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Journal articles on the topic 'Fibulin-2'

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Published: 4 June 2021

Last updated: 19 February 2022

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1

Sicot, Francois-Xavier, Takeshi Tsuda, Dessislava Markova, John F. Klement, Machiko Arita, Rui-Zhu Zhang, Te-Cheng Pan, Robert P. Mecham, David E. Birk, and Mon-Li Chu. "Fibulin-2 Is Dispensable for Mouse Development and Elastic Fiber Formation." Molecular and Cellular Biology 28, no. 3 (December 10, 2007): 1061–67. http://dx.doi.org/10.1128/mcb.01876-07.

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ABSTRACT Fibulin-2 is an extracellular matrix protein belonging to the five-member fibulin family, of which two members have been shown to play essential roles in elastic fiber formation during development. Fibulin-2 interacts with two major constituents of elastic fibers, tropoelastin and fibrillin-1, in vitro and localizes to elastic fibers in many tissues in vivo. The protein is prominently expressed during morphogenesis of the heart and aortic arch vessels and at early stages of cartilage development. To examine its role in vivo, we generated mice that do not express the fibulin-2 gene (Fbln2) through homologous recombination of embryonic stem cells. Unexpectedly, the fibulin-2-null mice were viable and fertile and did not display gross and anatomical abnormalities. Histological and ultrastructural analyses revealed that elastic fibers assembled normally in the absence of fibulin-2. No compensatory up-regulation of mRNAs for other fibulin members was detected in the aorta and skin tissue. However, in the fibulin-2 null aortae, fibulin-1 immunostaining was increased in the inner elastic lamina, where fibulin-2 preferentially localizes. The results demonstrate that fibulin-2 is not required for mouse development and elastic fiber formation and suggest possible functional redundancy between fibulin-1 and fibulin-2.

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2

Sasaki, T., H. Wiedemann, M. Matzner, M. L. Chu, and R. Timpl. "Expression of fibulin-2 by fibroblasts and deposition with fibronectin into a fibrillar matrix." Journal of Cell Science 109, no. 12 (December 1, 1996): 2895–904. http://dx.doi.org/10.1242/jcs.109.12.2895.

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The extracellular matrix protein fibulin-2 was shown to be a typical product of cultured human and mouse fibroblasts by several immunological assays. It is secreted and deposited in cells and tissues as a disulfide-bonded oligomer identical in size to the previously described recombinant fibulin-2. Most of the fibroblast fibulin-2 is deposited into a dense fibrillar meshwork which requires treatment with EDTA and/or 6 M urea for solubilization. Fibulin-2 and fibronectin are synthesized at equivalent levels and both colocalize in the fibrils as shown by immunofluorescence. Metabolic labelling and pulse-chase studies demonstrated fibulin-2 oligomers in detergent extracts of cells and their rapid translocation to extracellular EDTA-sensitive assembly forms. Unlike for fibronectin and fibulin-1 only a little fibulin-2 was found in the cell culture medium. Immunogold staining of confluent human fibroblasts showed localization of fibulin-2 to a fine meshwork or bundles of amorphous microfibrils in the matrix. This also demonstrated a distinct colocalization of fibulin-2 and fibronectin at the electron microscope level, indicating that the interaction between these two protein shown in in vitro assays may also exist in situ. No distinct colocalization of both proteins could, however, be observed with cross-striated fibrils of collagen I and collagen VI microfibrils.

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3

Pan, T. C., T. Sasaki, R. Z. Zhang, R. Fässler, R. Timpl, and M. L. Chu. "Structure and expression of fibulin-2, a novel extracellular matrix protein with multiple EGF-like repeats and consensus motifs for calcium binding." Journal of Cell Biology 123, no. 5 (December 1, 1993): 1269–77. http://dx.doi.org/10.1083/jcb.123.5.1269.

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A new protein, fibulin-2, was predicted from sequence analysis of cDNA clones obtained from a mouse fibroblast library. This protein consists of a 1195-residue polypeptide preceded by a 26-residue signal peptide. The COOH-terminal region of 787 amino acids contained three anaphylatoxin-related segments (domain I), 11 EGF-like repeats (domain II), 10 of which had a consensus motif for calcium-binding, and a 115-residue globular domain III. Except for two additional EGF-like repeats, this COOH-terminal region showed 43% sequence identity with the previously described fibulin-1 (BM-90). The NH2-terminal 408 residues, unique to fibulin-2, showed no sequence homology to other known proteins and presumably form two additional domains that differ in their cysteine content. Recombinant fibulin-2 was produced and secreted by human cell clones as a disulfide-bonded trimer. Rotary shadowing visualized the protein as three 40-45 nm long rods which are connected at one end in a globe-like structure. No significant immunological cross-reaction could be detected between fibulin-1 and fibulin-2. Production of the fibulin-2 was demonstrated by Northern blots and radioimmunoassay in fibroblasts but not in several tumor cell lines. Together with the observation that the serum level of fibulin-2 is 1,000-fold lower than that of fibulin-1, the data indicate that these two isoforms are not always coordinately expressed. This is also suggested by Northern blots of tissue mRNAs and by immunofluorescence localizations using mouse tissues. The latter studies also demonstrated an extracellular localization for fibulin-2 in basement membranes and other connective tissue compartments.

