Document Detail


Long-range mechanical force enables self-assembly of epithelial tubular patterns.
MedLine Citation:
PMID:  22427356     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Enabling long-range transport of molecules, tubules are critical for human body homeostasis. One fundamental question in tubule formation is how individual cells coordinate their positioning over long spatial scales, which can be as long as the sizes of tubular organs. Recent studies indicate that type I collagen (COL) is important in the development of epithelial tubules. Nevertheless, how cell-COL interactions contribute to the initiation or the maintenance of long-scale tubular patterns is unclear. Using a two-step process to quantitatively control cell-COL interaction, we show that epithelial cells developed various patterns in response to fine-tuned percentages of COL in ECM. In contrast with conventional thoughts, these patterns were initiated and maintained by traction forces created by cells but not diffusive factors secreted by cells. In particular, COL-dependent transmission of force in the ECM led to long-scale (up to 600 μm) interactions between cells. A mechanical feedback effect was encountered when cells used forces to modify cell positioning and COL distribution and orientations. Such feedback led to a bistability in the formation of linear, tubule-like patterns. Using micro-patterning technique, we further show that the stability of tubule-like patterns depended on the lengths of tubules. Our results suggest a mechanical mechanism that cells can use to initiate and maintain long-scale tubular patterns.
Authors:
Chin-Lin Guo; Mingxing Ouyang; Jiun-Yann Yu; Jordan Maslov; Andrew Price; Chih-Yu Shen
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-03-16
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  109     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-04-12     Completed Date:  2012-06-04     Revised Date:  2013-06-26    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  5576-82     Citation Subset:  IM    
Affiliation:
Bioengineering, California Institute of Technology, MS 138-78, 1200 East California Boulevard, Pasadena, CA 91125, USA. guochin@caltech.edu
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MeSH Terms
Descriptor/Qualifier:
Animals
Biomechanics / drug effects
Cell Line
Collagen / pharmacology
Diffusion / drug effects
Epithelial Cells / cytology,  drug effects,  metabolism*
Focal Adhesion Protein-Tyrosine Kinases / metabolism
Humans
Mechanotransduction, Cellular / drug effects
Models, Biological
Phosphatidylinositol 3-Kinases / metabolism
Rats
Up-Regulation / drug effects
rac1 GTP-Binding Protein / metabolism
Chemical
Reg. No./Substance:
9007-34-5/Collagen; EC 2.7.1.-/Phosphatidylinositol 3-Kinases; EC 2.7.10.2/Focal Adhesion Protein-Tyrosine Kinases; EC 3.6.5.2/rac1 GTP-Binding Protein
Comments/Corrections
Comment In:
Proc Natl Acad Sci U S A. 2012 May 1;109(18):6790-1   [PMID:  22529392 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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