (June 5, 2019): 1320–31. http://dx.doi.org/10.1093/carcin/bgz103.

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Abstract Malignant pleural mesothelioma (MPM) is a rare but aggressive cancer, and early detection is associated with better survival. Mesothelin, fibulin-3 and osteopontin have been suggested as screening biomarkers. The study conducted a meta-analysis of the mean differences of mesothelin, osteopontin and fibulin-3 in blood and pleural samples. PubMed searches were conducted for studies that measured levels of mesothelin, osteopontin and fibulin-3 in participants with MPM compared with malignancy, benign lung disease or healthy participants. Thirty-two studies with mesothelin levels, 12 studies with osteopontin levels and 9 studies with fibulin-3 levels were included in the meta-analysis. Statistically significant mean differences were seen between MPM patients and all other comparison groups for mesothelin blood and pleural levels. Statistically significant differences in blood osteopontin levels were seen between participants with benign lung disease and healthy participants compared with participants with MPM, but not when comparing participants with cancer with MPM participants. There were not enough studies that reported osteopontin levels in pleural fluid to complete a meta-analysis. Statistically significant differences were seen in both blood and pleural levels of fibulin-3 in MPM patients compared with all other groups. On the basis of these results, mesothelin and fibulin-3 levels appear to be significantly lower in all control groups compared with those with MPM, making them good candidates for screening biomarkers. Osteopontin may be a useful biomarker for screening healthy individuals or those with benign lung disease but would not be useful for screening patients with malignancies.

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13

Argraves, W. S., H. Tran, W. H. Burgess, and K. Dickerson. "Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure." Journal of Cell Biology 111, no. 6 (December 1, 1990): 3155–64. http://dx.doi.org/10.1083/jcb.111.6.3155.

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We have studied the expression of fibulin in cultured fibroblasts and determined its primary structure by cDNA cloning. Our results show that fibulin is a secreted glycoprotein that becomes incorporated into a fibrillar extracellular matrix when expressed by cultured cells or added exogenously to cell monolayers. In addition, we find that fibulin is present in plasma at a level of 33 +/- 3 micrograms/ml. Sequencing of multiple fibulin cDNAs indicates that a process of alternative splicing results in the expression of three fibulin transcripts. The transcripts encode overlapping polypeptides differing only in carboxy-terminal segments. Common to the three predicted forms of fibulin is a unique 537-amino acid-long cysteine-rich polypeptide and a 29-residue signal peptide. The amino-terminal portion of fibulin contains a repeated element with potential disulfide loop structure resembling that of the complement component anaphylatoxins C3a, C4a, and C5a as well as proteins of the albumin gene family. The bulk of the remaining portion of the molecule is a series of nine EGF-like repeats.

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14

Ledda, Caterina, Rosario Caltabiano, Francesca Vella, Serena Matera, Andrea Marconi, Carla Loreto, and Venerando Rapisarda. "Fibulin-3 as biomarker of malignant mesothelioma." Biomarkers in Medicine 13, no. 10 (July 2019): 875–86. http://dx.doi.org/10.2217/bmm-2018-0285.

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15

Burki, Talha Khan. "Fibulin-3 as a biomarker for mesothelioma." Lancet Oncology 13, no. 11 (November 2012): e469. http://dx.doi.org/10.1016/s1470-2045(12)70468-0.

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16

Han, A. L., B. A. Veeneman, L. El-Sawy, K. C. Day, M. L. Day, S. A. Tomlins, and E. T. Keller. "Fibulin-3 promotes muscle-invasive bladder cancer." Oncogene 36, no. 37 (May 15, 2017): 5243–51. http://dx.doi.org/10.1038/onc.2017.149.

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17

Koba, Taro, Yoshito Takeda, Ryohei Narumi, Takashi Shiromizu, Yosui Nojima, Mari Ito, Muneyoshi Kuroyama, et al. "Proteomics of serum extracellular vesicles identifies a novel COPD biomarker, fibulin-3 from elastic fibres." ERJ Open Research 7, no. 1 (January 2021): 00658–2020. http://dx.doi.org/10.1183/23120541.00658-2020.