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4

Sofela, Agbolahan A., David A. Hilton, Sylwia Ammoun, Daniele Baiz, Claire L. Adams, Emanuela Ercolano, Michael D. Jenkinson, et al. "Fibulin-2: A Novel Biomarker for Differentiating Grade II from Grade I Meningiomas." International Journal of Molecular Sciences 22, no. 2 (January 8, 2021): 560. http://dx.doi.org/10.3390/ijms22020560.

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There is an unmet need for the identification of biomarkers to aid in the diagnosis, clinical management, prognosis and follow-up of meningiomas. There is currently no consensus on the optimum management of WHO grade II meningiomas. In this study, we identified the calcium binding extracellular matrix glycoprotein, Fibulin-2, via mass-spectrometry-based proteomics, assessed its expression in grade I and II meningiomas and explored its potential as a grade II biomarker. A total of 87 grade I and 91 grade II different meningioma cells, tissue and plasma samples were used for the various experimental techniques employed to assess Fibulin-2 expression. The tumours were reviewed and classified according to the 2016 edition of the Classification of the Tumours of the central nervous system (CNS). Mass spectrometry proteomic analysis identified Fibulin-2 as a differentially expressed protein between grade I and II meningioma cell cultures. Fibulin-2 levels were further evaluated in meningioma cells using Western blotting and Real-time Quantitative Polymerase Chain Reaction (RT-qPCR); in meningioma tissues via immunohistochemistry and RT-qPCR; and in plasma via Enzyme-Linked Immunosorbent Assay (ELISA). Proteomic analyses (p < 0.05), Western blotting (p < 0.05) and RT-qPCR (p < 0.01) confirmed significantly higher Fibulin-2 (FBLN2) expression levels in grade II meningiomas compared to grade I. Fibulin-2 blood plasma levels were also significantly higher in grade II meningioma patients compared to grade I patients. This study suggests that elevated Fibulin-2 might be a novel grade II meningioma biomarker, when differentiating them from the grade I tumours. The trend of Fibulin-2 expression observed in plasma may serve as a useful non-invasive biomarker.

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5

Sofela, Agbolahan A., David A. Hilton, Sylwia Ammoun, Daniele Baiz, Claire L. Adams, Emanuela Ercolano, Michael D. Jenkinson, et al. "Fibulin-2: A Novel Biomarker for Differentiating Grade II from Grade I Meningiomas." International Journal of Molecular Sciences 22, no. 2 (January 8, 2021): 560. http://dx.doi.org/10.3390/ijms22020560.

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There is an unmet need for the identification of biomarkers to aid in the diagnosis, clinical management, prognosis and follow-up of meningiomas. There is currently no consensus on the optimum management of WHO grade II meningiomas. In this study, we identified the calcium binding extracellular matrix glycoprotein, Fibulin-2, via mass-spectrometry-based proteomics, assessed its expression in grade I and II meningiomas and explored its potential as a grade II biomarker. A total of 87 grade I and 91 grade II different meningioma cells, tissue and plasma samples were used for the various experimental techniques employed to assess Fibulin-2 expression. The tumours were reviewed and classified according to the 2016 edition of the Classification of the Tumours of the central nervous system (CNS). Mass spectrometry proteomic analysis identified Fibulin-2 as a differentially expressed protein between grade I and II meningioma cell cultures. Fibulin-2 levels were further evaluated in meningioma cells using Western blotting and Real-time Quantitative Polymerase Chain Reaction (RT-qPCR); in meningioma tissues via immunohistochemistry and RT-qPCR; and in plasma via Enzyme-Linked Immunosorbent Assay (ELISA). Proteomic analyses (p < 0.05), Western blotting (p < 0.05) and RT-qPCR (p < 0.01) confirmed significantly higher Fibulin-2 (FBLN2) expression levels in grade II meningiomas compared to grade I. Fibulin-2 blood plasma levels were also significantly higher in grade II meningioma patients compared to grade I patients. This study suggests that elevated Fibulin-2 might be a novel grade II meningioma biomarker, when differentiating them from the grade I tumours. The trend of Fibulin-2 expression observed in plasma may serve as a useful non-invasive biomarker.

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6

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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7

Cangemi, Claudia, Vibe Skov, Michael Kjaer Poulsen, Jonas Funder, Waleed O. Twal, Mari-Anne Gall, Vibeke Hjortdal, et al. "Fibulin-1 Is a Marker for Arterial Extracellular Matrix Alterations in Type 2 Diabetes." Clinical Chemistry 57, no. 11 (November 1, 2011): 1556–65. http://dx.doi.org/10.1373/clinchem.2011.162966.

