scholarly journals Analysis of Stromal Cell Secretomes Reveals a Critical Role for Stromal Cell–Derived Hepatocyte Growth Factor and Fibronectin in Angiogenesis

2013 ◽  
Vol 33 (3) ◽  
pp. 513-522 ◽  
Author(s):  
Andrew C. Newman ◽  
Wayne Chou ◽  
Katrina M. Welch-Reardon ◽  
Ashley H. Fong ◽  
Stephanie A. Popson ◽  
...  
2004 ◽  
Vol 89 (2) ◽  
pp. 823-832 ◽  
Author(s):  
Souichi Yoshida ◽  
Tasuku Harada ◽  
Masahiro Mitsunari ◽  
Tomio Iwabe ◽  
Yasuko Sakamoto ◽  
...  

2004 ◽  
Vol 32 (10) ◽  
pp. 955-961 ◽  
Author(s):  
Yoshiko Matsuda-Hashii ◽  
Kenji Takai ◽  
Hideaki Ohta ◽  
Hiroyuki Fujisaki ◽  
Sadao Tokimasa ◽  
...  

2016 ◽  
Vol 5 (10) ◽  
pp. 1307-1318 ◽  
Author(s):  
Emer F. Cahill ◽  
Helen Kennelly ◽  
Fiona Carty ◽  
Bernard P. Mahon ◽  
Karen English

2009 ◽  
Vol 20 (2) ◽  
pp. 642-657 ◽  
Author(s):  
Maria Cristina Stella ◽  
Livio Trusolino ◽  
Paolo M. Comoglio

The Slit protein acts through the Roundabout receptor as a paracrine chemorepellent in axon guidance and as an inhibitor in leukocyte chemotaxis, but its role in epithelial cell motility and morphogenesis remains largely unexplored. We report that nontransformed epithelial cells and cancerous cells empower the Slit-2/Robo1 signaling system to limit outward migration in response to motogenic attractants and to remain positionally confined within their primitive location. Short hairpin RNA-mediated depletion of SLIT-2 or ectopic expression of a soluble decoy Robo enhance hepatocyte growth factor (HGF)-induced migration, matrix invasion, and tubulogenesis, concomitantly with the up-regulation of Cdc-42 and the down-modulation of Rac-1 activities. Accordingly, autocrine overexpression or exogenous administration of Slit-2 prevent HGF-triggered motile responses, reduce Cdc-42 activation, and stimulate Rac-1. This antimigratory activity of Slit-2 derives from the inhibition of actin-based protrusive forces and from an increased adhesive strength of cadherin-mediated intercellular contacts. These results disclose a novel function for Slit and Robo in the inhibition of growth factor-mediated epithelial cell motility and morphogenesis, invoking a critical role for both molecules as natural antagonists of neoplastic invasive growth.


Author(s):  
Min Liu ◽  
Cai Yuan ◽  
Yunbin Jiang ◽  
Longguang Jiang ◽  
Mingdong Huang

Hepatocyte growth factor activator inhibitor 1 (HAI-1) is a multi-domain membrane-associated protease inhibitor that potently inhibits a variety of serine proteases such as hepatocyte growth factor activator and matriptase. Different truncates of HAI-1 show varying potencies for inhibition of target proteases, suggesting that the domain organization of HAI-1 plays a critical role in its function. Here, the soluble full-length extracellular part of HAI-1 (sHAI-1) was expressed using theDrosophilaS2 insect-cell expression system. Diffraction-quality crystals of sHAI-1 were produced using ammonium sulfate as precipitant. The crystal diffracted to 3.8 Å resolution and belonged to space groupP41212, with unit-cell parametersa=b= 95.42,c= 124.50 Å. The asymmetric unit contains one sHAI-1 molecule.


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