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There is an unmet need for novel biomarkers in the diagnosis of multifactorial COPD. We applied next-generation proteomics to serum extracellular vesicles (EVs) to discover novel COPD biomarkers.EVs from 10 patients with COPD and six healthy controls were analysed by tandem mass tag-based non-targeted proteomics, and those from elastase-treated mouse models of emphysema were also analysed by non-targeted proteomics. For validation, EVs from 23 patients with COPD and 20 healthy controls were validated by targeted proteomics.Using non-targeted proteomics, we identified 406 proteins, 34 of which were significantly upregulated in patients with COPD. Of note, the EV protein signature from patients with COPD reflected inflammation and remodelling. We also identified 63 upregulated candidates from 1956 proteins by analysing EVs isolated from mouse models. Combining human and mouse biomarker candidates, we validated 45 proteins by targeted proteomics, selected reaction monitoring. Notably, levels of fibulin-3, tripeptidyl-peptidase 2, fibulin-1, and soluble scavenger receptor cysteine-rich domain-containing protein were significantly higher in patients with COPD. Moreover, six proteins; fibulin-3, tripeptidyl-peptidase 2, UTP-glucose-1-phosphate uridylyl transferase, CD81, CD177, and oncoprotein-induced transcript 3, were correlated with emphysema. Upregulation of fibulin-3 was confirmed by immunoblotting of EVs and immunohistochemistry in lungs. Strikingly, fibulin-3 knockout mice spontaneously developed emphysema with age, as evidenced by alveolar enlargement and elastin destruction.We discovered potential pathogenic biomarkers for COPD using next-generation proteomics of EVs. This is a novel strategy for biomarker discovery and precision medicine.

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18

Hasegawa, A., T. Yonezawa, N. Taniguchi, K. Otabe, Y. Akasaki, T. Matsukawa, M. Saito, M. Neo, L. Marmorstein, and M. Lotz. "Fibulin-3 in joint aging and osteoarthritis pathogenesis." Osteoarthritis and Cartilage 22 (April 2014): S8. http://dx.doi.org/10.1016/j.joca.2014.02.036.

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19

Giltay, Richard, Rupert Timpl, and Günter Kostka. "Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4." Matrix Biology 18, no. 5 (October 1999): 469–80. http://dx.doi.org/10.1016/s0945-053x(99)00038-4.

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20

Hulleman, John D., Joseph C. Genereux, and Annie Nguyen. "Mapping wild-type and R345W fibulin-3 intracellular interactomes." Experimental Eye Research 153 (December 2016): 165–69. http://dx.doi.org/10.1016/j.exer.2016.10.017.

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21

Luo, Rongzhen, Meifang Zhang, Lili Liu, Shixun Lu, Chris Zhiyi Zhang, and Jingping Yun. "Decrease of Fibulin-3 in Hepatocellular Carcinoma Indicates Poor Prognosis." PLoS ONE 8, no. 8 (August 1, 2013): e70511. http://dx.doi.org/10.1371/journal.pone.0070511.

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22

Murtha, Lucy A., Nishani R. Mabotuwana, Sean A. Hardy, and Andrew J. Boyle. "Fibulin-3 as a Potential Therapeutic Target for Cardiac Fibrosis." Journal of Cardiac Failure 23, no. 8 (August 2017): S28. http://dx.doi.org/10.1016/j.cardfail.2017.07.071.

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23

Rapisarda, Venerando, Rosario Caltabiano, Giuseppe Musumeci, Paola Castrogiovanni, Margherita Ferrante, Caterina Ledda, Claudia Lombardo, Adriana Carol Eleonora Graziano, Venera Cardile, and Carla Loreto. "Analysis of fibulin-3 after exposure to asbestos-like fibers." Environmental Research 156 (July 2017): 381–87. http://dx.doi.org/10.1016/j.envres.2017.03.055.