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BACKGROUND Extracellular matrix alterations are important elements in the arterial changes seen in diabetes, being associated with increased vascular stiffness and the development of cardiovascular diseases. However, no biomarkers for diabetes-related arterial changes have been defined. METHODS Mammary artery specimens from 17 men with type 2 diabetes and 18 nondiabetic individuals were used for microarray expression profiling, quantitative real-time PCR, immunoassay, and immunohistochemical analyses. A derived candidate marker, fibulin-1, which is an elastin-associated matrix molecule, was measured immunochemically in plasma from (a) 70 patients scheduled for vascular surgery, (b) 305 patients with type 2 diabetes examined with carotid ultrasonography and echocardiography, and (c) 308 patients with type 2 diabetes, followed for 15 years. RESULTS The most upregulated transcript in nonatherosclerotic arterial tissue from patients with type 2 diabetes encoded the extracellular matrix protein, fibulin-1. Higher concentrations of fibulin-1-protein were present in artery extracts from patients with diabetes than extracts from individuals without diabetes, and increased fibulin-1 immunostaining was apparent around the external elastic lamina of diabetic arteries. Patients with diabetes displayed increased plasma concentrations of fibulin-1 (P = 0.006). Plasma fibulin-1 concentrations correlated with hemoglobin A1c (P < 0.001), arterial stiffness indices including pulse pressure (P < 0.001), and carotid compliance (P = 0.004), as well as plasma N-terminal pro–B-type natriuretic peptide concentrations (P < 0.001) and were predictive of 15-year mortality (P = 0.013). CONCLUSIONS Fibulin-1 accumulates in the arterial wall and in plasma of patients with type 2 diabetes, and appears to be a factor associated with arterial extracellular matrix changes in type 2 diabetes.

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8

CASTOLDI, Mirco, and Mon-Li CHU. "Structural and functional characterization of the human and mouse fibulin-1 gene promoters: role of Sp1 and Sp3." Biochemical Journal 362, no. 1 (February 8, 2002): 41–50. http://dx.doi.org/10.1042/bj3620041.

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Fibulin-1 is a multifunctional extracellular protein involved in diverse biological processes including cardiovascular development, haemostasis and cancer. To investigate the transcriptional regulation of the gene encoding fibulin-1 we cloned and analysed about 4.0kb of the 5′-flanking regions of both the human and mouse fibulin-1 genes. The human and mouse fibulin-1 promoters share little sequence similarity except for a short region of approx. 150–170bp immediately upstream of the translation start site. The conserved region contains a TATA-like sequence (ATAATT) and multiple consensus binding sites for Sp1 and activator protein 2 (AP-2). That the short conserved region in each gene confers basal promoter activity is demonstrated by transient transfections of promoter deletion constructs for both the human and mouse genes into cells that express fibulin-1 constitutively. Co-transfections of promoter constructs with expression plasmids for Sp1, Sp3 and Sp4 into Drosophila SL2 cells indicate that Sp1 and Sp3 are essential for transcriptional activation and that these two factors act synergistically. Electrophoretic mobility-shift assays show that Sp1 and Sp3, but not AP-2, bind to the basal promoter of the human fibulin-1 gene. The results demonstrate the functional importance of Sp1 and Sp3 in regulating the expression of the fibulin-1 gene.

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9

Zhang, Hong-Yan, Rupert Timpl, Takako Sasaki, Mon-Li Chu, and Peter Ekblom. "Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo." Developmental Dynamics 205, no. 3 (March 1996): 348–64. http://dx.doi.org/10.1002/(sici)1097-0177(199603)205:3<348::aid-aja13>3.0.co;2-0.

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10

Zhang, Hangxiang, Jing Wu, Hailong Dong, Shaukat A. Khan, Mon-Li Chu, and Takeshi Tsuda. "Fibulin-2 deficiency attenuates angiotensin II-induced cardiac hypertrophy by reducing transforming growth factor-β signalling." Clinical Science 126, no. 4 (October 14, 2013): 275–88. http://dx.doi.org/10.1042/cs20120636.

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AngII (angiotensin II) is a potent neurohormone responsible for cardiac hypertrophy, in which TGF (transforming growth factor)-β serves as a principal downstream mediator. We recently found that ablation of fibulin-2 in mice attenuated TGF-β signalling, protected mice against progressive ventricular dysfunction, and significantly reduced the mortality after experimental MI (myocardial infarction). In the present study, we investigated the role of fibulin-2 in AngII-induced TGF-β signalling and subsequent cardiac hypertrophy. We performed chronic subcutaneous infusion of AngII in fibulin-2 null (Fbln2−/−), heterozygous (Fbln2+/−) and WT (wild-type) mice by a mini-osmotic pump. After 4 weeks of subpressor dosage of AngII infusion (0.2 μg/kg of body weight per min), WT mice developed significant hypertrophy, whereas the Fbln2−/− showed no response. In WT, AngII treatment significantly up-regulated mRNAs for fibulin-2, ANP (atrial natriuretic peptide), TGF-β1, Col I (collagen type I), Col III (collagen type III), MMP (matrix metalloproteinase)-2 and MMP-9, and increased the phosphorylation of TGF-β-downstream signalling markers, Smad2, TAK1 (TGF-β-activated kinase 1) and p38 MAPK (mitogen-activated protein kinase), which were all unchanged in AngII-treated Fbln2−/− mice. The Fbln2+/− mice consistently displayed AngII-induced effects intermediate between WT and Fbln2−/−. Pressor dosage of AngII (2 mg/kg of body weight per min) induced significant fibrosis in WT but not in Fbln2−/− mice with comparable hypertension and hypertrophy in both groups. Isolated CFs (cardiac fibroblasts) were treated with AngII, in which direct AngII effects and TGF-β-mediated autocrine effects was observed in WT. The latter effects were totally abolished in Fbln2−/− cells, suggesting that fibulin-2 is essential for AngII-induced TGF-β activation. In conclusion our data indicate that fibulin-2 is essential for AngII-induced TGF-β-mediated cardiac hypertrophy via enhanced TGF-β activation and suggest that fibulin-2 is a potential therapeutic target to inhibit AngII-induced cardiac remodelling.

