Results 21 to 30 of about 1,605 (151)

Interaction of Tropoelastin with the Amino-terminal Domains of Fibrillin-1 and Fibrillin-2 Suggests a Role for the Fibrillins in Elastic Fiber Assembly [PDF]

Journal of Biological Chemistry, 2000
Alignment of tropoelastin molecules during the process of elastogenesis is thought to require fibrillin-containing microfibrils. In this study, we have demonstrated that amino-terminal domains of two microfibrillar proteins, fibrillin-1 and fibrillin-2, interact with tropoelastin in solid phase binding assays.
T M, Trask, B C, Trask, T M, Ritty, W R, Abrams, J, Rosenbloom, R P, Mecham   +5 more
openaire   +2 more sources

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

Biogenesis and function of fibrillin assemblies [PDF]

Cell and Tissue Research, 2009
Fibrillin-1 and fibrillin-2 are large cysteine-rich glycoproteins that serve two key physiological functions: as supporting structures that impart tissue integrity and as regulators of signaling events that instruct cell performance. The structural role of fibrillins is exerted through the temporal and hierarchical assembly of microfibrils and elastic ...
Francesco, Ramirez, Lynn Y, Sakai
openaire   +2 more sources

Material and mechanical properties of bones deficient for fibrillin-1 or fibrillin-2 microfibrils [PDF]

Matrix Biology, 2011
The contribution of non-collagenous components of the extracellular matrix to bone strength is largely undefined. Here we report that deficiency of fibrillin-1 or fibrillin-2 microfibrils causes distinct changes in bone material and mechanical properties. Morphometric examination of mice with hypomorphic or null mutations in fibrillin-1 or fibrillin-2,
Emilio, Arteaga-Solis, Lee, Sui-Arteaga, Minwook, Kim, Mitchell B, Schaffler, Karl J, Jepsen, Nancy, Pleshko, Francesco, Ramirez   +6 more
openaire   +2 more sources

Arabidopsis thaliana plastoglobule‐associated fibrillin 1a interacts with fibrillin 1b in vivo [PDF]

FEBS Letters, 2014
Plant fibrillins are a well‐conserved protein family found in the plastids of all photosynthetic organisms, where they perform a wide range of functions. A number of these proteins have been suggested to be involved in the maintenance of thylakoids and the formation of plastoglobules, preventing their coalescence and favoring their clustering via an as‐
Gámez Arjona, Francisco M., Raynaud, Sandy, Mérida Berlanga, Ángel, Concepción, Juan Carlos de la   +3 more
openaire   +5 more sources

Fibulin-4 deposition requires EMILIN-1 in the extracellular matrix of osteoblasts

Scientific Reports, 2017
Tissue microenvironments formed by extracellular matrix networks play an important role in regulating tissue structure and function. Extracellular microfibrillar networks composed of fibrillins and their associated ligands such as LTBPs, fibulins, and ...
Alvise Schiavinato, Douglas R. Keene, Thomas Imhof, Roberto Doliana, Takako Sasaki, Gerhard Sengle   +5 more
doaj   +1 more source

ENU mutagenesis reveals a novel phenotype of reduced limb strength in mice lacking fibrillin 2.

PLoS ONE, 2010
BackgroundFibrillins 1 (FBN1) and 2 (FBN2) are components of microfibrils, microfilaments that are present in many connective tissues, either alone or in association with elastin.
Gaynor Miller, Monica Neilan, Ruth Chia, Nabeia Gheryani, Natalie Holt, Annabelle Charbit, Sara Wells, Valter Tucci, Zuzanne Lalanne, Paul Denny, Elizabeth M C Fisher, Michael Cheeseman, Graham N Askew, T Neil Dear   +13 more
doaj   +1 more source

Fibrillin-1 and fibrillin-2 in human embryonic and early fetal development

Matrix Biology, 2002
The extracellular glycoproteins fibrillin-1 and fibrillin-2 are major components of connective tissue microfibrils. Mutations in the fibrillin-1 and fibrillin-2 genes are responsible for the phenotypical manifestations of Marfan syndrome and congenital contractural arachnodactyly respectively, which emphasizes their essential roles in developmental ...
Quondamatteo, Fabio, Reinhardt, D. P., Charbonneau, N. L., Pophal, G., Sakai, L. Y., Herken, R.   +5 more
openaire   +3 more sources

Fibrillin-1 and fibrillin-1-derived asprosin in adipose tissue function and metabolic disorders [PDF]

Journal of Cell Communication and Signaling, 2020
The extracellular matrix microenvironment of adipose tissue is of critical importance for the differentiation, remodeling and function of adipocytes. Fibrillin-1 is one of the main components of microfibrils and a key player in this process. Furin processing of profibrillin-1 results in mature fibrillin-1 and releases the C-terminal propeptide as a ...
Muthu L. Muthu, Dieter P. Reinhardt
openaire   +2 more sources

Elastin in the Liver

Frontiers in Physiology, 2016
A characteristic feature of liver cirrhosis is the accumulation of large amounts of connective tissue with the prevailing content of type I collagen. Elastin is a minor connective tissue component in normal liver but it is actively synthesized by hepatic
Jiri Kanta
doaj   +1 more source