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24

Agha, Mohammed A., Mahmoud M. El-Habashy, and Rania A. El-Shazly. "Role of fibulin-3 in the diagnosis of malignant mesothelioma." Egyptian Journal of Chest Diseases and Tuberculosis 63, no. 1 (January 2014): 99–105. http://dx.doi.org/10.1016/j.ejcdt.2013.10.004.

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Rahn, David D., Jesús F. Acevedo, Shayzreen Roshanravan, Patrick W. Keller, Elaine C. Davis, Lihua Y. Marmorstein, and R. Ann Word. "Failure of Pelvic Organ Support in Mice Deficient In Fibulin-3." American Journal of Pathology 174, no. 1 (January 2009): 206–15. http://dx.doi.org/10.2353/ajpath.2009.080212.

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26

McCullough, A. "Fibulin-3 as a Blood and Effusion Biomarker for Pleural Mesothelioma." Yearbook of Pathology and Laboratory Medicine 2013 (January 2013): 298–300. http://dx.doi.org/10.1016/j.ypat.2012.10.023.

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27

Creaney, Jenette, Ian M. Dick, Tarek M. Meniawy, Su Lyn Leong, Justine S. Leon, Yvonne Demelker, Amanda Segal, et al. "Comparison of fibulin-3 and mesothelin as markers in malignant mesothelioma." Thorax 69, no. 10 (July 18, 2014): 895–902. http://dx.doi.org/10.1136/thoraxjnl-2014-205205.

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28

Pass, Harvey I., Stephen M. Levin, Michael R. Harbut, Jonathan Melamed, Luis Chiriboga, Jessica Donington, Margaret Huflejt, et al. "Fibulin-3 as a Blood and Effusion Biomarker for Pleural Mesothelioma." New England Journal of Medicine 367, no. 15 (October 11, 2012): 1417–27. http://dx.doi.org/10.1056/nejmoa1115050.

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29

Kaya, Halide, Melike Demir, Mahsuk Taylan, Cengizhan Sezgi, Abdullah Cetin Tanrikulu, Sureyya Yilmaz, Mehmet Bayram, Ibrahim Kaplan, and Abdurrahman Senyigit. "Fibulin-3 as a Diagnostic Biomarker in Patients with Malignant Mesothelioma." Asian Pacific Journal of Cancer Prevention 16, no. 4 (March 9, 2015): 1403–7. http://dx.doi.org/10.7314/apjcp.2015.16.4.1403.

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30

Wang, Xin, Qing Zhang, Changji Li, Xiaoyan Qu, Peiwen Yang, Jinjing Jia, Liumei Song, Wenxin Fan, Huiling Jing, and Yan Zheng. "Fibulin-3 Has Anti-Tumorigenic Activities in Cutaneous Squamous Cell Carcinoma." Journal of Investigative Dermatology 139, no. 8 (August 2019): 1798–808. http://dx.doi.org/10.1016/j.jid.2019.01.022.

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31

Chen, Xiaojun, Jie Meng, Wen Yue, Jian Yu, Jie Yang, Zhi Yao, and Lin Zhang. "Fibulin-3 suppresses Wnt/β-catenin signaling and lung cancer invasion." Carcinogenesis 35, no. 8 (January 30, 2014): 1707–16. http://dx.doi.org/10.1093/carcin/bgu023.

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32

Gao, Lian-Bo, Shen Tian, Hong-Hua Gao, and Yan-Yuan Xu. "Metformin inhibits glioma cell U251 invasion by downregulation of fibulin-3." NeuroReport 24, no. 10 (July 2013): 504–8. http://dx.doi.org/10.1097/wnr.0b013e32836277fb.

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Murray, James. "Fibulin-3 as a blood and effusion biomarker for pleural mesothelioma." Thorax 68, no. 12 (March 7, 2013): 1180. http://dx.doi.org/10.1136/thoraxjnl-2013-203396.