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11

Kumra, Heena, Valentin Nelea, Hana Hakami, Amelie Pagliuzza, Jelena Djokic, Jiongci Xu, Hiromi Yanagisawa, and Dieter P. Reinhardt. "Fibulin-4 exerts a dual role in LTBP-4L–mediated matrix assembly and function." Proceedings of the National Academy of Sciences 116, no. 41 (September 23, 2019): 20428–37. http://dx.doi.org/10.1073/pnas.1901048116.

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Elastogenesis is a hierarchical process by which cells form functional elastic fibers, providing elasticity and the ability to regulate growth factor bioavailability in tissues, including blood vessels, lung, and skin. This process requires accessory proteins, including fibulin-4 and -5, and latent TGF binding protein (LTBP)-4. Our data demonstrate mechanisms in elastogenesis, focusing on the interaction and functional interdependence between fibulin-4 and LTBP-4L and its impact on matrix deposition and function. We show that LTBP-4L is not secreted in the expected extended structure based on its domain composition, but instead adopts a compact conformation. Interaction with fibulin-4 surprisingly induced a conformational switch from the compact to an elongated LTBP-4L structure. This conversion was only induced by fibulin-4 multimers associated with increased avidity for LTBP-4L; fibulin-4 monomers were inactive. The fibulin-4–induced conformational change caused functional consequences in LTBP-4L in terms of binding to other elastogenic proteins, including fibronectin and fibrillin-1, and of LTBP-4L assembly. A transient exposure of LTBP-4L with fibulin-4 was sufficient to stably induce conformational and functional changes; a stable complex was not required. These data define fibulin-4 as a molecular extracellular chaperone for LTBP-4L. The altered LTBP-4L conformation also promoted elastogenesis, but only in the presence of fibulin-4, which is required to escort tropoelastin onto the extended LTBP-4L molecule. Altogether, this study provides a dual mechanism for fibulin-4 in 1) inducing a stable conformational and functional change in LTBP-4L, and 2) promoting deposition of tropoelastin onto the elongated LTBP-4L.

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12

Ducros, E., A. Berthaut, P. Mirshahi, S. Lemarchand, J. Soria, J. M. Legeais, and M. Mirshahi. "Expression of Extracellular Matrix Proteins Fibulin-1 and Fibulin-2 by Human Corneal Fibroblasts." Current Eye Research 32, no. 6 (January 2007): 481–90. http://dx.doi.org/10.1080/02713680701411269.

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13

Miosge, Nicolai, Werner Götz, Takako Sasaki, Mon-Li Chu, Rupert Timpl, and Rainer Herken. "The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo." Histochemical Journal 28, no. 2 (February 1996): 109–16. http://dx.doi.org/10.1007/bf02331415.

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14

Hirai, Maretoshi, Tetsuya Ohbayashi, Masahito Horiguchi, Katsuya Okawa, Akari Hagiwara, Kenneth R. Chien, Toru Kita, and Tomoyuki Nakamura. "Fibulin-5/DANCE has an elastogenic organizer activity that is abrogated by proteolytic cleavage in vivo." Journal of Cell Biology 176, no. 7 (March 19, 2007): 1061–71. http://dx.doi.org/10.1083/jcb.200611026.

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Elastic fibers are required for the elasticity and integrity of various organs. We and others previously showed that fibulin-5 (also called developing arteries and neural crest EGF-like [DANCE] or embryonic vascular EGF-like repeat–containing protein [EVEC]) is indispensable for elastogenesis by studying fibulin-5–deficient mice, which recapitulate human aging phenotypes caused by disorganized elastic fibers (Nakamura, T., P.R. Lozano, Y. Ikeda, Y. Iwanaga, A. Hinek, S. Minamisawa, C.F. Cheng, K. Kobuke, N. Dalton, Y. Takada, et al. 2002. Nature. 415:171–175; Yanagisawa, H., E.C. Davis, B.C. Starcher, T. Ouchi, M. Yanagisawa, J.A. Richardson, and E.N. Olson. 2002. Nature. 415:168–171). However, the molecular mechanism by which fiblin-5 contributes to elastogenesis remains unknown. We report that fibulin-5 protein potently induces elastic fiber assembly and maturation by organizing tropoelastin and cross-linking enzymes onto microfibrils. Deposition of fibulin-5 on microfibrils promotes coacervation and alignment of tropoelastins on microfibrils, and also facilitates cross-linking of tropoelastin by tethering lysyl oxidase-like 1, 2, and 4 enzymes. Notably, recombinant fibulin-5 protein induced elastogenesis even in serum-free conditions, although elastogenesis in cell culture has been believed to be serum-dependent. Moreover, the amount of full-length fibulin-5 diminishes with age, while truncated fibulin-5, which cannot promote elastogenesis, increases. These data suggest that fibulin-5 could be a novel therapeutic target for elastic fiber regeneration.

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Ibrahim, Ayman M., Mohamed Roshdy, Sara Elshorbagy, Mohammed Hosny, Sarah Halawa, Dina Yehia, Hasnaa A. Elfawy, et al. "An Investigation of Fibulin-2 in Hypertrophic Cardiomyopathy." International Journal of Molecular Sciences 21, no. 19 (September 29, 2020): 7176. http://dx.doi.org/10.3390/ijms21197176.

