Abstract/Details

The role of extracellular membrane matrix proteins and integrin alpha chains in three-dimensional capillary morphogenesis


2006 2006

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Abstract (summary)

Using siRNA technology, our studies show suppression of α 2 and α3 integrin subunits markedly blocks both EC capillary lumen formation and invasion, whereas suppression of the α 11 integrin subunit appears to promote EC invasion in model systems. Knockdown of type IV collagen, a major component in EC basement membranes, and type VI collagen, also showed inhibitory effects in EC capillary lumen formation and invasion. Additionally, siRNA directed to the α4 laminin chain, which has been shown to be important in microvessel stability, and the β2 aminin chain, which are both upregulated in DNA microarray studies, block EC capillary lumen formation and invasion as well. This work demonstrates that siRNA technology can be utilized to define the functional role of specific endothelial genes during capillary tube morphogenesis in 3D extracellular matrix environments, and validates a key role for specific integrin and basement membrane matrix genes in these events.

Indexing (details)


Subject
Molecular biology;
Cellular biology;
Pathology
Classification
0307: Molecular biology
0379: Cellular biology
0571: Pathology
Identifier / keyword
Health and environmental sciences; Biological sciences
Title
The role of extracellular membrane matrix proteins and integrin alpha chains in three-dimensional capillary morphogenesis
Author
Mareth, Amanda Katherine
Number of pages
53
Publication year
2006
Degree date
2006
School code
1388
Source
MAI 45/01M, Masters Abstracts International
Place of publication
Ann Arbor
Country of publication
United States
ISBN
9780542882784
Advisor
Davis, George E.
University/institution
The Texas A&M University System Health Science Center
University location
United States -- Texas
Degree
M.S.
Source type
Dissertations & Theses
Language
English
Document type
Dissertation/Thesis
Dissertation/thesis number
1437974
ProQuest document ID
304910227
Copyright
Database copyright ProQuest LLC; ProQuest does not claim copyright in the individual underlying works.
Document URL
http://search.proquest.com/docview/304910227
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