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Related Concept Videos

Structural Protein Function01:56

Structural Protein Function

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Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Actin Filament Depolymerization01:19

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Actin filaments (F-actin) are composed of actin subunits. The dissociation of actin monomers can occur from either end of F-actin. The rate of dissociation is faster from the minus-end or the pointed end, where the actin subunits exist with a bound ADP, together known as ADP-actin. The depolymerization of F-actin is aided by proteins, including the actin-depolymerizing factor (ADF) and cofilin family of proteins, gelsolin, and glia maturation factor (GMF).
In F-actin, the ADF/cofilin proteins...
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Fibril-associated Collagen01:11

Fibril-associated Collagen

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

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Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

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Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
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Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

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In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
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Observing and Quantifying Fibroblast-mediated Fibrin Gel Compaction
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Microenvironmental regulation by fibrillin-1.

Gerhard Sengle1, Ko Tsutsui, Douglas R Keene

  • 1Department of Biochemistry and Molecular Biology, Oregon Health and Science University, Portland, Oregon, United States of America.

Plos Genetics
|January 14, 2012
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A novel fibrillin-1 mutation causes Weill-Marchesani syndrome (WMS) features in mice, distinct from Marfan syndrome. This highlights fibrillin-1’s role in maintaining tissue microenvironments and skin homeostasis.

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Area of Science:

  • Extracellular matrix biology
  • Connective tissue disorders
  • Molecular genetics

Background:

  • Fibrillin-1 is crucial for extracellular matrix structure and sequesters growth factors.
  • Mutations in FBN1 cause Marfan syndrome (MFS), characterized by tall stature, aortic issues, and eye problems, primarily via TGFβ signaling.
  • The role of fibrillin-1 in specifying tissue microenvironments is not fully understood.

Purpose of the Study:

  • To investigate the function of a novel FBN1 mutation associated with Weill-Marchesani syndrome (WMS).
  • To elucidate the mechanisms by which fibrillin-1 mutations affect tissue microenvironments and signaling pathways.
  • To differentiate the pathogenetic mechanisms of WMS from MFS.

Main Methods:

  • Generated and analyzed a mouse model with a novel FBN1 mutation identified in a WMS family.
  • Examined microfibril ultrastructure in WMS patients and mice.
  • Investigated the molecular interactions involving fibrillin-1, ADAMTSLIKE proteins, and ADAMTS-10.

Main Results:

  • The novel FBN1 mutation in mice recapitulated WMS phenotypes (thick skin, short stature, brachydactyly), confirming it does not cause MFS.
  • The mutation disrupted binding sites for ADAMTSLIKE-2, -3, -6, and papilin, implicating them in a pathway with fibrillin-1 and ADAMTS-10.
  • Microfibril scaffold modulation impacts local tissue microenvironments, affecting skin homeostasis and dermal collagen production.

Conclusions:

  • Dysregulated WMS microenvironments diverge from MFS pathogenetic mechanisms.
  • Fibrillin-1 microfibril scaffolds, modulated by ADAMTSLIKE proteins and ADAMTS enzymes, maintain tissue-specific microenvironments.
  • This study links fibrillin-1 function to skin homeostasis and collagen regulation, distinct from MFS pathways.