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Hypertrophic cardiomyopathy (HCM) is the most common inherited heart muscle disease, with a prevalence of at least 1 in 500 in the general population. The disease is pleiotropic and is characterized by an increased stiffness of the myocardium, partly due to changes in the extracellular matrix (ECM), with elevated levels of interstitial fibrosis. Myocardial fibrosis is linked to impaired diastolic function and possibly phenotypic heterogeneity of HCM. The ECM consists of a very large number of proteins, which actively interact with each other as well as with myocardial cells. The role of other multiple components of the ECM in HCM has not been defined. Fibulin-2 is a glycoprotein component of the ECM, which plays an important role during embryogenesis of the heart; however, its role in adult myocardium has not been adequately studied. We here describe, for the first time, abnormal expression of fibulin-2 in the myocardium in patients with HCM as compared to normal controls. This abnormal expression was localized in the cytoplasm of myocardial cells and in the interstitial fibroblasts. In addition, fibulin-2 levels, measured by ELISA, were significantly elevated in the serum of patients with HCM as compared to normal controls.

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Gu, Yu-Chen, Kenneth Nilsson, Hubert Eng, and Marja Ekblom. "Association of extracellular matrix proteins fibulin-1 and fibulin-2 with fibronectin in bone marrow stroma." British Journal of Haematology 109, no. 2 (May 2000): 305–13. http://dx.doi.org/10.1046/j.1365-2141.2000.02011.x.

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17

Davila-Avila, Ned, Frida P. Muñiz-Ruvalcaba, Luis Fernando Hernandez-Zimbron, Roberto Gonzalez-Salinas, Claudia Corredor-Ortega, Jose Perez-Vazquez, Santiago Soberon, and Hugo Quiroz-Mercado. "Expression of Fibulin-2 and Fibulin-5 on subretinal fluid in human primary rhegmatogenous retinal detachment." Experimental Eye Research 194 (May 2020): 107992. http://dx.doi.org/10.1016/j.exer.2020.107992.

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18

Alcendor, Donald J., Susan Knobel, Prashant Desai, Wen Qui Zhu, and Gary S. Hayward. "KSHV Regulation of Fibulin-2 in Kaposi's Sarcoma." American Journal of Pathology 179, no. 3 (September 2011): 1443–54. http://dx.doi.org/10.1016/j.ajpath.2011.05.024.

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19

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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Sasaki, Takako, Karlheinz Mann, Gillian Murphy, Mon-Li Chu, and Rupert Timpl. "Different Susceptibilities of Fibulin-1 and Fibulin-2 to Cleavage by Matrix Metalloproteinases and Other Tissue Proteases." European Journal of Biochemistry 240, no. 2 (September 1996): 427–34. http://dx.doi.org/10.1111/j.1432-1033.1996.0427h.x.

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21

Gu, Yu-Chen, Jan Fredrik Talts, Donald Gullberg, Rupert Timpl, and Marja Ekblom. "Glucocorticoids down-regulate the extracellular matrix proteins fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma." European Journal of Haematology 67, no. 3 (September 2001): 176–84. http://dx.doi.org/10.1034/j.1600-0609.2001.5790528.x.

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22

Yan, Bingdi, Yanbing Hu, Tiangang Ma, and Yanjun Wang. "IDH1 mutation promotes lung cancer cell proliferation through methylation of Fibulin-5." Open Biology 8, no. 10 (October 2018): 180086. http://dx.doi.org/10.1098/rsob.180086.

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Mutation in isocitrate dehydrogenase ( IDH ) leads to an aberrant function of the enzyme, leading to the production of hydroxyglutarate, as well as changes in cellular metabolism, DNA methylation and histone modification. Previous studies uncovered mutations in IDH1 in several malignancies, with the most frequent mutation being IDH1 R132H. It has been demonstrated that IDH1 expression is induced in non-small-cell lung cancer (NSCLC). However, the contribution of IDH1 mutation in the malignant transformation and development of NSCLC is unclear. In our study, we show that IDH1 R132H enhanced the migration and proliferation of NSCLC cells. Moreover, IDH1 R132H was a crucial modulator of 2-hydroxyglutarate, whose production from cells with IDH1 mutation promoted the binding of DNA-methyltransferase 1 (DNMT1) to the Fibulin-5 promoter, leading to its methylation. As a result, Fibulin-5 silencing in cells with IDH1 mutation enhanced the migration and proliferation of NSCLC cells. We show that the IDH1 mutation was present in tissues sampled from patients with NSCLC, which was reversely linked to Fibulin-5 expression. In this study, we suggest an innovative model for IDH1 R132H/Fibulin-5 pathway, which could throw light upon the activity of IDH1 R132H in NSCLC.

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23

Burchert, D., F. Wagenlehner, K. Steger, W. Weidner, S. Gattenloehner, and T. Dansranjavin. "280 Epigenetic regulation of fibulin-2 in prostate cancer." European Urology Supplements 14, no. 2 (April 2015): e280. http://dx.doi.org/10.1016/s1569-9056(15)60277-9.

