World Library  


Add to Book Shelf
Flag as Inappropriate
Email this Book

Plos One : Fibrillin-1 Mutations Causing Weill-marchesani Syndrome and Acromicric and Geleophysic Dysplasias Disrupt Heparan Sulfate Interactions, Volume 7

By Zhang, Xin

Click here to view

Book Id: WPLBN0003937661
Format Type: PDF eBook :
File Size:
Reproduction Date: 2015

Title: Plos One : Fibrillin-1 Mutations Causing Weill-marchesani Syndrome and Acromicric and Geleophysic Dysplasias Disrupt Heparan Sulfate Interactions, Volume 7  
Author: Zhang, Xin
Volume: Volume 7
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
Publication Date:
Publisher: Plos

Citation

APA MLA Chicago

Zhang, X. (n.d.). Plos One : Fibrillin-1 Mutations Causing Weill-marchesani Syndrome and Acromicric and Geleophysic Dysplasias Disrupt Heparan Sulfate Interactions, Volume 7. Retrieved from http://netlibrary.net/


Description
Description : 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. This is in contrast to mutations within a heparin-binding TB domain (TB5), which is downstream of the arg-gly-asp cell adhesion domain, which can cause Weill-Marchesani syndrome (WMS) or Acromicric (AD) and Geleophysic Dysplasias (GD). WMS is characterized by short limbs, joint stiffness and ocular defects, whilst fibrillin-1 AD and GD have severe short stature, joint defects and thickened skin. We previously showed that TB5 binds heparin. Here, we show that the corresponding region of fibrillin-2 binds heparin very poorly, highlighting a novel functional difference between the two isoforms. This finding enabled us to map heparin/heparan sulfate binding to two sites on fibrillin-1 TB5 using a mutagenesis approach. Once these sites were mapped, we were able to investigate whether disease-causing mutations in this domain disrupt binding to HS. We show that a WMS deletion mutant, and five AD and GD point mutants all have disrupted heparin binding to TB5. These data provide insights into the biology of fibrillins and the pathologies of WMS, AD and GD.

 

Click To View

Additional Books


  • Plos One : Copper Bracelets and Magnetic... (by )
  • Plos One : Association Between Transform... (by )
  • Plos One : a Novel Micro-linear Vector f... (by )
  • Plos One : Wengen, the Sole Tumour Necro... (by )
  • Plos One : Genomic and Proteomic Analyse... (by )
  • Plos One : Increasing Maternal Age is As... (by )
  • Plos One : Radiation-induced Temporal Lo... (by )
  • Plos One : Activation of the Kinin B1 Re... (by )
  • Plos One : Interactions Between Zooplank... (by )
  • Plos One : Graft Transmission of Rna Sil... (by )
  • Plos One : Combinatorial Treatment of Dn... (by )
  • Plos One : Interacting Epidemics and Coi... (by )
Scroll Left
Scroll Right

 



Copyright © World Library Foundation. All rights reserved. eBooks from World Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.