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34

Engle, Dannielle D., Hervé Tiriac, Keith D. Rivera, Arnaud Pommier, Sean Whalen, Tobiloba E. Oni, Brinda Alagesan, et al. "The glycan CA19-9 promotes pancreatitis and pancreatic cancer in mice." Science 364, no. 6446 (June 20, 2019): 1156–62. http://dx.doi.org/10.1126/science.aaw3145.

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Glycosylation alterations are indicative of tissue inflammation and neoplasia, but whether these alterations contribute to disease pathogenesis is largely unknown. To study the role of glycan changes in pancreatic disease, we inducibly expressed human fucosyltransferase 3 and β1,3-galactosyltransferase 5 in mice, reconstituting the glycan sialyl-Lewisa, also known as carbohydrate antigen 19-9 (CA19-9). Notably, CA19-9 expression in mice resulted in rapid and severe pancreatitis with hyperactivation of epidermal growth factor receptor (EGFR) signaling. Mechanistically, CA19-9 modification of the matricellular protein fibulin-3 increased its interaction with EGFR, and blockade of fibulin-3, EGFR ligands, or CA19-9 prevented EGFR hyperactivation in organoids. CA19-9–mediated pancreatitis was reversible and could be suppressed with CA19-9 antibodies. CA19-9 also cooperated with the KrasG12D oncogene to produce aggressive pancreatic cancer. These findings implicate CA19-9 in the etiology of pancreatitis and pancreatic cancer and nominate CA19-9 as a therapeutic target.

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Ahn, K. H., T. Kim, J. Y. Hur, S. H. Kim, K. W. Lee, and Y. T. Kim. "Relationship between the expression of fibulin-3 and anterior vaginal wall prolapse." Journal of Obstetrics and Gynaecology 32, no. 4 (April 20, 2012): 362–66. http://dx.doi.org/10.3109/01443615.2012.658893.

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Zhang, Chiming, Chan Yu, Wenlei Li, Yaoyao Zhu, Yuling Ye, Zhuo Wang, and Zhongwei Lin. "Fibulin-3 affects vascular endothelial function and is regulated by angiotensin II." Microvascular Research 132 (November 2020): 104043. http://dx.doi.org/10.1016/j.mvr.2020.104043.

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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." Investigative Opthalmology & Visual Science 58, no. 7 (June 20, 2017): 3046. http://dx.doi.org/10.1167/iovs.17-21720.

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Rapisarda, Venerando, Rossella Salemi, Andrea Marconi, Carla Loreto, Adriana C. Graziano, Venera Cardile, Maria S. Basile, et al. "Fluoro-edenite induces fibulin-3 overexpression in non-malignant human mesothelial cells." Oncology Letters 12, no. 5 (August 26, 2016): 3363–67. http://dx.doi.org/10.3892/ol.2016.5051.

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Wang, X., X. Sun, X. Qu, C. Li, P. Yang, J. Jia, J. Liu, and Y. Zheng. "Overexpressed fibulin‐3 contributes to the pathogenesis of psoriasis by promoting angiogenesis." Clinical and Experimental Dermatology 44, no. 4 (August 26, 2018): e64-e72. http://dx.doi.org/10.1111/ced.13720.

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Daniel, Steffi, Marian Renwick, Viet Q. Chau, Shyamtanu Datta, Prabhavathi Maddineni, Gulab Zode, Emma M. Wade, Stephen P. Robertson, W. Matthew Petroll, and John D. Hulleman. "Fibulin-3 knockout mice demonstrate corneal dysfunction but maintain normal retinal integrity." Journal of Molecular Medicine 98, no. 11 (September 22, 2020): 1639–56. http://dx.doi.org/10.1007/s00109-020-01974-z.

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Murtha, L., N. Mabotuwana, S. Hardy, M. Bigland, B. Coulter, J. Hwang, J. Ye, et al. "Fibulin-3 is Necessary for the Formation of Infarct-Induced Cardiac Fibrosis." Heart, Lung and Circulation 28 (2019): S131. http://dx.doi.org/10.1016/j.hlc.2019.06.002.