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24

Utani, A., M. Nomizu, R. Timpl, and Y. Yamada. "038 Supramolecular assembly of laminin family and fibulin-2." Journal of Dermatological Science 12, no. 2 (June 1996): 188. http://dx.doi.org/10.1016/0923-1811(96)89440-0.

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25

Yamauchi, Yoshinori, Eichi Tsuruga, Kazuki Nakashima, Yoshihiko Sawa, and Hiroyuki Ishikawa. "Fibulin-4 and -5, but not Fibulin-2, are Associated with Tropoelastin Deposition in Elastin-Producing Cell Culture." ACTA HISTOCHEMICA ET CYTOCHEMICA 43, no. 6 (2010): 131–38. http://dx.doi.org/10.1267/ahc.10026.

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Lemaire, Raphael, Joseph H. Korn, William P. Schiemann, and Robert Lafyatis. "Fibulin-2 and Fibulin-5 Alterations in Tsk Mice Associated with Disorganized Hypodermal Elastic Fibers and Skin Tethering." Journal of Investigative Dermatology 123, no. 6 (December 2004): 1063–69. http://dx.doi.org/10.1111/j.0022-202x.2004.23471.x.

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Miosge, N., T. Sasaki, M. L. Chu, R. Herken, and R. Timpl. "Ultrastructural localization of microfibrillar fibulin-1 and fibulin-2 during heart development indicates a switch in molecular associations." Cellular and Molecular Life Sciences (CMLS) 54, no. 6 (June 1, 1998): 606–13. http://dx.doi.org/10.1007/s000180050188.

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28

Chapman, Shelby L., F. X. Sicot, Elaine C. Davis, Jianbin Huang, Takako Sasaki, Mon-Li Chu, and Hiromi Yanagisawa. "Fibulin-2 and Fibulin-5 Cooperatively Function to Form the Internal Elastic Lamina and Protect From Vascular Injury." Arteriosclerosis, Thrombosis, and Vascular Biology 30, no. 1 (January 2010): 68–74. http://dx.doi.org/10.1161/atvbaha.109.196725.

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29

Kusubata, Masashi, Arisa Hirota, Tetsuya Ebihara, Kumiko Kuwaba, Youco Matsubara, Takako Sasaki, Moriaki Kusakabe, Teruyo Tsukada, Shinkichi Irie, and Yoh-ichi Koyama. "Spatiotemporal Changes of Fibronectin, Tenascin-C, Fibulin-1, and Fibulin-2 in the Skin During the Development of Chronic Contact Dermatitis." Journal of Investigative Dermatology 113, no. 6 (December 1999): 906–12. http://dx.doi.org/10.1046/j.1523-1747.1999.00802.x.

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30

Boss, Anna L., Lawrence W. Chamley, Anna E. S. Brooks, and Joanna L. James. "Differences in human placental mesenchymal stromal cells may impair vascular function in FGR." Reproduction 162, no. 4 (October 1, 2021): 319–30. http://dx.doi.org/10.1530/rep-21-0226.

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Placentae from pregnancies with foetal growth restriction (FGR) exhibit poor oxygen and nutrient exchange, in part due to impaired placental vascular development. Placental mesenchymal stromal cells (pMSCs) reside in a perivascular niche, where they may influence blood vessel formation/function. However, the role of pMSCs in vascular dysfunction in FGR is unclear. To elucidate the mechanisms by which pMSCs may impact placental vascularisation we compared the transcriptomes of human pMSCs isolated from FGR (<5th centile) (n = 7) and gestation-matched control placentae (n = 9) using Affymetrix microarrays. At the transcriptome level, there were no statistically significant differences between normal and FGR pMSCs; however, several genes linked to vascular function exhibited notable fold changes, and thus the dataset was used as a hypothesis-generating tool for possible dysfunction in FGR. Genes/proteins of interest were followed up by real-time PCR, western blot and immunohistochemistry. Gene expression of ADAMTS1 and FBLN2 (fibulin-2) were significantly upregulated, whilst HAS2 (hyaluronan synthase-2) was significantly downregulated, in pMSCs from FGR placentae (n = 8) relative to controls (n = 7, P < 0.05 for all). At the protein level, significant differences in the level of fibulin-2 and hyaluronan synthase-2, but not ADAMTS1, were confirmed between pMSCs from FGR and control pregnancies by Western blot. All three proteins demonstrated perivascular expression in third-trimester placentae. Fibulin-2 maintains vessel elasticity, and its increased expression in FGR pMSCs could help explain the increased distensibility of FGR blood vessels. ADAMTS1 and hyaluronan synthase-2 regulate angiogenesis, and their differential expression by FGR pMSCs may contribute to the impaired angiogenesis in these placentae.

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31

Yi, Chun-Hui, David J. Smith, William W. West, and Michael A. Hollingsworth. "Loss of Fibulin-2 Expression Is Associated with Breast Cancer Progression." American Journal of Pathology 170, no. 5 (May 2007): 1535–45. http://dx.doi.org/10.2353/ajpath.2007.060478.

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32

Baird, Brandi N., Mark J. Schliekelman, Young-Ho Ahn, Yulong Chen, Jonathon D. Roybal, Bartley J. Gill, Dhruva K. Mishra, et al. "Fibulin-2 Is a Driver of Malignant Progression in Lung Adenocarcinoma." PLoS ONE 8, no. 6 (June 10, 2013): e67054. http://dx.doi.org/10.1371/journal.pone.0067054.

