نتایج جستجو برای: fibrillin

تعداد نتایج: 907  

Journal: :The Journal of clinical investigation 2004
Daniel P Judge Nancy J Biery Douglas R Keene Jessica Geubtner Loretha Myers David L Huso Lynn Y Sakai Harry C Dietz

Marfan syndrome is a connective tissue disorder caused by mutations in the gene encoding fibrillin-1 (FBN1). A dominant-negative mechanism has been inferred based upon dominant inheritance, mulitimerization of monomers to form microfibrils, and the dramatic paucity of matrix-incorporated fibrillin-1 seen in heterozygous patient samples. Yeast artificial chromosome-based transgenesis was used to...

2014
Takahiro Fujita Eichi Tsuruga Kaori Yamanouchi Yoshihiko Sawa Hiroyuki Ishikawa

The ciliary zonule in the eye, also known as Zinn's zonule, is composed of oxytalan fibers, which are bundles of microfibrils consisting mainly of fibrillin-1. However, it is still unclear which of the microfibril-associated molecules present in the ciliary zonule controls oxytalan fibers. Microfibril-associated glycoprotein-1 (MAGP-1) is the only microfibril-associated molecule identified in t...

Journal: :The British journal of ophthalmology 2001
S Akhtar A J Bron N R Hawksworth R E Bonshek K M Meek

AIMS To investigate the ultrastructural localisation of proteoglycans (PG), betaig-h3 (keratoepithelin), tenascin-C (TN-C)), fibrillin, and fibronectin in bullous keratopathy (BK) corneas. METHODS Five corneas from cases of pseudophakic bullous keratopathy (BK) were examined by electron microscopy. PG were demonstrated using cuprolinic blue, and the proteins betaig-h3, TN-C, fibrillin, and fi...

Journal: :Journal of medical genetics 2006
P N Robinson E Arteaga-Solis C Baldock G Collod-Béroud P Booms A De Paepe H C Dietz G Guo P A Handford D P Judge C M Kielty B Loeys D M Milewicz A Ney F Ramirez D P Reinhardt K Tiedemann P Whiteman M Godfrey

Marfan syndrome (MFS), a relatively common autosomal dominant hereditary disorder of connective tissue with prominent manifestations in the skeletal, ocular, and cardiovascular systems, is caused by mutations in the gene for fibrillin-1 (FBN1). The leading cause of premature death in untreated individuals with MFS is acute aortic dissection, which often follows a period of progressive dilatatio...

Journal: :Investigative ophthalmology & visual science 1994
A Maier C N McDaniels R Mayne

PURPOSE Bovine extraocular rectus muscles were examined to map the distribution of elastin and fibrillin in extrafusal tissue and muscle spindles. METHODS Immunohistochemical techniques and immunolocalization were employed to pin-point the placement of molecules relative to muscle fibers. RESULTS Strands containing elastin and fibrillin surrounded all extrafusal fibers. They also covered th...

Journal: :Journal of cell science 2010
Teresa Massam-Wu Maybo Chiu Rawshan Choudhury Shazia S Chaudhry Andrew K Baldwin Amanda McGovern Clair Baldock C Adrian Shuttleworth Cay M Kielty

Control of the bioavailability of the growth factor TGFbeta is essential for tissue formation and homeostasis, yet precisely how latent TGFbeta is incorporated into the extracellular matrix is unknown. Here, we show that deposition of a large latent TGFbeta complex (LLC), which contains latent TGFbeta-binding protein 1 (LTBP-1), is directly dependent on the pericellular assembly of fibrillin mi...

Journal: :Circulation 2006
Gao Guo Patrick Booms Marc Halushka Harry C Dietz Andreas Ney Sigmar Stricker Jochen Hecht Stefan Mundlos Peter N Robinson

BACKGROUND The primary cause of early death in untreated Marfan syndrome (MFS) patients is aortic dilatation and dissection. METHODS AND RESULTS We investigated whether ascending aortic samples from the fibrillin-1-underexpressing mgR mouse model for MFS or a recombinant fibrillin-1 fragment containing an elastin-binding protein (EBP) recognition sequence can act as chemotactic stimuli for ma...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2014
Sacha A Jensen Georgia Aspinall Penny A Handford

Fibrillin microfibrils are 10-12 nm diameter, extracellular matrix assemblies that provide dynamic tissues of metazoan species with many of their biomechanical properties as well as sequestering growth factors and cytokines. Assembly of fibrillin monomers into microfibrils is thought to occur at the cell surface, with initial steps including proprotein processing, multimerization driven by the ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2006
Clair Baldock Veronique Siegler Daniel V Bax Stuart A Cain Kieran T Mellody Andrew Marson J Louise Haston Richard Berry Ming-Chuan Wang J Günter Grossmann Manfred Roessle Cay M Kielty Tim J Wess

Fibrillin-1 is a 330-kDa multidomain extracellular matrix protein that polymerizes to form 57-nm periodic microfibrils, which are essential for all tissue elasticity. Fibrillin-1 is a member of the calcium-binding EGF repeat family and has served as a prototype for structural analyses. Nevertheless, both the detailed structure of fibrillin-1 and its organization within microfibrils are poorly u...

Journal: :The Journal of biological chemistry 2003
Noe L Charbonneau Bette J Dzamba Robert N Ono Douglas R Keene Glen M Corson Dieter P Reinhardt Lynn Y Sakai

Fibrillins are microfibril-forming extracellular matrix macromolecules that modulate skeletal development. In humans, mutations in fibrillins result in long bone overgrowth as well as other distinct phenotypes. Whether fibrillins form independent microfibrillar networks or can co-polymerize, forming a single microfibril, is not known. However, this knowledge is required to determine whether phe...

نمودار تعداد نتایج جستجو در هر سال

با کلیک روی نمودار نتایج را به سال انتشار فیلتر کنید