Fibulins: physiological and disease perspectives

Argraves, W. Scott; Greene, Lisa M.; Cooley, Marion A.; Gallagher, William M.

doi:10.1038/sj.embor.7400033

Cited by 285 publications

(251 citation statements)

References 64 publications

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“…The targets of miR-197 are ACVR1 and TSPAN3 genes while EFEMP2 is the target of miR-346 [156]. The EFEMP2 gene is thought to have tumor suppressor functions while the ACVR1 and TSPAN3 genes are involved in the control of cell growth and metastatic potential, respectively [157][158][159]. In vitro studies related with these miRNAs showed that their overexpression induced significant cell proliferation whereas inhibition caused growth arrest in human thyroid carcinoma follicular cells [154,156].…”

Section: Micrornasmentioning

confidence: 99%

An update on molecular biology of thyroid cancers

Ömür

Baran

2014

Critical Reviews in Oncology/Hematology

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Section: Micrornasmentioning

confidence: 99%

An update on molecular biology of thyroid cancers

Ömür

Baran

2014

Critical Reviews in Oncology/Hematology

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“…Fibulins are 50-200 kDa in size (Timpl et al, 2003) and have a series of calcium binding EGF-like domains followed by a carboxyterminal fibulin-like domain (Argraves et al, 2003). There are five members of the fibulin family.…”

Section: Fibulinsmentioning

confidence: 99%

New insights into elastic fiber assembly

Wagenseil

Mecham

2007

Birth Defects Research Pt C

357

354

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Elastic fibers provide recoil to tissues that undergo repeated stretch, such as the large arteries and lung. These large extracellular matrix (ECM) structures contain numerous components, and our understanding of elastic fiber assembly is changing as we learn more about the various molecules associated with the assembly process. The main components of elastic fibers are elastin and microfibrils. Elastin makes up the bulk of the mature fiber and is encoded by a single gene. Microfibrils consist mainly of fibrillin, but also contain or associate with proteins such as microfibril associated glycoproteins (MAGPs), fibulins, and EMILIN-1. Microfibrils were thought to facilitate alignment of elastin monomers prior to cross-linking by lysyl oxidase (LOX). We now know that their role, as well as the overall assembly process, is more complex. Elastic fiber formation involves elaborate spatial and temporal regulation of all of the involved proteins and is difficult to recapitulate in adult tissues. This report summarizes the known interactions between elastin and the microfibrillar proteins and their role in elastic fiber assembly based on in vitro studies and evidence from knockout mice. We also propose a model of elastic fiber assembly based on the current data that incorporates interactions between elastin, LOXs, fibulins and the microfibril, as well as the pivotal role played by cells in structuring the final functional fiber. Birth Defects Research (Part C) 81:229-240,

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“…Fibulins constitute a small family of five extracellular matrix proteins that share a distinctive carboxyl-terminal globular domain and a tandem array of calcium-binding epidermal growth factor-like modules (1,25). Fibulin-1 and fibulin-2 contain an additional domain of three anaphylatoxin modules preceding the calcium-binding epidermal growth factor-like repeats and therefore are larger than fibulin-3, -4, and -5, which have identical modular structures.…”

mentioning

confidence: 99%

Fibulin-2 Is Dispensable for Mouse Development and Elastic Fiber Formation

Sicot¹,

Tsuda²,

Markova³

et al. 2008

Molecular and Cellular Biology

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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.

show abstract

Fibulins: physiological and disease perspectives

Cited by 285 publications

References 64 publications

An update on molecular biology of thyroid cancers

An update on molecular biology of thyroid cancers

New insights into elastic fiber assembly

Fibulin-2 Is Dispensable for Mouse Development and Elastic Fiber Formation

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