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33

Sasaki, Takako, Walter Göhring, Te-Cheng Pan, Mon-Li Chu, and Rupert Timpl. "Binding of Mouse and Human Fibulin-2 to Extracellular Matrix Ligands." Journal of Molecular Biology 254, no. 5 (December 1995): 892–99. http://dx.doi.org/10.1006/jmbi.1995.0664.

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34

Grassel, Susanne, Francois-Xavier Sicot, Susan Gotta, and Mon-Li Chu. "Mouse fibulin-2 gene. Complete exon-intron organization and promoter characterization." European Journal of Biochemistry 263, no. 2 (July 15, 1999): 471–77. http://dx.doi.org/10.1046/j.1432-1327.1999.00523.x.

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35

Collod, Gwenaëlle, Mon-Li Chu, Takako Sasaki, Monique Coulon, Rupert Timpl, Loretta Renkart, Jean Weissenbach, et al. "Fibulin-2: Genetic Mapping and Exclusion as a Candidate Gene in Marfan Syndrome Type 2." European Journal of Human Genetics 4, no. 5 (1996): 292–95. http://dx.doi.org/10.1159/000472216.

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36

Tsuda, Takeshi, Jing Wu, Erhe Gao, Jennifer Joyce, Dessislava Markova, Hailong Dong, Ying Liu, et al. "Loss of fibulin-2 protects against progressive ventricular dysfunction after myocardial infarction." Journal of Molecular and Cellular Cardiology 52, no. 1 (January 2012): 273–82. http://dx.doi.org/10.1016/j.yjmcc.2011.11.001.

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37

Reinhardt, Dieter P., Takako Sasaki, Bette J. Dzamba, Douglas R. Keene, Mon-Li Chu, Walter Göhring, Rupert Timpl, and Lynn Y. Sakai. "Fibrillin-1 and Fibulin-2 Interact and Are Colocalized in Some Tissues." Journal of Biological Chemistry 271, no. 32 (August 9, 1996): 19489–96. http://dx.doi.org/10.1074/jbc.271.32.19489.

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38

Kanan, Yogita, Daniel Brobst, Zongchao Han, Muna I. Naash, and Muayyad R. Al-Ubaidi. "Fibulin 2, a TyrosineO-Sulfated Protein, Is Up-regulated Following Retinal Detachment." Journal of Biological Chemistry 289, no. 19 (April 1, 2014): 13419–33. http://dx.doi.org/10.1074/jbc.m114.562157.

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39

Chan, Wilson, Hodan Ismail, Dominique Mayaki, Veronica Sanchez, Kerstin Tiedemann, Elaine C. Davis, and Sabah N. A. Hussain. "Fibulin-5 Regulates Angiopoietin-1/Tie-2 Receptor Signaling in Endothelial Cells." PLOS ONE 11, no. 6 (June 15, 2016): e0156994. http://dx.doi.org/10.1371/journal.pone.0156994.

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40

Yazici, Hulya, Mukaddes Avsar, Ozge Sukruoglu, Seda Kilic, Demet Akdeniz, Bugra Tuncer, Rumeysa Ciftci, Aysel Ahmedova, Sezai Vatansever, and Makbule Tambas. "The different roles on metastasis of fibulin-2 gene in lung cancer." Journal of Clinical Oncology 32, no. 15_suppl (May 20, 2014): e19130-e19130. http://dx.doi.org/10.1200/jco.2014.32.15_suppl.e19130.

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41

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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42

Zhang, Xiliang, Lian Duan, Yuxing Zhang, Huibin Zhao, Xiaodong Yang, and Chaojun Zhang. "Correlation of Fibulin‑2 expression with proliferation, migration and invasion of breast cancer cells." Oncology Letters 20, no. 2 (June 17, 2020): 1945–51. http://dx.doi.org/10.3892/ol.2020.11747.

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43

Hunzelmann, N., R. Nischt, P. Brenneisen, A. Eickert, and T. Krieg. "Increased deposition of fibulin-2 in solar elastosis and its colocalization with elastic fibres." British Journal of Dermatology 145, no. 2 (August 2001): 217–22. http://dx.doi.org/10.1046/j.1365-2133.2001.04337.x.

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44

Cooley, Marion A., Keerthi Harikrishnan, James A. Oppel, Sloan F. Miler, Jeremy L. Barth, Courtney J. Haycraft, Sakamuri V. Reddy, and W. Scott Argraves. "Fibulin-1 is required for bone formation and Bmp-2-mediated induction of Osterix." Bone 69 (December 2014): 30–38. http://dx.doi.org/10.1016/j.bone.2014.07.038.

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45

Gruemmer, R., L. Klein-Hitpaß, and J. Neulen. "Regulation of gene expression in endothelial cells: the role of human follicular fluid." Journal of Molecular Endocrinology 34, no. 1 (February 2005): 37–46. http://dx.doi.org/10.1677/jme.1.01589.

