Results 31 to 40 of about 10,140 (168)

Processing and assembly of fibrillin‐1

International Journal of Experimental Pathology, 2000
Fibrillins are extracellular matrix proteins of ˜350 kD. They have a complex multidomain structure and are the major components of microfibrillar structures in both elastic and nonelastic tissues (Sakai et al. 1986; Kielty & Shuttleworth 1995). Mutations in the FBN-1 gene cause Marfan Syndrome, which is a heritable connective tissue disease with an ...
Matthew J. Rock, C. Adrian Shuttleworth, Cay M. Kielty   +2 more
openaire   +2 more sources

The influence of fibrillin‐1 and physical activity upon tendon tissue morphology and mechanical properties in mice

Physiological Reports, 2019
Fibrillin‐1 mutations cause pathological changes in connective tissue that constitute the complex phenotype of Marfan syndrome. In this study, we used fibrillin‐1 hypomorphic and haploinsufficient mice (Fbn1mgr/mgR and Fbn1+/− mice, respectively) to ...
Peter H. T. Tran, Tanja Skrba, Elisabeth Wondimu, Giuseppina Galatioto, René Brüggebusch Svensson, Annesofie T. Olesen, Abigail L. Mackey, S. Peter Magnusson, Francesco Ramirez, Michael Kjaer   +9 more
doaj   +1 more source

The evolution of extracellular fibrillins and their functional domains.

PLoS ONE, 2012
Fibrillins constitute the major backbone of multifunctional microfibrils in elastic and non-elastic extracellular matrices, and are known to interact with several binding partners including tropoelastin and integrins.
Adam Piha-Gossack, Wayne Sossin, Dieter P Reinhardt   +2 more
doaj   +1 more source

Extracellular matrix and vascular dynamics in the kidney of a murine model for Marfan syndrome.

PLoS ONE, 2023
Fibrillin-1 is a pivotal structural component of the kidney's glomerulus and peritubular tissue. Mutations in the fibrillin-1 gene result in Marfan syndrome (MFS), an autosomal dominant disease of the connective tissue.
Rodrigo Barbosa de Souza, Renan Barbosa Lemes, Orestes Foresto-Neto, Luara Lucena Cassiano, Dieter P Reinhardt, Keith M Meek, Ivan Hong Jun Koh, Philip N Lewis, Lygia V Pereira   +8 more
doaj   +1 more source

Fibrillin-1 mutations causing Weill-Marchesani syndrome and acromicric and geleophysic dysplasias disrupt heparan sulfate interactions.

PLoS ONE, 2012
The extracellular glycoprotein fibrillin-1 forms microfibrils that act as the template for elastic fibers. Most mutations in fibrillin-1 cause Marfan syndrome with severe cardiovascular and ocular symptoms, and tall stature.
Stuart A Cain, Amanda McGovern, Andrew K Baldwin, Clair Baldock, Cay M Kielty   +4 more
doaj   +1 more source

Fibulin-5 interacts with fibrillin-1 molecules and microfibrils [PDF]

Biochemical Journal, 2005
Fibulin-5 plays an important role in elastic fibre formation in vivo. We have investigated the molecular interactions between fibulin-5 and components of fibrillin-rich microfibrils which form a template for elastin. Fibulin-5 interacted in a dose-dependent manner with a fibrillin-1 N-terminal sequence and with tropoelastin, but not with MAGP-1 ...
Freeman, LJ, Lomas, A, Hodson, N, Sherratt, MJ, Mellody, KT, Weiss, AS, Shuttleworth, A, Kielty, CM   +7 more
openaire   +3 more sources

Targeted deletion of fibrillin-1 in the mouse eye results in ectopia lentis and other ocular phenotypes associated with Marfan syndrome

Disease Models & Mechanisms, 2019
Fibrillin is an evolutionarily ancient protein that lends elasticity and resiliency to a variety of tissues. In humans, mutations in fibrillin-1 cause Marfan and related syndromes, conditions in which the eye is often severely affected.
Wendell Jones, Juan Rodriguez, Steven Bassnett   +2 more
doaj   +1 more source

Association of FBN1 polymorphism with susceptibility of adolescent idiopathic scoliosis: a case-control study

BMC Musculoskeletal Disorders, 2022
Background Fibrillin-1 (FBN1) is an extracellular matrix glycoprotein essential to the structural component of microfibrils and FBN1 gene polymorphisms can be associated with adolescent idiopathic scoliosis (AIS) susceptibility.
Gustavo Borges Laurindo de Azevedo, Jamila Alessandra Perini, Antônio Eulálio Pedrosa Araújo Junior, Luis Antonio Medeiros Moliterno, Rodrigo Mantelatto Andrande, João Antonio Matheus Guimarães, Helton Luiz Aparecido Defino   +6 more
doaj   +1 more source

Proteomic fingerprints of damage in extracellular matrix assemblies

Matrix Biology Plus, 2020
In contrast to the dynamic intracellular environment, structural extracellular matrix (ECM) proteins with half-lives measured in decades, are susceptible to accumulating damage.
Alexander Eckersley, Matiss Ozols, Ronan O'Cualain, Emma-Jayne Keevill, April Foster, Suzanne Pilkington, David Knight, Christopher E.M. Griffiths, Rachel E.B. Watson, Michael J. Sherratt   +9 more
doaj   +1 more source

P3.11 INCREASED CAROTID PLAQUE OCCURRENCE IN MEN WITH THE FIBRILLIN-1 2–3 GENOTYPE

Artery Research, 2009
Background: Fibrillin-1 is an important constituent of the vascular wall and earlier studies have indicated an effect of the fibrillin-1 2–3 genotype on blood pressure as well as aortic stiffness.
R. DeBasso, B. Hedblad, J. Carlson, G. Berglund, T. Länne   +4 more
doaj   +1 more source