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Vukovic, Jana, Lihua Y. Marmorstein, Precious J. McLaughlin, Takako Sasaki, Giles W. Plant, Alan R. Harvey, and Marc J. Ruitenberg. "Lack of fibulin-3 alters regenerative tissue responses in the primary olfactory pathway." Matrix Biology 28, no. 7 (September 2009): 406–15. http://dx.doi.org/10.1016/j.matbio.2009.06.001.

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Sanchez, C., C. Lambert, F. Comblain, C. Legrand, and Y. Henrotin. "Osteoarthritic sclerotic subchondral osteoblasts secreted elevated concentration of Fibulin-3 fragments in vitro." Osteoarthritis and Cartilage 24 (April 2016): S83. http://dx.doi.org/10.1016/j.joca.2016.01.176.

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Wang, Xinmei, Lisha Zhu, Jingxian Wu, and Yong Zhao. "The expression of Fibulin-3 in ovarian cancer and its relationship with prognosis." Translational Cancer Research 9, no. 9 (September 2020): 5173–81. http://dx.doi.org/10.21037/tcr-20-984.

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XU, SHUN, YONG YANG, YAN-BIN SUN, HAO-YOU WANG, CHANG-BO SUN, and XIN ZHANG. "Role of fibulin-3 in lung cancer: In vivo and in vitro analyses." Oncology Reports 31, no. 1 (October 18, 2013): 79–86. http://dx.doi.org/10.3892/or.2013.2799.

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Arechederra, María, Neibla Priego, Ana Vázquez-Carballo, Celia Sequera, Álvaro Gutiérrez-Uzquiza, María Isabel Cerezo-Guisado, Sara Ortiz-Rivero, et al. "p38 MAPK Down-regulates Fibulin 3 Expression through Methylation of Gene Regulatory Sequences." Journal of Biological Chemistry 290, no. 7 (December 29, 2014): 4383–97. http://dx.doi.org/10.1074/jbc.m114.582239.

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Caltabiano, Rosario, Carla Loreto, Ermanno Vitale, Serena Matera, Edoardo Miozzi, Marcello Migliore, Giuseppe Angelico, Rosario Tumino, Caterina Ledda, and Venerando Rapisarda. "Fibulin-3 immunoexpression in malignant mesothelioma due to fluoro-edenite: a preliminary report." Future Oncology 14, no. 6s (March 2018): 53–57. http://dx.doi.org/10.2217/fon-2017-0386.

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Vukovic, Jana, Marc J. Ruitenberg, Kasper Roet, Elske Franssen, Ajanthy Arulpragasam, Takako Sasaki, Joost Verhaagen, Alan R. Harvey, Samantha J. Busfield, and Giles W. Plant. "The glycoprotein fibulin-3 regulates morphology and motility of olfactory ensheathing cellsin vitro." Glia 57, no. 4 (March 2009): 424–43. http://dx.doi.org/10.1002/glia.20771.

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Henrotin, Yves, Myriam Gharbi, Gabriel Mazzucchelli, Jean-Emile Dubuc, Edwin De Pauw, and Michelle Deberg. "Fibulin 3 peptides Fib3-1 and Fib3-2 are potential biomarkers of osteoarthritis." Arthritis & Rheumatism 64, no. 7 (June 26, 2012): 2260–67. http://dx.doi.org/10.1002/art.34392.

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Bizzari, Sami, Lara El-Bazzal, Pratibha Nair, Antoine Younan, Samantha Stora, Cybel Mehawej, Stephany El-Hayek, Valerie Delague, and André Mégarbané. "Recessive marfanoid syndrome with herniation associated with a homozygous mutation in Fibulin-3." European Journal of Medical Genetics 63, no. 5 (May 2020): 103869. http://dx.doi.org/10.1016/j.ejmg.2020.103869.

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