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A precise regulation of angiogenesis is a prerequisite for an adequate maturation of ovarian follicles. Despite the production of vascular endothelial growth factor (VEGF) by granulosa cells in antral follicles, angiogenesis is restricted to the theca cell layer. The maturing follicle remains avascular before ovulation, implying regulatory mechanisms which prevent premature follicular vascularization. In order to investigate the role of follicular fluid and of granulosa cells in the regulation of endothelial gene expression, human umbilical vein endothelial cells (HUVECs) were incubated in vitro with media conditioned with human follicular fluid obtained from individual patients undergoing oocyte retrieval for in vitro fertilization procedures or with culture medium conditioned by human granulosa cells respectively. Using microarray technology, the gene expression pattern was compared between untreated monolayers of HUVECs and HUVECs treated either with follicular fluid or with granulosa cell conditioned media. We identified a total of 15 genes that were significantly up-regulated and 11 genes that were significantly down-regulated in endothelial cells treated with follicular fluid at least 2.5-fold in more than 70% of comparisons. Up-regulated genes involved in angiogenesis were the anti-angiogenic factors gro-beta (16.5-fold), angiopoietin-2 (3.9-fold), alpha-2-macroglobulin (24.3-fold) and the pro-angiogenic factors E-selectin (5.3-fold) and vascular cell adhesion molecule-1 (VCAM-1) (4.4-fold), whereas a significant down-regulation of the pro-angiogenic genes fibulin-5 (3.5-fold) and elastin (14.9-fold) could be observed. Culturing of HUVECs with conditioned medium from cultured human luteinized granulosa cells demonstrated a similar regulatory pattern of gene expression for fibulin-5, elastin, gro-beta, and E-selectin. The gene regulation in endothelial cells by follicular fluid could be confirmed by RT-PCR for gro-beta, angiopoietin-2, elastin, fibulin-5, and E-selectin. The present work reveals that compounds secreted by granulosa cells lead to the expression of anti-angiogenic factors on the transcript level in endothelial cells and thus could help to explain the temporal and spatial discrepancy between the high expression of VEGF and the restricted angiogenesis in the preovulatory follicle.

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Chailley-Heu, Bernadette, Olivier Boucherat, Anne-Marie Barlier-Mur, and Jacques R. Bourbon. "FGF-18 is upregulated in the postnatal rat lung and enhances elastogenesis in myofibroblasts." American Journal of Physiology-Lung Cellular and Molecular Physiology 288, no. 1 (January 2005): L43—L51. http://dx.doi.org/10.1152/ajplung.00096.2004.

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The fibroblast growth factors (FGFs) are key players in fetal lung development, but little is known about their status in postnatal lung. Here, we investigated the expression pattern of FGF-18 transcripts through the perinatal period and evidenced a sevenfold increase after birth that paralleled changes in elastin expression. In vitro, recombinant human (rh)FGF-18 had a mitogenic activity on day 21 fetal rat lung fibroblasts and stimulated its own expression in the latter, whereas FGF-2 inhibited it. At 50 or 100 ng/ml, rhFGF-18 increased the expression of α-smooth muscle actin (α-SMA; 2.5-fold), a characteristic marker of myofibroblasts, of tropoelastin (6.5-fold), of lysyl oxidase (2-fold), and of fibulins 1 and 5 (8- and 2.2-fold) in confluent fibroblasts isolated from fetal day 21 lung; similar results were obtained with fibroblasts from day 3 postnatal lungs. Elastin protein expression was also slightly increased in fetal fibroblasts. Lung analysis on day 4 in rat pups that had received rhFGF-18 (3 μg) on days 0 and 1 showed a 1.7-fold increase of tropoelastin transcripts, whereas α-SMA transcripts were unchanged. In contrast, rhFGF-2 markedly decreased expression of elastin in vitro and in vivo and of fibulin 5 in vitro. In addition, vitamin A, which is known to enhance alveolar development, elevated FGF-18 and elastin expressions in day 2 lungs, thus advancing the biological increase. We postulate that FGF-18 is involved in postnatal lung development through stimulating myofibroblast proliferation and differentiation.

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Schaeffer, Julia, David Tannahill, Jean-Michel Cioni, Dáire Rowlands, and Roger Keynes. "Identification of the extracellular matrix protein Fibulin-2 as a regulator of spinal nerve organization." Developmental Biology 442, no. 1 (October 2018): 101–14. http://dx.doi.org/10.1016/j.ydbio.2018.06.014.

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48

Olin, Anders I., Matthias Mörgelin, Takako Sasaki, Rupert Timpl, Dick Heinegård, and Anders Aspberg. "The Proteoglycans Aggrecan and Versican Form Networks with Fibulin-2 through Their Lectin Domain Binding." Journal of Biological Chemistry 276, no. 2 (October 18, 2000): 1253–61. http://dx.doi.org/10.1074/jbc.m006783200.

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49

Sasaki, T. "Dimer model for the microfibrillar protein fibulin-2 and identification of the connecting disulfide bridge." EMBO Journal 16, no. 11 (June 1, 1997): 3035–43. http://dx.doi.org/10.1093/emboj/16.11.3035.

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50

Olijnyk, D., A. M. Ibrahim, R. K. Ferrier, T. Tsuda, M. L. Chu, B. A. Gusterson, T. Stein, and J. S. Morris. "Fibulin-2 is involved in early extracellular matrix development of the outgrowing mouse mammary epithelium." Cellular and Molecular Life Sciences 71, no. 19 (February 13, 2014): 3811–28. http://dx.doi.org/10.1007/s00018-014-1577-4.

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