Results 11 to 20 of about 10,140 (168)

Microenvironmental regulation by fibrillin-1.

open access: yesPLoS Genetics, 2012
Fibrillin-1 is a ubiquitous extracellular matrix molecule that sequesters latent growth factor complexes. A role for fibrillin-1 in specifying tissue microenvironments has not been elucidated, even though the concept that fibrillin-1 provides ...
Gerhard Sengle   +14 more
doaj   +4 more sources

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

open access: yesJ Cell Commun Signal, 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 ML, Reinhardt DP.
europepmc   +4 more sources

POGLUT2 and POGLUT3 O-glucosylate multiple EGF repeats in fibrillin-1, -2, and LTBP1 and promote secretion of fibrillin-1. [PDF]

open access: yesJ Biol Chem, 2021
Fibrillin-1 (FBN1) is the major component of extracellular matrix microfibrils, which are required for proper development of elastic tissues, including the heart and lungs. Through protein-protein interactions with latent transforming growth factor (TGF) β-binding protein 1 (LTBP1), microfibrils regulate TGF-β signaling.
Williamson DB   +3 more
europepmc   +4 more sources

Proteolysis of fibrillin-2 microfibrils is essential for normal skeletal development

open access: yeseLife, 2022
The embryonic extracellular matrix (ECM) undergoes transition to mature ECM as development progresses, yet few mechanisms ensuring ECM proteostasis during this period are known.
Timothy J Mead   +10 more
doaj   +1 more source

Circulating fibrillin fragment concentrations in patients with and without aortic pathology

open access: yesJVS - Vascular Science, 2022
Objective: Fragments of fibrillin-1 and fibrillin-2 will be detectable in the plasma of patients with aortic dissections and aneurysms. We sought to determine whether the plasma fibrillin fragment levels (PFFLs) differ between patients with thoracic ...
Eric J. Carlson, PhD   +11 more
doaj   +1 more source

The Multiple Functions of Fibrillin-1 Microfibrils in Organismal Physiology. [PDF]

open access: yesInt J Mol Sci, 2022
Fibrillin-1 is the major structural component of the 10 nm-diameter microfibrils that confer key physical and mechanical properties to virtually every tissue, alone and together with elastin in the elastic fibers. Mutations in fibrillin-1 cause pleiotropic manifestations in Marfan syndrome (MFS), including dissecting thoracic aortic aneurysms ...
Asano K   +3 more
europepmc   +4 more sources

Is There a Relationship Between Pelvic Organ Prolapse and Tissue Fibrillin-1 Levels? [PDF]

open access: yesInternational Neurourology Journal, 2015
Purpose: Pelvic organ prolapse is a multifactorial disorder in which extracellular matrix defects are implicated. Fibrillin-1 level is reduced in stress urinary incontinence.
Ayla Eser   +8 more
doaj   +1 more source

Role of fibrilins in human cancer: A narrative review

open access: yesHealth Science Reports, 2023
Background Fibrillin is one of the extracellular matrix glycoproteins and participates in forming microfibrils found in many connective tissues. The microfibrils enable the elasticity and stretching properties of the ligaments and support connective ...
Mahsa Mahdizadehi   +3 more
doaj   +1 more source

Homotypic Fibrillin-1 Interactions in Microfibril Assembly [PDF]

open access: yesJournal of Biological Chemistry, 2005
We have defined the homotypic interactions of fibrillin-1 to obtain new insights into microfibril assembly. Dose-dependent saturable high affinity binding was demonstrated between N-terminal fragments, between furin processed C-terminal fragments, and between these N- and C-terminal fragments.
Marson, Andrew   +8 more
openaire   +3 more sources

Involvement of Aquaporin 1 in the Motility and in the Production of Fibrillin 1 and Type I Collagen of Cultured Human Dermal Fibroblasts

open access: yesCosmetics, 2022
Aminocarbonyl proteins increase with age in the dermal layer. Gene Chip analysis of mRNA expression in human dermal fibroblasts cultured on collagen gels treated with glyceraldehyde as an aminocarbonyl protein and on untreated collagen gels showed a ...
Kazuhisa Maeda, Shiori Yoshida
doaj   +1 more source

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